BindingDB Reactant_set_id Ligand SMILES Ligand InChI Ligand InChI Key BindingDB MonomerID BindingDB Ligand Name Target Name Target Source Organism According to Curator or DataSource Ki (nM) IC50 (nM) Kd (nM) EC50 (nM) kon (M-1-s-1) koff (s-1) pH Temp (C) Curation/DataSource Article DOI BindingDB Entry DOI PMID PubChem AID Patent Number Authors Date of publication Date in BindingDB Institution Link to Ligand in BindingDB Link to Target in BindingDB Link to Ligand-Target Pair in BindingDB Ligand HET ID in PDB PDB ID(s) for Ligand-Target Complex PubChem CID PubChem SID ChEBI ID of Ligand ChEMBL ID of Ligand DrugBank ID of Ligand IUPHAR_GRAC ID of Ligand KEGG ID of Ligand ZINC ID of Ligand Number of Protein Chains in Target (>1 implies a multichain complex) BindingDB Target Chain Sequence 1 PDB ID(s) of Target Chain 1 UniProt (SwissProt) Recommended Name of Target Chain 1 UniProt (SwissProt) Entry Name of Target Chain 1 UniProt (SwissProt) Primary ID of Target Chain 1 UniProt (SwissProt) Secondary ID(s) of Target Chain 1 UniProt (SwissProt) Alternative ID(s) of Target Chain 1 UniProt (TrEMBL) Submitted Name of Target Chain 1 UniProt (TrEMBL) Entry Name of Target Chain 1 UniProt (TrEMBL) Primary ID of Target Chain 1 UniProt (TrEMBL) Secondary ID(s) of Target Chain 1 UniProt (TrEMBL) Alternative ID(s) of Target Chain 1 BindingDB Target Chain Sequence 2 PDB ID(s) of Target Chain 2 UniProt (SwissProt) Recommended Name of Target Chain 2 UniProt (SwissProt) Entry Name of Target Chain 2 UniProt (SwissProt) Primary ID of Target Chain 2 UniProt (SwissProt) Secondary ID(s) of Target Chain 2 UniProt (SwissProt) Alternative ID(s) of Target Chain 2 UniProt (TrEMBL) Submitted Name of Target Chain 2 UniProt (TrEMBL) Entry Name of Target Chain 2 UniProt (TrEMBL) Primary ID of Target Chain 2 UniProt (TrEMBL) Secondary ID(s) of Target Chain 2 UniProt (TrEMBL) Alternative ID(s) of Target Chain 2 BindingDB Target Chain Sequence 3 PDB ID(s) of Target Chain 3 UniProt (SwissProt) Recommended Name of Target Chain 3 UniProt (SwissProt) Entry Name of Target Chain 3 UniProt (SwissProt) Primary ID of Target Chain 3 UniProt (SwissProt) Secondary ID(s) of Target Chain 3 UniProt (SwissProt) Alternative ID(s) of Target Chain 3 UniProt (TrEMBL) Submitted Name of Target Chain 3 UniProt (TrEMBL) Entry Name of Target Chain 3 UniProt (TrEMBL) Primary ID of Target Chain 3 UniProt (TrEMBL) Secondary ID(s) of Target Chain 3 UniProt (TrEMBL) Alternative ID(s) of Target Chain 3 BindingDB Target Chain Sequence 4 PDB ID(s) of Target Chain 4 UniProt (SwissProt) Recommended Name of Target Chain 4 UniProt (SwissProt) Entry Name of Target Chain 4 UniProt (SwissProt) Primary ID of Target Chain 4 UniProt (SwissProt) Secondary ID(s) of Target Chain 4 UniProt (SwissProt) Alternative ID(s) of Target Chain 4 UniProt (TrEMBL) Submitted Name of Target Chain 4 UniProt (TrEMBL) Entry Name of Target Chain 4 UniProt (TrEMBL) Primary ID of Target Chain 4 UniProt (TrEMBL) Secondary ID(s) of Target Chain 4 UniProt (TrEMBL) Alternative ID(s) of Target Chain 4 BindingDB Target Chain Sequence 5 PDB ID(s) of Target Chain 5 UniProt (SwissProt) Recommended Name of Target Chain 5 UniProt (SwissProt) Entry Name of Target Chain 5 UniProt (SwissProt) Primary ID of Target Chain 5 UniProt (SwissProt) Secondary ID(s) of Target Chain 5 UniProt (SwissProt) Alternative ID(s) of Target Chain 5 UniProt (TrEMBL) Submitted Name of Target Chain 5 UniProt (TrEMBL) Entry Name of Target Chain 5 UniProt (TrEMBL) Primary ID of Target Chain 5 UniProt (TrEMBL) Secondary ID(s) of Target Chain 5 UniProt (TrEMBL) Alternative ID(s) of Target Chain 5 BindingDB Target Chain Sequence 6 PDB ID(s) of Target Chain 6 UniProt (SwissProt) Recommended Name of Target Chain 6 UniProt (SwissProt) Entry Name of Target Chain 6 UniProt (SwissProt) Primary ID of Target Chain 6 UniProt (SwissProt) Secondary ID(s) of Target Chain 6 UniProt (SwissProt) Alternative ID(s) of Target Chain 6 UniProt (TrEMBL) Submitted Name of Target Chain 6 UniProt (TrEMBL) Entry Name of Target Chain 6 UniProt (TrEMBL) Primary ID of Target Chain 6 UniProt (TrEMBL) Secondary ID(s) of Target Chain 6 UniProt (TrEMBL) Alternative ID(s) of Target Chain 6 BindingDB Target Chain Sequence 7 PDB ID(s) of Target Chain 7 UniProt (SwissProt) Recommended Name of Target Chain 7 UniProt (SwissProt) Entry Name of Target Chain 7 UniProt (SwissProt) Primary ID of Target Chain 7 UniProt (SwissProt) Secondary ID(s) of Target Chain 7 UniProt (SwissProt) Alternative ID(s) of Target Chain 7 UniProt (TrEMBL) Submitted Name of Target Chain 7 UniProt (TrEMBL) Entry Name of Target Chain 7 UniProt (TrEMBL) Primary ID of Target Chain 7 UniProt (TrEMBL) Secondary ID(s) of Target Chain 7 UniProt (TrEMBL) Alternative ID(s) of Target Chain 7 BindingDB Target Chain Sequence 8 PDB ID(s) of Target Chain 8 UniProt (SwissProt) Recommended Name of Target Chain 8 UniProt (SwissProt) Entry Name of Target Chain 8 UniProt (SwissProt) Primary ID of Target Chain 8 UniProt (SwissProt) Secondary ID(s) of Target Chain 8 UniProt (SwissProt) Alternative ID(s) of Target Chain 8 UniProt (TrEMBL) Submitted Name of Target Chain 8 UniProt (TrEMBL) Entry Name of Target Chain 8 UniProt (TrEMBL) Primary ID of Target Chain 8 UniProt (TrEMBL) Secondary ID(s) of Target Chain 8 UniProt (TrEMBL) Alternative ID(s) of Target Chain 8 BindingDB Target Chain Sequence 9 PDB ID(s) of Target Chain 9 UniProt (SwissProt) Recommended Name of Target Chain 9 UniProt (SwissProt) Entry Name of Target Chain 9 UniProt (SwissProt) Primary ID of Target Chain 9 UniProt (SwissProt) Secondary ID(s) of Target Chain 9 UniProt (SwissProt) Alternative ID(s) of Target Chain 9 UniProt (TrEMBL) Submitted Name of Target Chain 9 UniProt (TrEMBL) Entry Name of Target Chain 9 UniProt (TrEMBL) Primary ID of Target Chain 9 UniProt (TrEMBL) Secondary ID(s) of Target Chain 9 UniProt (TrEMBL) Alternative ID(s) of Target Chain 9 BindingDB Target Chain Sequence 10 PDB ID(s) of Target Chain 10 UniProt (SwissProt) Recommended Name of Target Chain 10 UniProt (SwissProt) Entry Name of Target Chain 10 UniProt (SwissProt) Primary ID of Target Chain 10 UniProt (SwissProt) Secondary ID(s) of Target Chain 10 UniProt (SwissProt) Alternative ID(s) of Target Chain 10 UniProt (TrEMBL) Submitted Name of Target Chain 10 UniProt (TrEMBL) Entry Name of Target Chain 10 UniProt (TrEMBL) Primary ID of Target Chain 10 UniProt (TrEMBL) Secondary ID(s) of Target Chain 10 UniProt (TrEMBL) Alternative ID(s) of Target Chain 10 BindingDB Target Chain Sequence 11 PDB ID(s) of Target Chain 11 UniProt (SwissProt) Recommended Name of Target Chain 11 UniProt (SwissProt) Entry Name of Target Chain 11 UniProt (SwissProt) Primary ID of Target Chain 11 UniProt (SwissProt) Secondary ID(s) of Target Chain 11 UniProt (SwissProt) Alternative ID(s) of Target Chain 11 UniProt (TrEMBL) Submitted Name of Target Chain 11 UniProt (TrEMBL) Entry Name of Target Chain 11 UniProt (TrEMBL) Primary ID of Target Chain 11 UniProt (TrEMBL) Secondary ID(s) of Target Chain 11 UniProt (TrEMBL) Alternative ID(s) of Target Chain 11 BindingDB Target Chain Sequence 12 PDB ID(s) of Target Chain 12 UniProt (SwissProt) Recommended Name of Target Chain 12 UniProt (SwissProt) Entry Name of Target Chain 12 UniProt (SwissProt) Primary ID of Target Chain 12 UniProt (SwissProt) Secondary ID(s) of Target Chain 12 UniProt (SwissProt) Alternative ID(s) of Target Chain 12 UniProt (TrEMBL) Submitted Name of Target Chain 12 UniProt (TrEMBL) Entry Name of Target Chain 12 UniProt (TrEMBL) Primary ID of Target Chain 12 UniProt (TrEMBL) Secondary ID(s) of Target Chain 12 UniProt (TrEMBL) Alternative ID(s) of Target Chain 12 BindingDB Target Chain Sequence 13 PDB ID(s) of Target Chain 13 UniProt (SwissProt) Recommended Name of Target Chain 13 UniProt (SwissProt) Entry Name of Target Chain 13 UniProt (SwissProt) Primary ID of Target Chain 13 UniProt (SwissProt) Secondary ID(s) of Target Chain 13 UniProt (SwissProt) Alternative ID(s) of Target Chain 13 UniProt (TrEMBL) Submitted Name of Target Chain 13 UniProt (TrEMBL) Entry Name of Target Chain 13 UniProt (TrEMBL) Primary ID of Target Chain 13 UniProt (TrEMBL) Secondary ID(s) of Target Chain 13 UniProt (TrEMBL) Alternative ID(s) of Target Chain 13 BindingDB Target Chain Sequence 14 PDB ID(s) of Target Chain 14 UniProt (SwissProt) Recommended Name of Target Chain 14 UniProt (SwissProt) Entry Name of Target Chain 14 UniProt (SwissProt) Primary ID of Target Chain 14 UniProt (SwissProt) Secondary ID(s) of Target Chain 14 UniProt (SwissProt) Alternative ID(s) of Target Chain 14 UniProt (TrEMBL) Submitted Name of Target Chain 14 UniProt (TrEMBL) Entry Name of Target Chain 14 UniProt (TrEMBL) Primary ID of Target Chain 14 UniProt (TrEMBL) Secondary ID(s) of Target Chain 14 UniProt (TrEMBL) Alternative ID(s) of Target Chain 14 BindingDB Target Chain Sequence 15 PDB ID(s) of Target Chain 15 UniProt (SwissProt) Recommended Name of Target Chain 15 UniProt (SwissProt) Entry Name of Target Chain 15 UniProt (SwissProt) Primary ID of Target Chain 15 UniProt (SwissProt) Secondary ID(s) of Target Chain 15 UniProt (SwissProt) Alternative ID(s) of Target Chain 15 UniProt (TrEMBL) Submitted Name of Target Chain 15 UniProt (TrEMBL) Entry Name of Target Chain 15 UniProt (TrEMBL) Primary ID of Target Chain 15 UniProt (TrEMBL) Secondary ID(s) of Target Chain 15 UniProt (TrEMBL) Alternative ID(s) of Target Chain 15 BindingDB Target Chain Sequence 16 PDB ID(s) of Target Chain 16 UniProt (SwissProt) Recommended Name of Target Chain 16 UniProt (SwissProt) Entry Name of Target Chain 16 UniProt (SwissProt) Primary ID of Target Chain 16 UniProt (SwissProt) Secondary ID(s) of Target Chain 16 UniProt (SwissProt) Alternative ID(s) of Target Chain 16 UniProt (TrEMBL) Submitted Name of Target Chain 16 UniProt (TrEMBL) Entry Name of Target Chain 16 UniProt (TrEMBL) Primary ID of Target Chain 16 UniProt (TrEMBL) Secondary ID(s) of Target Chain 16 UniProt (TrEMBL) Alternative ID(s) of Target Chain 16 BindingDB Target Chain Sequence 17 PDB ID(s) of Target Chain 17 UniProt (SwissProt) Recommended Name of Target Chain 17 UniProt (SwissProt) Entry Name of Target Chain 17 UniProt (SwissProt) Primary ID of Target Chain 17 UniProt (SwissProt) Secondary ID(s) of Target Chain 17 UniProt (SwissProt) Alternative ID(s) of Target Chain 17 UniProt (TrEMBL) Submitted Name of Target Chain 17 UniProt (TrEMBL) Entry Name of Target Chain 17 UniProt (TrEMBL) Primary ID of Target Chain 17 UniProt (TrEMBL) Secondary ID(s) of Target Chain 17 UniProt (TrEMBL) Alternative ID(s) of Target Chain 17 BindingDB Target Chain Sequence 18 PDB ID(s) of Target Chain 18 UniProt (SwissProt) Recommended Name of Target Chain 18 UniProt (SwissProt) Entry Name of Target Chain 18 UniProt (SwissProt) Primary ID of Target Chain 18 UniProt (SwissProt) Secondary ID(s) of Target Chain 18 UniProt (SwissProt) Alternative ID(s) of Target Chain 18 UniProt (TrEMBL) Submitted Name of Target Chain 18 UniProt (TrEMBL) Entry Name of Target Chain 18 UniProt (TrEMBL) Primary ID of Target Chain 18 UniProt (TrEMBL) Secondary ID(s) of Target Chain 18 UniProt (TrEMBL) Alternative ID(s) of Target Chain 18 BindingDB Target Chain Sequence 19 PDB ID(s) of Target Chain 19 UniProt (SwissProt) Recommended Name of Target Chain 19 UniProt (SwissProt) Entry Name of Target Chain 19 UniProt (SwissProt) Primary ID of Target Chain 19 UniProt (SwissProt) Secondary ID(s) of Target Chain 19 UniProt (SwissProt) Alternative ID(s) of Target Chain 19 UniProt (TrEMBL) Submitted Name of Target Chain 19 UniProt (TrEMBL) Entry Name of Target Chain 19 UniProt (TrEMBL) Primary ID of Target Chain 19 UniProt (TrEMBL) Secondary ID(s) of Target Chain 19 UniProt (TrEMBL) Alternative ID(s) of Target Chain 19 BindingDB Target Chain Sequence 20 PDB ID(s) of Target Chain 20 UniProt (SwissProt) Recommended Name of Target Chain 20 UniProt (SwissProt) Entry Name of Target Chain 20 UniProt (SwissProt) Primary ID of Target Chain 20 UniProt (SwissProt) Secondary ID(s) of Target Chain 20 UniProt (SwissProt) Alternative ID(s) of Target Chain 20 UniProt (TrEMBL) Submitted Name of Target Chain 20 UniProt (TrEMBL) Entry Name of Target Chain 20 UniProt (TrEMBL) Primary ID of Target Chain 20 UniProt (TrEMBL) Secondary ID(s) of Target Chain 20 UniProt (TrEMBL) Alternative ID(s) of Target Chain 20 BindingDB Target Chain Sequence 21 PDB ID(s) of Target Chain 21 UniProt (SwissProt) Recommended Name of Target Chain 21 UniProt (SwissProt) Entry Name of Target Chain 21 UniProt (SwissProt) Primary ID of Target Chain 21 UniProt (SwissProt) Secondary ID(s) of Target Chain 21 UniProt (SwissProt) Alternative ID(s) of Target Chain 21 UniProt (TrEMBL) Submitted Name of Target Chain 21 UniProt (TrEMBL) Entry Name of Target Chain 21 UniProt (TrEMBL) Primary ID of Target Chain 21 UniProt (TrEMBL) Secondary ID(s) of Target Chain 21 UniProt (TrEMBL) Alternative ID(s) of Target Chain 21 BindingDB Target Chain Sequence 22 PDB ID(s) of Target Chain 22 UniProt (SwissProt) Recommended Name of Target Chain 22 UniProt (SwissProt) Entry Name of Target Chain 22 UniProt (SwissProt) Primary ID of Target Chain 22 UniProt (SwissProt) Secondary ID(s) of Target Chain 22 UniProt (SwissProt) Alternative ID(s) of Target Chain 22 UniProt (TrEMBL) Submitted Name of Target Chain 22 UniProt (TrEMBL) Entry Name of Target Chain 22 UniProt (TrEMBL) Primary ID of Target Chain 22 UniProt (TrEMBL) Secondary ID(s) of Target Chain 22 UniProt (TrEMBL) Alternative ID(s) of Target Chain 22 BindingDB Target Chain Sequence 23 PDB ID(s) of Target Chain 23 UniProt (SwissProt) Recommended Name of Target Chain 23 UniProt (SwissProt) Entry Name of Target Chain 23 UniProt (SwissProt) Primary ID of Target Chain 23 UniProt (SwissProt) Secondary ID(s) of Target Chain 23 UniProt (SwissProt) Alternative ID(s) of Target Chain 23 UniProt (TrEMBL) Submitted Name of Target Chain 23 UniProt (TrEMBL) Entry Name of Target Chain 23 UniProt (TrEMBL) Primary ID of Target Chain 23 UniProt (TrEMBL) Secondary ID(s) of Target Chain 23 UniProt (TrEMBL) Alternative ID(s) of Target Chain 23 BindingDB Target Chain Sequence 24 PDB ID(s) of Target Chain 24 UniProt (SwissProt) Recommended Name of Target Chain 24 UniProt (SwissProt) Entry Name of Target Chain 24 UniProt (SwissProt) Primary ID of Target Chain 24 UniProt (SwissProt) Secondary ID(s) of Target Chain 24 UniProt (SwissProt) Alternative ID(s) of Target Chain 24 UniProt (TrEMBL) Submitted Name of Target Chain 24 UniProt (TrEMBL) Entry Name of Target Chain 24 UniProt (TrEMBL) Primary ID of Target Chain 24 UniProt (TrEMBL) Secondary ID(s) of Target Chain 24 UniProt (TrEMBL) Alternative ID(s) of Target Chain 24 BindingDB Target Chain Sequence 25 PDB ID(s) of Target Chain 25 UniProt (SwissProt) Recommended Name of Target Chain 25 UniProt (SwissProt) Entry Name of Target Chain 25 UniProt (SwissProt) Primary ID of Target Chain 25 UniProt (SwissProt) Secondary ID(s) of Target Chain 25 UniProt (SwissProt) Alternative ID(s) of Target Chain 25 UniProt (TrEMBL) Submitted Name of Target Chain 25 UniProt (TrEMBL) Entry Name of Target Chain 25 UniProt (TrEMBL) Primary ID of Target Chain 25 UniProt (TrEMBL) Secondary ID(s) of Target Chain 25 UniProt (TrEMBL) Alternative ID(s) of Target Chain 25 BindingDB Target Chain Sequence 26 PDB ID(s) of Target Chain 26 UniProt (SwissProt) Recommended Name of Target Chain 26 UniProt (SwissProt) Entry Name of Target Chain 26 UniProt (SwissProt) Primary ID of Target Chain 26 UniProt (SwissProt) Secondary ID(s) of Target Chain 26 UniProt (SwissProt) Alternative ID(s) of Target Chain 26 UniProt (TrEMBL) Submitted Name of Target Chain 26 UniProt (TrEMBL) Entry Name of Target Chain 26 UniProt (TrEMBL) Primary ID of Target Chain 26 UniProt (TrEMBL) Secondary ID(s) of Target Chain 26 UniProt (TrEMBL) Alternative ID(s) of Target Chain 26 BindingDB Target Chain Sequence 27 PDB ID(s) of Target Chain 27 UniProt (SwissProt) Recommended Name of Target Chain 27 UniProt (SwissProt) Entry Name of Target Chain 27 UniProt (SwissProt) Primary ID of Target Chain 27 UniProt (SwissProt) Secondary ID(s) of Target Chain 27 UniProt (SwissProt) Alternative ID(s) of Target Chain 27 UniProt (TrEMBL) Submitted Name of Target Chain 27 UniProt (TrEMBL) Entry Name of Target Chain 27 UniProt (TrEMBL) Primary ID of Target Chain 27 UniProt (TrEMBL) Secondary ID(s) of Target Chain 27 UniProt (TrEMBL) Alternative ID(s) of Target Chain 27 BindingDB Target Chain Sequence 28 PDB ID(s) of Target Chain 28 UniProt (SwissProt) Recommended Name of Target Chain 28 UniProt (SwissProt) Entry Name of Target Chain 28 UniProt (SwissProt) Primary ID of Target Chain 28 UniProt (SwissProt) Secondary ID(s) of Target Chain 28 UniProt (SwissProt) Alternative ID(s) of Target Chain 28 UniProt (TrEMBL) Submitted Name of Target Chain 28 UniProt (TrEMBL) Entry Name of Target Chain 28 UniProt (TrEMBL) Primary ID of Target Chain 28 UniProt (TrEMBL) Secondary ID(s) of Target Chain 28 UniProt (TrEMBL) Alternative ID(s) of Target Chain 28 BindingDB Target Chain Sequence 29 PDB ID(s) of Target Chain 29 UniProt (SwissProt) Recommended Name of Target Chain 29 UniProt (SwissProt) Entry Name of Target Chain 29 UniProt (SwissProt) Primary ID of Target Chain 29 UniProt (SwissProt) Secondary ID(s) of Target Chain 29 UniProt (SwissProt) Alternative ID(s) of Target Chain 29 UniProt (TrEMBL) Submitted Name of Target Chain 29 UniProt (TrEMBL) Entry Name of Target Chain 29 UniProt (TrEMBL) Primary ID of Target Chain 29 UniProt (TrEMBL) Secondary ID(s) of Target Chain 29 UniProt (TrEMBL) Alternative ID(s) of Target Chain 29 BindingDB Target Chain Sequence 30 PDB ID(s) of Target Chain 30 UniProt (SwissProt) Recommended Name of Target Chain 30 UniProt (SwissProt) Entry Name of Target Chain 30 UniProt (SwissProt) Primary ID of Target Chain 30 UniProt (SwissProt) Secondary ID(s) of Target Chain 30 UniProt (SwissProt) Alternative ID(s) of Target Chain 30 UniProt (TrEMBL) Submitted Name of Target Chain 30 UniProt (TrEMBL) Entry Name of Target Chain 30 UniProt (TrEMBL) Primary ID of Target Chain 30 UniProt (TrEMBL) Secondary ID(s) of Target Chain 30 UniProt (TrEMBL) Alternative ID(s) of Target Chain 30 BindingDB Target Chain Sequence 31 PDB ID(s) of Target Chain 31 UniProt (SwissProt) Recommended Name of Target Chain 31 UniProt (SwissProt) Entry Name of Target Chain 31 UniProt (SwissProt) Primary ID of Target Chain 31 UniProt (SwissProt) Secondary ID(s) of Target Chain 31 UniProt (SwissProt) Alternative ID(s) of Target Chain 31 UniProt (TrEMBL) Submitted Name of Target Chain 31 UniProt (TrEMBL) Entry Name of Target Chain 31 UniProt (TrEMBL) Primary ID of Target Chain 31 UniProt (TrEMBL) Secondary ID(s) of Target Chain 31 UniProt (TrEMBL) Alternative ID(s) of Target Chain 31 BindingDB Target Chain Sequence 32 PDB ID(s) of Target Chain 32 UniProt (SwissProt) Recommended Name of Target Chain 32 UniProt (SwissProt) Entry Name of Target Chain 32 UniProt (SwissProt) Primary ID of Target Chain 32 UniProt (SwissProt) Secondary ID(s) of Target Chain 32 UniProt (SwissProt) Alternative ID(s) of Target Chain 32 UniProt (TrEMBL) Submitted Name of Target Chain 32 UniProt (TrEMBL) Entry Name of Target Chain 32 UniProt (TrEMBL) Primary ID of Target Chain 32 UniProt (TrEMBL) Secondary ID(s) of Target Chain 32 UniProt (TrEMBL) Alternative ID(s) of Target Chain 32 BindingDB Target Chain Sequence 33 PDB ID(s) of Target Chain 33 UniProt (SwissProt) Recommended Name of Target Chain 33 UniProt (SwissProt) Entry Name of Target Chain 33 UniProt (SwissProt) Primary ID of Target Chain 33 UniProt (SwissProt) Secondary ID(s) of Target Chain 33 UniProt (SwissProt) Alternative ID(s) of Target Chain 33 UniProt (TrEMBL) Submitted Name of Target Chain 33 UniProt (TrEMBL) Entry Name of Target Chain 33 UniProt (TrEMBL) Primary ID of Target Chain 33 UniProt (TrEMBL) Secondary ID(s) of Target Chain 33 UniProt (TrEMBL) Alternative ID(s) of Target Chain 33 BindingDB Target Chain Sequence 34 PDB ID(s) of Target Chain 34 UniProt (SwissProt) Recommended Name of Target Chain 34 UniProt (SwissProt) Entry Name of Target Chain 34 UniProt (SwissProt) Primary ID of Target Chain 34 UniProt (SwissProt) Secondary ID(s) of Target Chain 34 UniProt (SwissProt) Alternative ID(s) of Target Chain 34 UniProt (TrEMBL) Submitted Name of Target Chain 34 UniProt (TrEMBL) Entry Name of Target Chain 34 UniProt (TrEMBL) Primary ID of Target Chain 34 UniProt (TrEMBL) Secondary ID(s) of Target Chain 34 UniProt (TrEMBL) Alternative ID(s) of Target Chain 34 BindingDB Target Chain Sequence 35 PDB ID(s) of Target Chain 35 UniProt (SwissProt) Recommended Name of Target Chain 35 UniProt (SwissProt) Entry Name of Target Chain 35 UniProt (SwissProt) Primary ID of Target Chain 35 UniProt (SwissProt) Secondary ID(s) of Target Chain 35 UniProt (SwissProt) Alternative ID(s) of Target Chain 35 UniProt (TrEMBL) Submitted Name of Target Chain 35 UniProt (TrEMBL) Entry Name of Target Chain 35 UniProt (TrEMBL) Primary ID of Target Chain 35 UniProt (TrEMBL) Secondary ID(s) of Target Chain 35 UniProt (TrEMBL) Alternative ID(s) of Target Chain 35 BindingDB Target Chain Sequence 36 PDB ID(s) of Target Chain 36 UniProt (SwissProt) Recommended Name of Target Chain 36 UniProt (SwissProt) Entry Name of Target Chain 36 UniProt (SwissProt) Primary ID of Target Chain 36 UniProt (SwissProt) Secondary ID(s) of Target Chain 36 UniProt (SwissProt) Alternative ID(s) of Target Chain 36 UniProt (TrEMBL) Submitted Name of Target Chain 36 UniProt (TrEMBL) Entry Name of Target Chain 36 UniProt (TrEMBL) Primary ID of Target Chain 36 UniProt (TrEMBL) Secondary ID(s) of Target Chain 36 UniProt (TrEMBL) Alternative ID(s) of Target Chain 36 BindingDB Target Chain Sequence 37 PDB ID(s) of Target Chain 37 UniProt (SwissProt) Recommended Name of Target Chain 37 UniProt (SwissProt) Entry Name of Target Chain 37 UniProt (SwissProt) Primary ID of Target Chain 37 UniProt (SwissProt) Secondary ID(s) of Target Chain 37 UniProt (SwissProt) Alternative ID(s) of Target Chain 37 UniProt (TrEMBL) Submitted Name of Target Chain 37 UniProt (TrEMBL) Entry Name of Target Chain 37 UniProt (TrEMBL) Primary ID of Target Chain 37 UniProt (TrEMBL) Secondary ID(s) of Target Chain 37 UniProt (TrEMBL) Alternative ID(s) of Target Chain 37 BindingDB Target Chain Sequence 38 PDB ID(s) of Target Chain 38 UniProt (SwissProt) Recommended Name of Target Chain 38 UniProt (SwissProt) Entry Name of Target Chain 38 UniProt (SwissProt) Primary ID of Target Chain 38 UniProt (SwissProt) Secondary ID(s) of Target Chain 38 UniProt (SwissProt) Alternative ID(s) of Target Chain 38 UniProt (TrEMBL) Submitted Name of Target Chain 38 UniProt (TrEMBL) Entry Name of Target Chain 38 UniProt (TrEMBL) Primary ID of Target Chain 38 UniProt (TrEMBL) Secondary ID(s) of Target Chain 38 UniProt (TrEMBL) Alternative ID(s) of Target Chain 38 BindingDB Target Chain Sequence 39 PDB ID(s) of Target Chain 39 UniProt (SwissProt) Recommended Name of Target Chain 39 UniProt (SwissProt) Entry Name of Target Chain 39 UniProt (SwissProt) Primary ID of Target Chain 39 UniProt (SwissProt) Secondary ID(s) of Target Chain 39 UniProt (SwissProt) Alternative ID(s) of Target Chain 39 UniProt (TrEMBL) Submitted Name of Target Chain 39 UniProt (TrEMBL) Entry Name of Target Chain 39 UniProt (TrEMBL) Primary ID of Target Chain 39 UniProt (TrEMBL) Secondary ID(s) of Target Chain 39 UniProt (TrEMBL) Alternative ID(s) of Target Chain 39 BindingDB Target Chain Sequence 40 PDB ID(s) of Target Chain 40 UniProt (SwissProt) Recommended Name of Target Chain 40 UniProt (SwissProt) Entry Name of Target Chain 40 UniProt (SwissProt) Primary ID of Target Chain 40 UniProt (SwissProt) Secondary ID(s) of Target Chain 40 UniProt (SwissProt) Alternative ID(s) of Target Chain 40 UniProt (TrEMBL) Submitted Name of Target Chain 40 UniProt (TrEMBL) Entry Name of Target Chain 40 UniProt (TrEMBL) Primary ID of Target Chain 40 UniProt (TrEMBL) Secondary ID(s) of Target Chain 40 UniProt (TrEMBL) Alternative ID(s) of Target Chain 40 BindingDB Target Chain Sequence 41 PDB ID(s) of Target Chain 41 UniProt (SwissProt) Recommended Name of Target Chain 41 UniProt (SwissProt) Entry Name of Target Chain 41 UniProt (SwissProt) Primary ID of Target Chain 41 UniProt (SwissProt) Secondary ID(s) of Target Chain 41 UniProt (SwissProt) Alternative ID(s) of Target Chain 41 UniProt (TrEMBL) Submitted Name of Target Chain 41 UniProt (TrEMBL) Entry Name of Target Chain 41 UniProt (TrEMBL) Primary ID of Target Chain 41 UniProt (TrEMBL) Secondary ID(s) of Target Chain 41 UniProt (TrEMBL) Alternative ID(s) of Target Chain 41 BindingDB Target Chain Sequence 42 PDB ID(s) of Target Chain 42 UniProt (SwissProt) Recommended Name of Target Chain 42 UniProt (SwissProt) Entry Name of Target Chain 42 UniProt (SwissProt) Primary ID of Target Chain 42 UniProt (SwissProt) Secondary ID(s) of Target Chain 42 UniProt (SwissProt) Alternative ID(s) of Target Chain 42 UniProt (TrEMBL) Submitted Name of Target Chain 42 UniProt (TrEMBL) Entry Name of Target Chain 42 UniProt (TrEMBL) Primary ID of Target Chain 42 UniProt (TrEMBL) Secondary ID(s) of Target Chain 42 UniProt (TrEMBL) Alternative ID(s) of Target Chain 42 BindingDB Target Chain Sequence 43 PDB ID(s) of Target Chain 43 UniProt (SwissProt) Recommended Name of Target Chain 43 UniProt (SwissProt) Entry Name of Target Chain 43 UniProt (SwissProt) Primary ID of Target Chain 43 UniProt (SwissProt) Secondary ID(s) of Target Chain 43 UniProt (SwissProt) Alternative ID(s) of Target Chain 43 UniProt (TrEMBL) Submitted Name of Target Chain 43 UniProt (TrEMBL) Entry Name of Target Chain 43 UniProt (TrEMBL) Primary ID of Target Chain 43 UniProt (TrEMBL) Secondary ID(s) of Target Chain 43 UniProt (TrEMBL) Alternative ID(s) of Target Chain 43 BindingDB Target Chain Sequence 44 PDB ID(s) of Target Chain 44 UniProt (SwissProt) Recommended Name of Target Chain 44 UniProt (SwissProt) Entry Name of Target Chain 44 UniProt (SwissProt) Primary ID of Target Chain 44 UniProt (SwissProt) Secondary ID(s) of Target Chain 44 UniProt (SwissProt) Alternative ID(s) of Target Chain 44 UniProt (TrEMBL) Submitted Name of Target Chain 44 UniProt (TrEMBL) Entry Name of Target Chain 44 UniProt (TrEMBL) Primary ID of Target Chain 44 UniProt (TrEMBL) Secondary ID(s) of Target Chain 44 UniProt (TrEMBL) Alternative ID(s) of Target Chain 44 BindingDB Target Chain Sequence 45 PDB ID(s) of Target Chain 45 UniProt (SwissProt) Recommended Name of Target Chain 45 UniProt (SwissProt) Entry Name of Target Chain 45 UniProt (SwissProt) Primary ID of Target Chain 45 UniProt (SwissProt) Secondary ID(s) of Target Chain 45 UniProt (SwissProt) Alternative ID(s) of Target Chain 45 UniProt (TrEMBL) Submitted Name of Target Chain 45 UniProt (TrEMBL) Entry Name of Target Chain 45 UniProt (TrEMBL) Primary ID of Target Chain 45 UniProt (TrEMBL) Secondary ID(s) of Target Chain 45 UniProt (TrEMBL) Alternative ID(s) of Target Chain 45 BindingDB Target Chain Sequence 46 PDB ID(s) of Target Chain 46 UniProt (SwissProt) Recommended Name of Target Chain 46 UniProt (SwissProt) Entry Name of Target Chain 46 UniProt (SwissProt) Primary ID of Target Chain 46 UniProt (SwissProt) Secondary ID(s) of Target Chain 46 UniProt (SwissProt) Alternative ID(s) of Target Chain 46 UniProt (TrEMBL) Submitted Name of Target Chain 46 UniProt (TrEMBL) Entry Name of Target Chain 46 UniProt (TrEMBL) Primary ID of Target Chain 46 UniProt (TrEMBL) Secondary ID(s) of Target Chain 46 UniProt (TrEMBL) Alternative ID(s) of Target Chain 46 BindingDB Target Chain Sequence 47 PDB ID(s) of Target Chain 47 UniProt (SwissProt) Recommended Name of Target Chain 47 UniProt (SwissProt) Entry Name of Target Chain 47 UniProt (SwissProt) Primary ID of Target Chain 47 UniProt (SwissProt) Secondary ID(s) of Target Chain 47 UniProt (SwissProt) Alternative ID(s) of Target Chain 47 UniProt (TrEMBL) Submitted Name of Target Chain 47 UniProt (TrEMBL) Entry Name of Target Chain 47 UniProt (TrEMBL) Primary ID of Target Chain 47 UniProt (TrEMBL) Secondary ID(s) of Target Chain 47 UniProt (TrEMBL) Alternative ID(s) of Target Chain 47 BindingDB Target Chain Sequence 48 PDB ID(s) of Target Chain 48 UniProt (SwissProt) Recommended Name of Target Chain 48 UniProt (SwissProt) Entry Name of Target Chain 48 UniProt (SwissProt) Primary ID of Target Chain 48 UniProt (SwissProt) Secondary ID(s) of Target Chain 48 UniProt (SwissProt) Alternative ID(s) of Target Chain 48 UniProt (TrEMBL) Submitted Name of Target Chain 48 UniProt (TrEMBL) Entry Name of Target Chain 48 UniProt (TrEMBL) Primary ID of Target Chain 48 UniProt (TrEMBL) Secondary ID(s) of Target Chain 48 UniProt (TrEMBL) Alternative ID(s) of Target Chain 48 BindingDB Target Chain Sequence 49 PDB ID(s) of Target Chain 49 UniProt (SwissProt) Recommended Name of Target Chain 49 UniProt (SwissProt) Entry Name of Target Chain 49 UniProt (SwissProt) Primary ID of Target Chain 49 UniProt (SwissProt) Secondary ID(s) of Target Chain 49 UniProt (SwissProt) Alternative ID(s) of Target Chain 49 UniProt (TrEMBL) Submitted Name of Target Chain 49 UniProt (TrEMBL) Entry Name of Target Chain 49 UniProt (TrEMBL) Primary ID of Target Chain 49 UniProt (TrEMBL) Secondary ID(s) of Target Chain 49 UniProt (TrEMBL) Alternative ID(s) of Target Chain 49 BindingDB Target Chain Sequence 50 PDB ID(s) of Target Chain 50 UniProt (SwissProt) Recommended Name of Target Chain 50 UniProt (SwissProt) Entry Name of Target Chain 50 UniProt (SwissProt) Primary ID of Target Chain 50 UniProt (SwissProt) Secondary ID(s) of Target Chain 50 UniProt (SwissProt) Alternative ID(s) of Target Chain 50 UniProt (TrEMBL) Submitted Name of Target Chain 50 UniProt (TrEMBL) Entry Name of Target Chain 50 UniProt (TrEMBL) Primary ID of Target Chain 50 UniProt (TrEMBL) Secondary ID(s) of Target Chain 50 UniProt (TrEMBL) Alternative ID(s) of Target Chain 50 50042816 O=C1NC(=O)C2=C1c1cn(CCO[C@H](CNS(=O)(=O)c3ccccc3)CCn3cc2c2ccccc32)c2ccccc12 |c:5| InChI=1S/C32H28N4O5S/c37-31-29-25-19-35(27-12-6-4-10-23(25)27)15-14-21(18-33-42(39,40)22-8-2-1-3-9-22)41-17-16-36-20-26(30(29)32(38)34-31)24-11-5-7-13-28(24)36/h1-13,19-21,33H,14-18H2,(H,34,37,38) ADVDNJCNXOTAHZ-UHFFFAOYSA-N 50052036 3,5-dioxo-17-phenylsulfonamidomethyl-(17S)-18-oxa-4,14,21-triazahexacyclo[19.6.1.17,14.02,6.08,13.022,27]nonacosa-1(28),2(6),7(29),8(13),9,11,22(27),23,25-nonaene::CHEMBL315389 Protein kinase C alpha type Homo sapiens >5000 ChEMBL 10.1021/jm950588y 10.7270/Q25H7FBV 8709095 Jirousek, MR; Gillig, JR; Gonzalez, CM; Heath, WF; McDonald, JH; Neel, DA; Rito, CJ; Singh, U; Stramm, LE; Melikian-Badalian, A; Baevsky, M; Ballas, LM; Hall, SE; Winneroski, LL; Faul, MM 9/10/1996 11/10/2009 Eli Lilly http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50052036 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=599&target=Protein+kinase+C+alpha+type&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50052036&enzyme=Protein+kinase+C+alpha+type&column=ki&startPg=0&Increment=50&submit=Search 10650891 103948961 CHEMBL315389 1 MADVFPGNDSTASQDVANRFARKGALRQKNVHEVKDHKFIARFFKQPTFCSHCTDFIWGFGKQGFQCQVCCFVVHKRCHEFVTFSCPGADKGPDTDDPRSKHKFKIHTYGSPTFCDHCGSLLYGLIHQGMKCDTCDMNVHKQCVINVPSLCGMDHTEKRGRIYLKAEVADEKLHVTVRDAKNLIPMDPNGLSDPYVKLKLIPDPKNESKQKTKTIRSTLNPQWNESFTFKLKPSDKDRRLSVEIWDWDRTTRNDFMGSLSFGVSELMKMPASGWYKLLNQEEGEYYNVPIPEGDEEGNMELRQKFEKAKLGPAGNKVISPSEDRKQPSNNLDRVKLTDFNFLMVLGKGSFGKVMLADRKGTEELYAIKILKKDVVIQDDDVECTMVEKRVLALLDKPPFLTQLHSCFQTVDRLYFVMEYVNGGDLMYHIQQVGKFKEPQAVFYAAEISIGLFFLHKRGIIYRDLKLDNVMLDSEGHIKIADFGMCKEHMMDGVTTRTFCGTPDYIAPEIIAYQPYGKSVDWWAYGVLLYEMLAGQPPFDGEDEDELFQSIMEHNVSYPKSLSKEAVSVCKGLMTKHPAKRLGCGPEGERDVREHAFFRRIDWEKLENREIQPPFKPKVCGKGAENFDKFFTRGQPVLTPPDQLVIANIDQSDFEGFSYVNPQFVHPILQSAV 4RA4,4DNL Protein kinase C alpha type KPCA_HUMAN P17252 B5BU22 Q15137 Q32M72 Q96RE4 50042817 NC[C@@H]1CCn2cc(C3=C(C(=O)NC3=O)c3cn(CCO1)c1ccccc31)c1ccccc21 |t:8| InChI=1S/C26H24N4O3/c27-13-16-9-10-29-14-19(17-5-1-3-7-21(17)29)23-24(26(32)28-25(23)31)20-15-30(11-12-33-16)22-8-4-2-6-18(20)22/h1-8,14-16H,9-13,27H2,(H,28,31,32) JPLUPRIZLHXUPQ-UHFFFAOYSA-N 50052037 18-aminomethyl-(18S)-17-oxa-4,14,21-triazahexacyclo[19.6.1.17,14.02,6.08,13.022,27]nonacosa-1(28),2(6),7(29),8(13),9,11,22(27),23,25-nonaene-3,5-dione::CHEMBL316239 Protein kinase C alpha type Homo sapiens 1100 ChEMBL 10.1021/jm950588y 10.7270/Q25H7FBV 8709095 Jirousek, MR; Gillig, JR; Gonzalez, CM; Heath, WF; McDonald, JH; Neel, DA; Rito, CJ; Singh, U; Stramm, LE; Melikian-Badalian, A; Baevsky, M; Ballas, LM; Hall, SE; Winneroski, LL; Faul, MM 9/10/1996 11/10/2009 Eli Lilly http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50052037 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=599&target=Protein+kinase+C+alpha+type&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50052037&enzyme=Protein+kinase+C+alpha+type&column=ki&startPg=0&Increment=50&submit=Search 10527068 103948962 CHEMBL316239 1 MADVFPGNDSTASQDVANRFARKGALRQKNVHEVKDHKFIARFFKQPTFCSHCTDFIWGFGKQGFQCQVCCFVVHKRCHEFVTFSCPGADKGPDTDDPRSKHKFKIHTYGSPTFCDHCGSLLYGLIHQGMKCDTCDMNVHKQCVINVPSLCGMDHTEKRGRIYLKAEVADEKLHVTVRDAKNLIPMDPNGLSDPYVKLKLIPDPKNESKQKTKTIRSTLNPQWNESFTFKLKPSDKDRRLSVEIWDWDRTTRNDFMGSLSFGVSELMKMPASGWYKLLNQEEGEYYNVPIPEGDEEGNMELRQKFEKAKLGPAGNKVISPSEDRKQPSNNLDRVKLTDFNFLMVLGKGSFGKVMLADRKGTEELYAIKILKKDVVIQDDDVECTMVEKRVLALLDKPPFLTQLHSCFQTVDRLYFVMEYVNGGDLMYHIQQVGKFKEPQAVFYAAEISIGLFFLHKRGIIYRDLKLDNVMLDSEGHIKIADFGMCKEHMMDGVTTRTFCGTPDYIAPEIIAYQPYGKSVDWWAYGVLLYEMLAGQPPFDGEDEDELFQSIMEHNVSYPKSLSKEAVSVCKGLMTKHPAKRLGCGPEGERDVREHAFFRRIDWEKLENREIQPPFKPKVCGKGAENFDKFFTRGQPVLTPPDQLVIANIDQSDFEGFSYVNPQFVHPILQSAV 4RA4,4DNL Protein kinase C alpha type KPCA_HUMAN P17252 B5BU22 Q15137 Q32M72 Q96RE4 50042818 C[C@@]12[C@@H]([C@@H](C[C@@H](O1)n3c4ccccc4c5c3c6n2c7ccccc7c6c8c5C(=O)NC8)NC)OC InChI=1S/C28H26N4O3/c1-28-26(34-3)17(29-2)12-20(35-28)31-18-10-6-4-8-14(18)22-23-16(13-30-27(23)33)21-15-9-5-7-11-19(15)32(28)25(21)24(22)31/h4-11,17,20,26,29H,12-13H2,1-3H3,(H,30,33) HKSZLNNOFSGOKW-UHFFFAOYSA-N 2579 CHEMBL388978::Staurosporine, 8::Staurosporin, 4::(2S,3R,4R,6R)-3-methoxy-2-methyl-4-(methylamino)-29-oxa-1,7,17-triazaoctacyclo[12.12.2.1^{2,6}.0^{7,28}.0^{8,13}.0^{15,19}.0^{20,27}.0^{21,26}]nonacosa-8(13),9,11,14(28),15(19),20(27),21(26),22,24-nonaen-16-one::Staurosporine::US9206188, Staurosporine::US9226923, Staurosporine::US20240002365, Compound staurosporine::US11958831, Example Staurosporine::US20240254124, Compound Staurosporine::US20240309004, Compound STAUROSPORINE::US12350272, Compound Staurosporine::US12398142, Compound Staurosporine::US12410173, Compound Staurosporine Protein kinase C gamma type Homo sapiens 110 ChEMBL 10.1021/jm950588y 10.7270/Q25H7FBV 8709095 Jirousek, MR; Gillig, JR; Gonzalez, CM; Heath, WF; McDonald, JH; Neel, DA; Rito, CJ; Singh, U; Stramm, LE; Melikian-Badalian, A; Baevsky, M; Ballas, LM; Hall, SE; Winneroski, LL; Faul, MM 9/10/1996 11/10/2009 Eli Lilly http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=2579 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=602&target=Protein+kinase+C+gamma+type&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=2579&enzyme=Protein+kinase+C+gamma+type&column=ki&startPg=0&Increment=50&submit=Search STO 44259 8032349 CHEMBL388978 C02079 1 MAGLGPGVGDSEGGPRPLFCRKGALRQKVVHEVKSHKFTARFFKQPTFCSHCTDFIWGIGKQGLQCQVCSFVVHRRCHEFVTFECPGAGKGPQTDDPRNKHKFRLHSYSSPTFCDHCGSLLYGLVHQGMKCSCCEMNVHRRCVRSVPSLCGVDHTERRGRLQLEIRAPTADEIHVTVGEARNLIPMDPNGLSDPYVKLKLIPDPRNLTKQKTRTVKATLNPVWNETFVFNLKPGDVERRLSVEVWDWDRTSRNDFMGAMSFGVSELLKAPVDGWYKLLNQEEGEYYNVPVADADNCSLLQKFEACNYPLELYERVRMGPSSSPIPSPSPSPTDPKRCFFGASPGRLHISDFSFLMVLGKGSFGKVMLAERRGSDELYAIKILKKDVIVQDDDVDCTLVEKRVLALGGRGPGGRPHFLTQLHSTFQTPDRLYFVMEYVTGGDLMYHIQQLGKFKEPHAAFYAAEIAIGLFFLHNQGIIYRDLKLDNVMLDAEGHIKITDFGMCKENVFPGTTTRTFCGTPDYIAPEIIAYQPYGKSVDWWSFGVLLYEMLAGQPPFDGEDEEELFQAIMEQTVTYPKSLSREAVAICKGFLTKHPGKRLGSGPDGEPTIRAHGFFRWIDWERLERLEIPPPFRPRPCGRSGENFDKFFTRAAPALTPPDRLVLASIDQADFQGFTYVNPDFVHPDARSPTSPVPVPVM 2UZP Protein kinase C gamma type KPCG_HUMAN P05129 B7Z8Q0 50042819 C[C@@]12[C@@H]([C@@H](C[C@@H](O1)n3c4ccccc4c5c3c6n2c7ccccc7c6c8c5C(=O)NC8)NC)OC InChI=1S/C28H26N4O3/c1-28-26(34-3)17(29-2)12-20(35-28)31-18-10-6-4-8-14(18)22-23-16(13-30-27(23)33)21-15-9-5-7-11-19(15)32(28)25(21)24(22)31/h4-11,17,20,26,29H,12-13H2,1-3H3,(H,30,33) HKSZLNNOFSGOKW-UHFFFAOYSA-N 2579 CHEMBL388978::Staurosporine, 8::Staurosporin, 4::(2S,3R,4R,6R)-3-methoxy-2-methyl-4-(methylamino)-29-oxa-1,7,17-triazaoctacyclo[12.12.2.1^{2,6}.0^{7,28}.0^{8,13}.0^{15,19}.0^{20,27}.0^{21,26}]nonacosa-8(13),9,11,14(28),15(19),20(27),21(26),22,24-nonaen-16-one::Staurosporine::US9206188, Staurosporine::US9226923, Staurosporine::US20240002365, Compound staurosporine::US11958831, Example Staurosporine::US20240254124, Compound Staurosporine::US20240309004, Compound STAUROSPORINE::US12350272, Compound Staurosporine::US12398142, Compound Staurosporine::US12410173, Compound Staurosporine Protein kinase C beta type Homo sapiens 19 ChEMBL 10.1021/jm950588y 10.7270/Q25H7FBV 8709095 Jirousek, MR; Gillig, JR; Gonzalez, CM; Heath, WF; McDonald, JH; Neel, DA; Rito, CJ; Singh, U; Stramm, LE; Melikian-Badalian, A; Baevsky, M; Ballas, LM; Hall, SE; Winneroski, LL; Faul, MM 9/10/1996 11/10/2009 Eli Lilly http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=2579 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=600&target=Protein+kinase+C+beta+type&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=2579&enzyme=Protein+kinase+C+beta+type&column=ki&startPg=0&Increment=50&submit=Search STO 44259 8032349 CHEMBL388978 C02079 1 MADPAAGPPPSEGEESTVRFARKGALRQKNVHEVKNHKFTARFFKQPTFCSHCTDFIWGFGKQGFQCQVCCFVVHKRCHEFVTFSCPGADKGPASDDPRSKHKFKIHTYSSPTFCDHCGSLLYGLIHQGMKCDTCMMNVHKRCVMNVPSLCGTDHTERRGRIYIQAHIDRDVLIVLVRDAKNLVPMDPNGLSDPYVKLKLIPDPKSESKQKTKTIKCSLNPEWNETFRFQLKESDKDRRLSVEIWDWDLTSRNDFMGSLSFGISELQKASVDGWFKLLSQEEGEYFNVPVPPEGSEANEELRQKFERAKISQGTKVPEEKTTNTVSKFDNNGNRDRMKLTDFNFLMVLGKGSFGKVMLSERKGTDELYAVKILKKDVVIQDDDVECTMVEKRVLALPGKPPFLTQLHSCFQTMDRLYFVMEYVNGGDLMYHIQQVGRFKEPHAVFYAAEIAIGLFFLQSKGIIYRDLKLDNVMLDSEGHIKIADFGMCKENIWDGVTTKTFCGTPDYIAPEIIAYQPYGKSVDWWAFGVLLYEMLAGQAPFEGEDEDELFQSIMEHNVAYPKSMSKEAVAICKGLMTKHPGKRLGCGPEGERDIKEHAFFRYIDWEKLERKEIQPPYKPKARDKRDTSNFDKEFTRQPVELTPTDKLFIMNLDQNEFAGFSYTNPEFVINV 8SE4,8SE3,8SE2,3PFQ,9C5F,1A25 Protein kinase C beta type KPCB_HUMAN P05771 C5IFJ8 D3DWF5 O43744 P05127 Q15138 Q93060 Q9UE49 Q9UE50 Q9UEH8 Q9UJ30 Q9UJ33 50042820 CNC[C@@H]1CCn2cc(C3=C(C(=O)NC3=O)c3cn(CCO1)c1ccccc31)c1ccccc21 |t:9| InChI=1S/C27H26N4O3/c1-28-14-17-10-11-30-15-20(18-6-2-4-8-22(18)30)24-25(27(33)29-26(24)32)21-16-31(12-13-34-17)23-9-5-3-7-19(21)23/h2-9,15-17,28H,10-14H2,1H3,(H,29,32,33) ZEYTZKVCOZMUKL-UHFFFAOYSA-N 50052034 18-methylaminomethyl-(18S)-17-oxa-4,14,21-triazahexacyclo[19.6.1.17,14.02,6.08,13.022,27]nonacosa-1(28),2(6),7(29),8(13),9,11,22(27),23,25-nonaene-3,5-dione::CHEMBL311543 Protein kinase C alpha type Homo sapiens 240 ChEMBL 10.1021/jm950588y 10.7270/Q25H7FBV 8709095 Jirousek, MR; Gillig, JR; Gonzalez, CM; Heath, WF; McDonald, JH; Neel, DA; Rito, CJ; Singh, U; Stramm, LE; Melikian-Badalian, A; Baevsky, M; Ballas, LM; Hall, SE; Winneroski, LL; Faul, MM 9/10/1996 11/10/2009 Eli Lilly http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50052034 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=599&target=Protein+kinase+C+alpha+type&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50052034&enzyme=Protein+kinase+C+alpha+type&column=ki&startPg=0&Increment=50&submit=Search 10671412 103948959 CHEMBL311543 1 MADVFPGNDSTASQDVANRFARKGALRQKNVHEVKDHKFIARFFKQPTFCSHCTDFIWGFGKQGFQCQVCCFVVHKRCHEFVTFSCPGADKGPDTDDPRSKHKFKIHTYGSPTFCDHCGSLLYGLIHQGMKCDTCDMNVHKQCVINVPSLCGMDHTEKRGRIYLKAEVADEKLHVTVRDAKNLIPMDPNGLSDPYVKLKLIPDPKNESKQKTKTIRSTLNPQWNESFTFKLKPSDKDRRLSVEIWDWDRTTRNDFMGSLSFGVSELMKMPASGWYKLLNQEEGEYYNVPIPEGDEEGNMELRQKFEKAKLGPAGNKVISPSEDRKQPSNNLDRVKLTDFNFLMVLGKGSFGKVMLADRKGTEELYAIKILKKDVVIQDDDVECTMVEKRVLALLDKPPFLTQLHSCFQTVDRLYFVMEYVNGGDLMYHIQQVGKFKEPQAVFYAAEISIGLFFLHKRGIIYRDLKLDNVMLDSEGHIKIADFGMCKEHMMDGVTTRTFCGTPDYIAPEIIAYQPYGKSVDWWAYGVLLYEMLAGQPPFDGEDEDELFQSIMEHNVSYPKSLSKEAVSVCKGLMTKHPAKRLGCGPEGERDVREHAFFRRIDWEKLENREIQPPFKPKVCGKGAENFDKFFTRGQPVLTPPDQLVIANIDQSDFEGFSYVNPQFVHPILQSAV 4RA4,4DNL Protein kinase C alpha type KPCA_HUMAN P17252 B5BU22 Q15137 Q32M72 Q96RE4 50042821 CN1CCN(C[C@@H]2CCn3cc(C4=C(C(=O)NC4=O)c4cn(CCO2)c2ccccc42)c2ccccc32)CC1 |t:12| InChI=1S/C31H33N5O3/c1-33-12-14-34(15-13-33)18-21-10-11-35-19-24(22-6-2-4-8-26(22)35)28-29(31(38)32-30(28)37)25-20-36(16-17-39-21)27-9-5-3-7-23(25)27/h2-9,19-21H,10-18H2,1H3,(H,32,37,38) QKXPAKQCFJVAFI-UHFFFAOYSA-N 50052041 18-(4-methylhexahydro-1-pyrazinylmethyl)-(18S)-17-oxa-4,14,21-triazahexacyclo[19.6.1.17,14.02,6.08,13.022,27]nonacosa-1(28),2(6),7(29),8(13),9,11,22(27),23,25-nonaene-3,5-dione::CHEMBL91959 Protein kinase C alpha type Homo sapiens 1800 ChEMBL 10.1021/jm950588y 10.7270/Q25H7FBV 8709095 Jirousek, MR; Gillig, JR; Gonzalez, CM; Heath, WF; McDonald, JH; Neel, DA; Rito, CJ; Singh, U; Stramm, LE; Melikian-Badalian, A; Baevsky, M; Ballas, LM; Hall, SE; Winneroski, LL; Faul, MM 9/10/1996 11/10/2009 Eli Lilly http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50052041 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=599&target=Protein+kinase+C+alpha+type&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50052041&enzyme=Protein+kinase+C+alpha+type&column=ki&startPg=0&Increment=50&submit=Search 10768377 103948966 CHEMBL91959 1 MADVFPGNDSTASQDVANRFARKGALRQKNVHEVKDHKFIARFFKQPTFCSHCTDFIWGFGKQGFQCQVCCFVVHKRCHEFVTFSCPGADKGPDTDDPRSKHKFKIHTYGSPTFCDHCGSLLYGLIHQGMKCDTCDMNVHKQCVINVPSLCGMDHTEKRGRIYLKAEVADEKLHVTVRDAKNLIPMDPNGLSDPYVKLKLIPDPKNESKQKTKTIRSTLNPQWNESFTFKLKPSDKDRRLSVEIWDWDRTTRNDFMGSLSFGVSELMKMPASGWYKLLNQEEGEYYNVPIPEGDEEGNMELRQKFEKAKLGPAGNKVISPSEDRKQPSNNLDRVKLTDFNFLMVLGKGSFGKVMLADRKGTEELYAIKILKKDVVIQDDDVECTMVEKRVLALLDKPPFLTQLHSCFQTVDRLYFVMEYVNGGDLMYHIQQVGKFKEPQAVFYAAEISIGLFFLHKRGIIYRDLKLDNVMLDSEGHIKIADFGMCKEHMMDGVTTRTFCGTPDYIAPEIIAYQPYGKSVDWWAYGVLLYEMLAGQPPFDGEDEDELFQSIMEHNVSYPKSLSKEAVSVCKGLMTKHPAKRLGCGPEGERDVREHAFFRRIDWEKLENREIQPPFKPKVCGKGAENFDKFFTRGQPVLTPPDQLVIANIDQSDFEGFSYVNPQFVHPILQSAV 4RA4,4DNL Protein kinase C alpha type KPCA_HUMAN P17252 B5BU22 Q15137 Q32M72 Q96RE4 50042822 O=C1NC(=O)C2=C1c1cn(CCO[C@H](CN3CCCC3)CCn3cc2c2ccccc32)c2ccccc12 |c:5| InChI=1S/C30H30N4O3/c35-29-27-23-18-33(25-9-3-1-7-21(23)25)14-11-20(17-32-12-5-6-13-32)37-16-15-34-19-24(28(27)30(36)31-29)22-8-2-4-10-26(22)34/h1-4,7-10,18-20H,5-6,11-17H2,(H,31,35,36) WORLFHNBHSSAJQ-UHFFFAOYSA-N 50052038 18-tetrahydro-1H-1-pyrrolylmethyl-(18S)-17-oxa-4,14,21-triazahexacyclo[19.6.1.17,14.02,6.08,13.022,27]nonacosa-1(28),2(6),7(29),8(13),9,11,22(27),23,25-nonaene-3,5-dione::CHEMBL419866 Protein kinase C beta type Homo sapiens 44.0 ChEMBL 10.1021/jm950588y 10.7270/Q25H7FBV 8709095 Jirousek, MR; Gillig, JR; Gonzalez, CM; Heath, WF; McDonald, JH; Neel, DA; Rito, CJ; Singh, U; Stramm, LE; Melikian-Badalian, A; Baevsky, M; Ballas, LM; Hall, SE; Winneroski, LL; Faul, MM 9/10/1996 11/10/2009 Eli Lilly http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50052038 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=600&target=Protein+kinase+C+beta+type&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50052038&enzyme=Protein+kinase+C+beta+type&column=ki&startPg=0&Increment=50&submit=Search 11799388 103948963 CHEMBL419866 1 MADPAAGPPPSEGEESTVRFARKGALRQKNVHEVKNHKFTARFFKQPTFCSHCTDFIWGFGKQGFQCQVCCFVVHKRCHEFVTFSCPGADKGPASDDPRSKHKFKIHTYSSPTFCDHCGSLLYGLIHQGMKCDTCMMNVHKRCVMNVPSLCGTDHTERRGRIYIQAHIDRDVLIVLVRDAKNLVPMDPNGLSDPYVKLKLIPDPKSESKQKTKTIKCSLNPEWNETFRFQLKESDKDRRLSVEIWDWDLTSRNDFMGSLSFGISELQKASVDGWFKLLSQEEGEYFNVPVPPEGSEANEELRQKFERAKISQGTKVPEEKTTNTVSKFDNNGNRDRMKLTDFNFLMVLGKGSFGKVMLSERKGTDELYAVKILKKDVVIQDDDVECTMVEKRVLALPGKPPFLTQLHSCFQTMDRLYFVMEYVNGGDLMYHIQQVGRFKEPHAVFYAAEIAIGLFFLQSKGIIYRDLKLDNVMLDSEGHIKIADFGMCKENIWDGVTTKTFCGTPDYIAPEIIAYQPYGKSVDWWAFGVLLYEMLAGQAPFEGEDEDELFQSIMEHNVAYPKSMSKEAVAICKGLMTKHPGKRLGCGPEGERDIKEHAFFRYIDWEKLERKEIQPPYKPKARDKRDTSNFDKEFTRQPVELTPTDKLFIMNLDQNEFAGFSYTNPEFVINV 8SE4,8SE3,8SE2,3PFQ,9C5F,1A25 Protein kinase C beta type KPCB_HUMAN P05771 C5IFJ8 D3DWF5 O43744 P05127 Q15138 Q93060 Q9UE49 Q9UE50 Q9UEH8 Q9UJ30 Q9UJ33 50042823 O=C1NC(=O)C2=C1c1cn(CCO[C@H](CN3CCOCC3)CCn3cc2c2ccccc32)c2ccccc12 |c:5| InChI=1S/C30H30N4O4/c35-29-27-23-18-33(25-7-3-1-5-21(23)25)10-9-20(17-32-11-14-37-15-12-32)38-16-13-34-19-24(28(27)30(36)31-29)22-6-2-4-8-26(22)34/h1-8,18-20H,9-17H2,(H,31,35,36) CLHMTFQYMLYQME-UHFFFAOYSA-N 50052035 18-(1,4-oxazinan-4-ylmethyl)-(18S)-17-oxa-4,14,21-triazahexacyclo[19.6.1.17,14.02,6.08,13.022,27]nonacosa-1(28),2(6),7(29),8(13),9,11,22(27),23,25-nonaene-3,5-dione::CHEMBL315357 Protein kinase C eta type Homo sapiens 1700 ChEMBL 10.1021/jm950588y 10.7270/Q25H7FBV 8709095 Jirousek, MR; Gillig, JR; Gonzalez, CM; Heath, WF; McDonald, JH; Neel, DA; Rito, CJ; Singh, U; Stramm, LE; Melikian-Badalian, A; Baevsky, M; Ballas, LM; Hall, SE; Winneroski, LL; Faul, MM 9/10/1996 11/10/2009 Eli Lilly http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50052035 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=605&target=Protein+kinase+C+eta+type&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50052035&enzyme=Protein+kinase+C+eta+type&column=ki&startPg=0&Increment=50&submit=Search 10673286 103948960 CHEMBL315357 1 MSSGTMKFNGYLRVRIGEAVGLQPTRWSLRHSLFKKGHQLLDPYLTVSVDQVRVGQTSTKQKTNKPTYNEEFCANVTDGGHLELAVFHETPLGYDHFVANCTLQFQELLRTTGASDTFEGWVDLEPEGKVFVVITLTGSFTEATLQRDRIFKHFTRKRQRAMRRRVHQINGHKFMATYLRQPTYCSHCREFIWGVFGKQGYQCQVCTCVVHKRCHHLIVTACTCQNNINKVDSKIAEQRFGINIPHKFSIHNYKVPTFCDHCGSLLWGIMRQGLQCKICKMNVHIRCQANVAPNCGVNAVELAKTLAGMGLQPGNISPTSKLVSRSTLRRQGKESSKEGNGIGVNSSNRLGIDNFEFIRVLGKGSFGKVMLARVKETGDLYAVKVLKKDVILQDDDVECTMTEKRILSLARNHPFLTQLFCCFQTPDRLFFVMEFVNGGDLMFHIQKSRRFDEARARFYAAEIISALMFLHDKGIIYRDLKLDNVLLDHEGHCKLADFGMCKEGICNGVTTATFCGTPDYIAPEILQEMLYGPAVDWWAMGVLLYEMLCGHAPFEAENEDDLFEAILNDEVVYPTWLHEDATGILKSFMTKNPTMRLGSLTQGGEHAILRHPFFKEIDWAQLNHRQIEPPFRPRIKSREDVSNFDPDFIKEEPVLTPIDEGHLPMINQDEFRNFSYVSPELQP 2FK9 Protein kinase C eta type KPCL_HUMAN P24723 B4DJN5 Q16246 Q8NE03 50042824 O=C1NC(=O)C2=C1c1cn(CCO[C@H](CN3CCCC3)CCn3cc2c2ccccc32)c2ccccc12 |c:5| InChI=1S/C30H30N4O3/c35-29-27-23-18-33(25-9-3-1-7-21(23)25)14-11-20(17-32-12-5-6-13-32)37-16-15-34-19-24(28(27)30(36)31-29)22-8-2-4-10-26(22)34/h1-4,7-10,18-20H,5-6,11-17H2,(H,31,35,36) WORLFHNBHSSAJQ-UHFFFAOYSA-N 50052038 18-tetrahydro-1H-1-pyrrolylmethyl-(18S)-17-oxa-4,14,21-triazahexacyclo[19.6.1.17,14.02,6.08,13.022,27]nonacosa-1(28),2(6),7(29),8(13),9,11,22(27),23,25-nonaene-3,5-dione::CHEMBL419866 Protein kinase C eta type Homo sapiens 350 ChEMBL 10.1021/jm950588y 10.7270/Q25H7FBV 8709095 Jirousek, MR; Gillig, JR; Gonzalez, CM; Heath, WF; McDonald, JH; Neel, DA; Rito, CJ; Singh, U; Stramm, LE; Melikian-Badalian, A; Baevsky, M; Ballas, LM; Hall, SE; Winneroski, LL; Faul, MM 9/10/1996 11/10/2009 Eli Lilly http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50052038 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=605&target=Protein+kinase+C+eta+type&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50052038&enzyme=Protein+kinase+C+eta+type&column=ki&startPg=0&Increment=50&submit=Search 11799388 103948963 CHEMBL419866 1 MSSGTMKFNGYLRVRIGEAVGLQPTRWSLRHSLFKKGHQLLDPYLTVSVDQVRVGQTSTKQKTNKPTYNEEFCANVTDGGHLELAVFHETPLGYDHFVANCTLQFQELLRTTGASDTFEGWVDLEPEGKVFVVITLTGSFTEATLQRDRIFKHFTRKRQRAMRRRVHQINGHKFMATYLRQPTYCSHCREFIWGVFGKQGYQCQVCTCVVHKRCHHLIVTACTCQNNINKVDSKIAEQRFGINIPHKFSIHNYKVPTFCDHCGSLLWGIMRQGLQCKICKMNVHIRCQANVAPNCGVNAVELAKTLAGMGLQPGNISPTSKLVSRSTLRRQGKESSKEGNGIGVNSSNRLGIDNFEFIRVLGKGSFGKVMLARVKETGDLYAVKVLKKDVILQDDDVECTMTEKRILSLARNHPFLTQLFCCFQTPDRLFFVMEFVNGGDLMFHIQKSRRFDEARARFYAAEIISALMFLHDKGIIYRDLKLDNVLLDHEGHCKLADFGMCKEGICNGVTTATFCGTPDYIAPEILQEMLYGPAVDWWAMGVLLYEMLCGHAPFEAENEDDLFEAILNDEVVYPTWLHEDATGILKSFMTKNPTMRLGSLTQGGEHAILRHPFFKEIDWAQLNHRQIEPPFRPRIKSREDVSNFDPDFIKEEPVLTPIDEGHLPMINQDEFRNFSYVSPELQP 2FK9 Protein kinase C eta type KPCL_HUMAN P24723 B4DJN5 Q16246 Q8NE03 50042825 C[C@@]12[C@@H]([C@@H](C[C@@H](O1)n3c4ccccc4c5c3c6n2c7ccccc7c6c8c5C(=O)NC8)NC)OC InChI=1S/C28H26N4O3/c1-28-26(34-3)17(29-2)12-20(35-28)31-18-10-6-4-8-14(18)22-23-16(13-30-27(23)33)21-15-9-5-7-11-19(15)32(28)25(21)24(22)31/h4-11,17,20,26,29H,12-13H2,1-3H3,(H,30,33) HKSZLNNOFSGOKW-UHFFFAOYSA-N 2579 CHEMBL388978::Staurosporine, 8::Staurosporin, 4::(2S,3R,4R,6R)-3-methoxy-2-methyl-4-(methylamino)-29-oxa-1,7,17-triazaoctacyclo[12.12.2.1^{2,6}.0^{7,28}.0^{8,13}.0^{15,19}.0^{20,27}.0^{21,26}]nonacosa-8(13),9,11,14(28),15(19),20(27),21(26),22,24-nonaen-16-one::Staurosporine::US9206188, Staurosporine::US9226923, Staurosporine::US20240002365, Compound staurosporine::US11958831, Example Staurosporine::US20240254124, Compound Staurosporine::US20240309004, Compound STAUROSPORINE::US12350272, Compound Staurosporine::US12398142, Compound Staurosporine::US12410173, Compound Staurosporine Protein kinase C zeta type Homo sapiens >1500 ChEMBL 10.1021/jm950588y 10.7270/Q25H7FBV 8709095 Jirousek, MR; Gillig, JR; Gonzalez, CM; Heath, WF; McDonald, JH; Neel, DA; Rito, CJ; Singh, U; Stramm, LE; Melikian-Badalian, A; Baevsky, M; Ballas, LM; Hall, SE; Winneroski, LL; Faul, MM 9/10/1996 11/10/2009 Eli Lilly http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=2579 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=606&target=Protein+kinase+C+zeta+type&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=2579&enzyme=Protein+kinase+C+zeta+type&column=ki&startPg=0&Increment=50&submit=Search STO 44259 8032349 CHEMBL388978 C02079 1 MPSRTGPKMEGSGGRVRLKAHYGGDIFITSVDAATTFEELCEEVRDMCRLHQQHPLTLKWVDSEGDPCTVSSQMELEEAFRLARQCRDEGLIIHVFPSTPEQPGLPCPGEDKSIYRRGARRWRKLYRANGHLFQAKRFNRRAYCGQCSERIWGLARQGYRCINCKLLVHKRCHGLVPLTCRKHMDSVMPSQEPPVDDKNEDADLPSEETDGIAYISSSRKHDSIKDDSEDLKPVIDGMDGIKISQGLGLQDFDLIRVIGRGSYAKVLLVRLKKNDQIYAMKVVKKELVHDDEDIDWVQTEKHVFEQASSNPFLVGLHSCFQTTSRLFLVIEYVNGGDLMFHMQRQRKLPEEHARFYAAEICIALNFLHERGIIYRDLKLDNVLLDADGHIKLTDYGMCKEGLGPGDTTSTFCGTPNYIAPEILRGEEYGFSVDWWALGVLMFEMMAGRSPFDIITDNPDMNTEDYLFQVILEKPIRIPRFLSVKASHVLKGFLNKDPKERLGCRPQTGFSDIKSHAFFRSIDWDLLEKKQALPPFQPQITDDYGLDNFDTQFTSEPVQLTPDDEDAIKRIDQSEFEGFEYINPLLLSTEESV Protein kinase C zeta type KPCZ_HUMAN Q05513 A8K4N0 A8MU64 B7Z2J7 E9PCW2 Q15207 Q5SYT5 Q969S4 50042826 O=C1NC(=O)C2=C1c1cn(CCO[C@H](CN3CCOCC3)CCn3cc2c2ccccc32)c2ccccc12 |c:5| InChI=1S/C30H30N4O4/c35-29-27-23-18-33(25-7-3-1-5-21(23)25)10-9-20(17-32-11-14-37-15-12-32)38-16-13-34-19-24(28(27)30(36)31-29)22-6-2-4-8-26(22)34/h1-8,18-20H,9-17H2,(H,31,35,36) CLHMTFQYMLYQME-UHFFFAOYSA-N 50052035 18-(1,4-oxazinan-4-ylmethyl)-(18S)-17-oxa-4,14,21-triazahexacyclo[19.6.1.17,14.02,6.08,13.022,27]nonacosa-1(28),2(6),7(29),8(13),9,11,22(27),23,25-nonaene-3,5-dione::CHEMBL315357 Protein kinase C alpha type Homo sapiens 3500 ChEMBL 10.1021/jm950588y 10.7270/Q25H7FBV 8709095 Jirousek, MR; Gillig, JR; Gonzalez, CM; Heath, WF; McDonald, JH; Neel, DA; Rito, CJ; Singh, U; Stramm, LE; Melikian-Badalian, A; Baevsky, M; Ballas, LM; Hall, SE; Winneroski, LL; Faul, MM 9/10/1996 11/10/2009 Eli Lilly http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50052035 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=599&target=Protein+kinase+C+alpha+type&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50052035&enzyme=Protein+kinase+C+alpha+type&column=ki&startPg=0&Increment=50&submit=Search 10673286 103948960 CHEMBL315357 1 MADVFPGNDSTASQDVANRFARKGALRQKNVHEVKDHKFIARFFKQPTFCSHCTDFIWGFGKQGFQCQVCCFVVHKRCHEFVTFSCPGADKGPDTDDPRSKHKFKIHTYGSPTFCDHCGSLLYGLIHQGMKCDTCDMNVHKQCVINVPSLCGMDHTEKRGRIYLKAEVADEKLHVTVRDAKNLIPMDPNGLSDPYVKLKLIPDPKNESKQKTKTIRSTLNPQWNESFTFKLKPSDKDRRLSVEIWDWDRTTRNDFMGSLSFGVSELMKMPASGWYKLLNQEEGEYYNVPIPEGDEEGNMELRQKFEKAKLGPAGNKVISPSEDRKQPSNNLDRVKLTDFNFLMVLGKGSFGKVMLADRKGTEELYAIKILKKDVVIQDDDVECTMVEKRVLALLDKPPFLTQLHSCFQTVDRLYFVMEYVNGGDLMYHIQQVGKFKEPQAVFYAAEISIGLFFLHKRGIIYRDLKLDNVMLDSEGHIKIADFGMCKEHMMDGVTTRTFCGTPDYIAPEIIAYQPYGKSVDWWAYGVLLYEMLAGQPPFDGEDEDELFQSIMEHNVSYPKSLSKEAVSVCKGLMTKHPAKRLGCGPEGERDVREHAFFRRIDWEKLENREIQPPFKPKVCGKGAENFDKFFTRGQPVLTPPDQLVIANIDQSDFEGFSYVNPQFVHPILQSAV 4RA4,4DNL Protein kinase C alpha type KPCA_HUMAN P17252 B5BU22 Q15137 Q32M72 Q96RE4 50042827 O=C1NC(=O)C2=C1c1cn(CCO[C@H](CNCc3ccccc3)CCn3cc2c2ccccc32)c2ccccc12 |c:5| InChI=1S/C33H30N4O3/c38-32-30-26-20-36(28-12-6-4-10-24(26)28)15-14-23(19-34-18-22-8-2-1-3-9-22)40-17-16-37-21-27(31(30)33(39)35-32)25-11-5-7-13-29(25)37/h1-13,20-21,23,34H,14-19H2,(H,35,38,39) RIXHNSFDUIBDSB-UHFFFAOYSA-N 50052040 18-benzylaminomethyl-(18S)-17-oxa-4,14,21-triazahexacyclo[19.6.1.17,14.02,6.08,13.022,27]nonacosa-1(28),2(6),7(29),8(13),9,11,22(27),23,25-nonaene-3,5-dione::CHEMBL328229 Protein kinase C alpha type Homo sapiens 6300 ChEMBL 10.1021/jm950588y 10.7270/Q25H7FBV 8709095 Jirousek, MR; Gillig, JR; Gonzalez, CM; Heath, WF; McDonald, JH; Neel, DA; Rito, CJ; Singh, U; Stramm, LE; Melikian-Badalian, A; Baevsky, M; Ballas, LM; Hall, SE; Winneroski, LL; Faul, MM 9/10/1996 11/10/2009 Eli Lilly http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50052040 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=599&target=Protein+kinase+C+alpha+type&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50052040&enzyme=Protein+kinase+C+alpha+type&column=ki&startPg=0&Increment=50&submit=Search 10768554 103948965 CHEMBL328229 1 MADVFPGNDSTASQDVANRFARKGALRQKNVHEVKDHKFIARFFKQPTFCSHCTDFIWGFGKQGFQCQVCCFVVHKRCHEFVTFSCPGADKGPDTDDPRSKHKFKIHTYGSPTFCDHCGSLLYGLIHQGMKCDTCDMNVHKQCVINVPSLCGMDHTEKRGRIYLKAEVADEKLHVTVRDAKNLIPMDPNGLSDPYVKLKLIPDPKNESKQKTKTIRSTLNPQWNESFTFKLKPSDKDRRLSVEIWDWDRTTRNDFMGSLSFGVSELMKMPASGWYKLLNQEEGEYYNVPIPEGDEEGNMELRQKFEKAKLGPAGNKVISPSEDRKQPSNNLDRVKLTDFNFLMVLGKGSFGKVMLADRKGTEELYAIKILKKDVVIQDDDVECTMVEKRVLALLDKPPFLTQLHSCFQTVDRLYFVMEYVNGGDLMYHIQQVGKFKEPQAVFYAAEISIGLFFLHKRGIIYRDLKLDNVMLDSEGHIKIADFGMCKEHMMDGVTTRTFCGTPDYIAPEIIAYQPYGKSVDWWAYGVLLYEMLAGQPPFDGEDEDELFQSIMEHNVSYPKSLSKEAVSVCKGLMTKHPAKRLGCGPEGERDVREHAFFRRIDWEKLENREIQPPFKPKVCGKGAENFDKFFTRGQPVLTPPDQLVIANIDQSDFEGFSYVNPQFVHPILQSAV 4RA4,4DNL Protein kinase C alpha type KPCA_HUMAN P17252 B5BU22 Q15137 Q32M72 Q96RE4 50042828 NC[C@@H]1CCn2cc(C3=C(C(=O)NC3=O)c3cn(CCO1)c1ccccc31)c1ccccc21 |t:8| InChI=1S/C26H24N4O3/c27-13-16-9-10-29-14-19(17-5-1-3-7-21(17)29)23-24(26(32)28-25(23)31)20-15-30(11-12-33-16)22-8-4-2-6-18(20)22/h1-8,14-16H,9-13,27H2,(H,28,31,32) JPLUPRIZLHXUPQ-UHFFFAOYSA-N 50052037 18-aminomethyl-(18S)-17-oxa-4,14,21-triazahexacyclo[19.6.1.17,14.02,6.08,13.022,27]nonacosa-1(28),2(6),7(29),8(13),9,11,22(27),23,25-nonaene-3,5-dione::CHEMBL316239 Protein kinase C eta type Homo sapiens 240 ChEMBL 10.1021/jm950588y 10.7270/Q25H7FBV 8709095 Jirousek, MR; Gillig, JR; Gonzalez, CM; Heath, WF; McDonald, JH; Neel, DA; Rito, CJ; Singh, U; Stramm, LE; Melikian-Badalian, A; Baevsky, M; Ballas, LM; Hall, SE; Winneroski, LL; Faul, MM 9/10/1996 11/10/2009 Eli Lilly http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50052037 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=605&target=Protein+kinase+C+eta+type&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50052037&enzyme=Protein+kinase+C+eta+type&column=ki&startPg=0&Increment=50&submit=Search 10527068 103948962 CHEMBL316239 1 MSSGTMKFNGYLRVRIGEAVGLQPTRWSLRHSLFKKGHQLLDPYLTVSVDQVRVGQTSTKQKTNKPTYNEEFCANVTDGGHLELAVFHETPLGYDHFVANCTLQFQELLRTTGASDTFEGWVDLEPEGKVFVVITLTGSFTEATLQRDRIFKHFTRKRQRAMRRRVHQINGHKFMATYLRQPTYCSHCREFIWGVFGKQGYQCQVCTCVVHKRCHHLIVTACTCQNNINKVDSKIAEQRFGINIPHKFSIHNYKVPTFCDHCGSLLWGIMRQGLQCKICKMNVHIRCQANVAPNCGVNAVELAKTLAGMGLQPGNISPTSKLVSRSTLRRQGKESSKEGNGIGVNSSNRLGIDNFEFIRVLGKGSFGKVMLARVKETGDLYAVKVLKKDVILQDDDVECTMTEKRILSLARNHPFLTQLFCCFQTPDRLFFVMEFVNGGDLMFHIQKSRRFDEARARFYAAEIISALMFLHDKGIIYRDLKLDNVLLDHEGHCKLADFGMCKEGICNGVTTATFCGTPDYIAPEILQEMLYGPAVDWWAMGVLLYEMLCGHAPFEAENEDDLFEAILNDEVVYPTWLHEDATGILKSFMTKNPTMRLGSLTQGGEHAILRHPFFKEIDWAQLNHRQIEPPFRPRIKSREDVSNFDPDFIKEEPVLTPIDEGHLPMINQDEFRNFSYVSPELQP 2FK9 Protein kinase C eta type KPCL_HUMAN P24723 B4DJN5 Q16246 Q8NE03 50042829 O=C1NC(=O)C2=C1c1cn(CCO[C@H](CN3CCCC3)CCn3cc2c2ccccc32)c2ccccc12 |c:5| InChI=1S/C30H30N4O3/c35-29-27-23-18-33(25-9-3-1-7-21(23)25)14-11-20(17-32-12-5-6-13-32)37-16-15-34-19-24(28(27)30(36)31-29)22-8-2-4-10-26(22)34/h1-4,7-10,18-20H,5-6,11-17H2,(H,31,35,36) WORLFHNBHSSAJQ-UHFFFAOYSA-N 50052038 18-tetrahydro-1H-1-pyrrolylmethyl-(18S)-17-oxa-4,14,21-triazahexacyclo[19.6.1.17,14.02,6.08,13.022,27]nonacosa-1(28),2(6),7(29),8(13),9,11,22(27),23,25-nonaene-3,5-dione::CHEMBL419866 Protein kinase C beta type Homo sapiens 44 ChEMBL 10.1021/jm950588y 10.7270/Q25H7FBV 8709095 Jirousek, MR; Gillig, JR; Gonzalez, CM; Heath, WF; McDonald, JH; Neel, DA; Rito, CJ; Singh, U; Stramm, LE; Melikian-Badalian, A; Baevsky, M; Ballas, LM; Hall, SE; Winneroski, LL; Faul, MM 9/10/1996 11/10/2009 Eli Lilly http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50052038 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=600&target=Protein+kinase+C+beta+type&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50052038&enzyme=Protein+kinase+C+beta+type&column=ki&startPg=0&Increment=50&submit=Search 11799388 103948963 CHEMBL419866 1 MADPAAGPPPSEGEESTVRFARKGALRQKNVHEVKNHKFTARFFKQPTFCSHCTDFIWGFGKQGFQCQVCCFVVHKRCHEFVTFSCPGADKGPASDDPRSKHKFKIHTYSSPTFCDHCGSLLYGLIHQGMKCDTCMMNVHKRCVMNVPSLCGTDHTERRGRIYIQAHIDRDVLIVLVRDAKNLVPMDPNGLSDPYVKLKLIPDPKSESKQKTKTIKCSLNPEWNETFRFQLKESDKDRRLSVEIWDWDLTSRNDFMGSLSFGISELQKASVDGWFKLLSQEEGEYFNVPVPPEGSEANEELRQKFERAKISQGTKVPEEKTTNTVSKFDNNGNRDRMKLTDFNFLMVLGKGSFGKVMLSERKGTDELYAVKILKKDVVIQDDDVECTMVEKRVLALPGKPPFLTQLHSCFQTMDRLYFVMEYVNGGDLMYHIQQVGRFKEPHAVFYAAEIAIGLFFLQSKGIIYRDLKLDNVMLDSEGHIKIADFGMCKENIWDGVTTKTFCGTPDYIAPEIIAYQPYGKSVDWWAFGVLLYEMLAGQAPFEGEDEDELFQSIMEHNVAYPKSMSKEAVAICKGLMTKHPGKRLGCGPEGERDIKEHAFFRYIDWEKLERKEIQPPYKPKARDKRDTSNFDKEFTRQPVELTPTDKLFIMNLDQNEFAGFSYTNPEFVINV 8SE4,8SE3,8SE2,3PFQ,9C5F,1A25 Protein kinase C beta type KPCB_HUMAN P05771 C5IFJ8 D3DWF5 O43744 P05127 Q15138 Q93060 Q9UE49 Q9UE50 Q9UEH8 Q9UJ30 Q9UJ33 50042830 CN(C)C[C@@H]1CCn2cc(C3=C(C(=O)NC3=O)c3cn(CCO1)c1ccccc31)c1ccccc21 |r,t:10| InChI=1S/C28H28N4O3/c1-30(2)15-18-11-12-31-16-21(19-7-3-5-9-23(19)31)25-26(28(34)29-27(25)33)22-17-32(13-14-35-18)24-10-6-4-8-20(22)24/h3-10,16-18H,11-15H2,1-2H3,(H,29,33,34) ZCBUQCWBWNUWSU-UHFFFAOYSA-N 17055 (9S)-9-[(dimethylamino)methyl]-6,7,10,11-tetrahydro-9H,18H-5,21:12,17-di(metheno)dibenzo[e,k]pyrrolo[3,4-h][1,4,13]oxadiazacyclohexadecine-18,20(19H)-dione::(18S)-18-[(dimethylamino)methyl]-17-oxa-4,14,21-triazahexacyclo[19.6.1.1^{7,14}.0^{2,6}.0^{8,13}.0^{22,27}]nonacosa-1(28),2(6),7(29),8(13),9,11,22(27),23,25-nonaene-3,5-dione::K00587a::Ruboxistaurin::LY-333531::cid_153999::LY 333531::LY333531 Protein kinase C eta type Homo sapiens 52 ChEMBL 10.1021/jm950588y 10.7270/Q25H7FBV 8709095 Jirousek, MR; Gillig, JR; Gonzalez, CM; Heath, WF; McDonald, JH; Neel, DA; Rito, CJ; Singh, U; Stramm, LE; Melikian-Badalian, A; Baevsky, M; Ballas, LM; Hall, SE; Winneroski, LL; Faul, MM 9/10/1996 11/10/2009 Eli Lilly http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=17055 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=605&target=Protein+kinase+C+eta+type&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=17055&enzyme=Protein+kinase+C+eta+type&column=ki&startPg=0&Increment=50&submit=Search 153999 46517285 1 MSSGTMKFNGYLRVRIGEAVGLQPTRWSLRHSLFKKGHQLLDPYLTVSVDQVRVGQTSTKQKTNKPTYNEEFCANVTDGGHLELAVFHETPLGYDHFVANCTLQFQELLRTTGASDTFEGWVDLEPEGKVFVVITLTGSFTEATLQRDRIFKHFTRKRQRAMRRRVHQINGHKFMATYLRQPTYCSHCREFIWGVFGKQGYQCQVCTCVVHKRCHHLIVTACTCQNNINKVDSKIAEQRFGINIPHKFSIHNYKVPTFCDHCGSLLWGIMRQGLQCKICKMNVHIRCQANVAPNCGVNAVELAKTLAGMGLQPGNISPTSKLVSRSTLRRQGKESSKEGNGIGVNSSNRLGIDNFEFIRVLGKGSFGKVMLARVKETGDLYAVKVLKKDVILQDDDVECTMTEKRILSLARNHPFLTQLFCCFQTPDRLFFVMEFVNGGDLMFHIQKSRRFDEARARFYAAEIISALMFLHDKGIIYRDLKLDNVLLDHEGHCKLADFGMCKEGICNGVTTATFCGTPDYIAPEILQEMLYGPAVDWWAMGVLLYEMLCGHAPFEAENEDDLFEAILNDEVVYPTWLHEDATGILKSFMTKNPTMRLGSLTQGGEHAILRHPFFKEIDWAQLNHRQIEPPFRPRIKSREDVSNFDPDFIKEEPVLTPIDEGHLPMINQDEFRNFSYVSPELQP 2FK9 Protein kinase C eta type KPCL_HUMAN P24723 B4DJN5 Q16246 Q8NE03 50042832 CN1CCN(C[C@@H]2CCn3cc(C4=C(C(=O)NC4=O)c4cn(CCO2)c2ccccc42)c2ccccc32)CC1 |t:12| InChI=1S/C31H33N5O3/c1-33-12-14-34(15-13-33)18-21-10-11-35-19-24(22-6-2-4-8-26(22)35)28-29(31(38)32-30(28)37)25-20-36(16-17-39-21)27-9-5-3-7-23(25)27/h2-9,19-21H,10-18H2,1H3,(H,32,37,38) QKXPAKQCFJVAFI-UHFFFAOYSA-N 50052041 18-(4-methylhexahydro-1-pyrazinylmethyl)-(18S)-17-oxa-4,14,21-triazahexacyclo[19.6.1.17,14.02,6.08,13.022,27]nonacosa-1(28),2(6),7(29),8(13),9,11,22(27),23,25-nonaene-3,5-dione::CHEMBL91959 Protein kinase C eta type Homo sapiens 2000 ChEMBL 10.1021/jm950588y 10.7270/Q25H7FBV 8709095 Jirousek, MR; Gillig, JR; Gonzalez, CM; Heath, WF; McDonald, JH; Neel, DA; Rito, CJ; Singh, U; Stramm, LE; Melikian-Badalian, A; Baevsky, M; Ballas, LM; Hall, SE; Winneroski, LL; Faul, MM 9/10/1996 11/10/2009 Eli Lilly http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50052041 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=605&target=Protein+kinase+C+eta+type&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50052041&enzyme=Protein+kinase+C+eta+type&column=ki&startPg=0&Increment=50&submit=Search 10768377 103948966 CHEMBL91959 1 MSSGTMKFNGYLRVRIGEAVGLQPTRWSLRHSLFKKGHQLLDPYLTVSVDQVRVGQTSTKQKTNKPTYNEEFCANVTDGGHLELAVFHETPLGYDHFVANCTLQFQELLRTTGASDTFEGWVDLEPEGKVFVVITLTGSFTEATLQRDRIFKHFTRKRQRAMRRRVHQINGHKFMATYLRQPTYCSHCREFIWGVFGKQGYQCQVCTCVVHKRCHHLIVTACTCQNNINKVDSKIAEQRFGINIPHKFSIHNYKVPTFCDHCGSLLWGIMRQGLQCKICKMNVHIRCQANVAPNCGVNAVELAKTLAGMGLQPGNISPTSKLVSRSTLRRQGKESSKEGNGIGVNSSNRLGIDNFEFIRVLGKGSFGKVMLARVKETGDLYAVKVLKKDVILQDDDVECTMTEKRILSLARNHPFLTQLFCCFQTPDRLFFVMEFVNGGDLMFHIQKSRRFDEARARFYAAEIISALMFLHDKGIIYRDLKLDNVLLDHEGHCKLADFGMCKEGICNGVTTATFCGTPDYIAPEILQEMLYGPAVDWWAMGVLLYEMLCGHAPFEAENEDDLFEAILNDEVVYPTWLHEDATGILKSFMTKNPTMRLGSLTQGGEHAILRHPFFKEIDWAQLNHRQIEPPFRPRIKSREDVSNFDPDFIKEEPVLTPIDEGHLPMINQDEFRNFSYVSPELQP 2FK9 Protein kinase C eta type KPCL_HUMAN P24723 B4DJN5 Q16246 Q8NE03 50042833 C[C@@]12[C@@H]([C@@H](C[C@@H](O1)n3c4ccccc4c5c3c6n2c7ccccc7c6c8c5C(=O)NC8)NC)OC InChI=1S/C28H26N4O3/c1-28-26(34-3)17(29-2)12-20(35-28)31-18-10-6-4-8-14(18)22-23-16(13-30-27(23)33)21-15-9-5-7-11-19(15)32(28)25(21)24(22)31/h4-11,17,20,26,29H,12-13H2,1-3H3,(H,30,33) HKSZLNNOFSGOKW-UHFFFAOYSA-N 2579 CHEMBL388978::Staurosporine, 8::Staurosporin, 4::(2S,3R,4R,6R)-3-methoxy-2-methyl-4-(methylamino)-29-oxa-1,7,17-triazaoctacyclo[12.12.2.1^{2,6}.0^{7,28}.0^{8,13}.0^{15,19}.0^{20,27}.0^{21,26}]nonacosa-8(13),9,11,14(28),15(19),20(27),21(26),22,24-nonaen-16-one::Staurosporine::US9206188, Staurosporine::US9226923, Staurosporine::US20240002365, Compound staurosporine::US11958831, Example Staurosporine::US20240254124, Compound Staurosporine::US20240309004, Compound STAUROSPORINE::US12350272, Compound Staurosporine::US12398142, Compound Staurosporine::US12410173, Compound Staurosporine Proto-oncogene tyrosine-protein kinase Src Homo sapiens 1 ChEMBL 10.1021/jm950588y 10.7270/Q25H7FBV 8709095 Jirousek, MR; Gillig, JR; Gonzalez, CM; Heath, WF; McDonald, JH; Neel, DA; Rito, CJ; Singh, U; Stramm, LE; Melikian-Badalian, A; Baevsky, M; Ballas, LM; Hall, SE; Winneroski, LL; Faul, MM 9/10/1996 11/10/2009 Eli Lilly http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=2579 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=13&target=Proto-oncogene+tyrosine-protein+kinase+Src&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=2579&enzyme=Proto-oncogene+tyrosine-protein+kinase+Src&column=ki&startPg=0&Increment=50&submit=Search STO 44259 8032349 CHEMBL388978 C02079 1 MGSNKSKPKDASQRRRSLEPAENVHGAGGGAFPASQTPSKPASADGHRGPSAAFAPAAAEPKLFGGFNSSDTVTSPQRAGPLAGGVTTFVALYDYESRTETDLSFKKGERLQIVNNTEGDWWLAHSLSTGQTGYIPSNYVAPSDSIQAEEWYFGKITRRESERLLLNAENPRGTFLVRESETTKGAYCLSVSDFDNAKGLNVKHYKIRKLDSGGFYITSRTQFNSLQQLVAYYSKHADGLCHRLTTVCPTSKPQTQGLAKDAWEIPRESLRLEVKLGQGCFGEVWMGTWNGTTRVAIKTLKPGTMSPEAFLQEAQVMKKLRHEKLVQLYAVVSEEPIYIVTEYMSKGSLLDFLKGETGKYLRLPQLVDMAAQIASGMAYVERMNYVHRDLRAANILVGENLVCKVADFGLARLIEDNEYTARQGAKFPIKWTAPEAALYGRFTIKSDVWSFGILLTELTTKGRVPYPGMVNREVLDQVERGYRMPCPPECPESLHDLMCQCWRKEPEERPTFEYLQAFLEDYFTSTEPQYQPGENL 8JN9,8JN8,2H8H,2SRC,1Y57,1FMK,2PTK,9NS0,8JF3,6ATE,4MXO,4MXX,2BDJ,2BDF,8HAQ,6E6E,1YI6 Proto-oncogene tyrosine-protein kinase Src SRC_HUMAN P12931 E1P5V4 Q76P87 Q86VB9 Q9H5A8 50042834 O=C1NC(=O)C2=C1c1cn(CCO[C@H](CNCc3ccccc3)CCn3cc2c2ccccc32)c2ccccc12 |c:5| InChI=1S/C33H30N4O3/c38-32-30-26-20-36(28-12-6-4-10-24(26)28)15-14-23(19-34-18-22-8-2-1-3-9-22)40-17-16-37-21-27(31(30)33(39)35-32)25-11-5-7-13-29(25)37/h1-13,20-21,23,34H,14-19H2,(H,35,38,39) RIXHNSFDUIBDSB-UHFFFAOYSA-N 50052040 18-benzylaminomethyl-(18S)-17-oxa-4,14,21-triazahexacyclo[19.6.1.17,14.02,6.08,13.022,27]nonacosa-1(28),2(6),7(29),8(13),9,11,22(27),23,25-nonaene-3,5-dione::CHEMBL328229 Protein kinase C eta type Homo sapiens 2500 ChEMBL 10.1021/jm950588y 10.7270/Q25H7FBV 8709095 Jirousek, MR; Gillig, JR; Gonzalez, CM; Heath, WF; McDonald, JH; Neel, DA; Rito, CJ; Singh, U; Stramm, LE; Melikian-Badalian, A; Baevsky, M; Ballas, LM; Hall, SE; Winneroski, LL; Faul, MM 9/10/1996 11/10/2009 Eli Lilly http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50052040 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=605&target=Protein+kinase+C+eta+type&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50052040&enzyme=Protein+kinase+C+eta+type&column=ki&startPg=0&Increment=50&submit=Search 10768554 103948965 CHEMBL328229 1 MSSGTMKFNGYLRVRIGEAVGLQPTRWSLRHSLFKKGHQLLDPYLTVSVDQVRVGQTSTKQKTNKPTYNEEFCANVTDGGHLELAVFHETPLGYDHFVANCTLQFQELLRTTGASDTFEGWVDLEPEGKVFVVITLTGSFTEATLQRDRIFKHFTRKRQRAMRRRVHQINGHKFMATYLRQPTYCSHCREFIWGVFGKQGYQCQVCTCVVHKRCHHLIVTACTCQNNINKVDSKIAEQRFGINIPHKFSIHNYKVPTFCDHCGSLLWGIMRQGLQCKICKMNVHIRCQANVAPNCGVNAVELAKTLAGMGLQPGNISPTSKLVSRSTLRRQGKESSKEGNGIGVNSSNRLGIDNFEFIRVLGKGSFGKVMLARVKETGDLYAVKVLKKDVILQDDDVECTMTEKRILSLARNHPFLTQLFCCFQTPDRLFFVMEFVNGGDLMFHIQKSRRFDEARARFYAAEIISALMFLHDKGIIYRDLKLDNVLLDHEGHCKLADFGMCKEGICNGVTTATFCGTPDYIAPEILQEMLYGPAVDWWAMGVLLYEMLCGHAPFEAENEDDLFEAILNDEVVYPTWLHEDATGILKSFMTKNPTMRLGSLTQGGEHAILRHPFFKEIDWAQLNHRQIEPPFRPRIKSREDVSNFDPDFIKEEPVLTPIDEGHLPMINQDEFRNFSYVSPELQP 2FK9 Protein kinase C eta type KPCL_HUMAN P24723 B4DJN5 Q16246 Q8NE03 50042835 O=C1NC(=O)C2=C1c1cn(CCO[C@H](CNCc3ccccc3)CCn3cc2c2ccccc32)c2ccccc12 |c:5| InChI=1S/C33H30N4O3/c38-32-30-26-20-36(28-12-6-4-10-24(26)28)15-14-23(19-34-18-22-8-2-1-3-9-22)40-17-16-37-21-27(31(30)33(39)35-32)25-11-5-7-13-29(25)37/h1-13,20-21,23,34H,14-19H2,(H,35,38,39) RIXHNSFDUIBDSB-UHFFFAOYSA-N 50052040 18-benzylaminomethyl-(18S)-17-oxa-4,14,21-triazahexacyclo[19.6.1.17,14.02,6.08,13.022,27]nonacosa-1(28),2(6),7(29),8(13),9,11,22(27),23,25-nonaene-3,5-dione::CHEMBL328229 Protein kinase C beta type Homo sapiens 310 ChEMBL 10.1021/jm950588y 10.7270/Q25H7FBV 8709095 Jirousek, MR; Gillig, JR; Gonzalez, CM; Heath, WF; McDonald, JH; Neel, DA; Rito, CJ; Singh, U; Stramm, LE; Melikian-Badalian, A; Baevsky, M; Ballas, LM; Hall, SE; Winneroski, LL; Faul, MM 9/10/1996 11/10/2009 Eli Lilly http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50052040 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=600&target=Protein+kinase+C+beta+type&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50052040&enzyme=Protein+kinase+C+beta+type&column=ki&startPg=0&Increment=50&submit=Search 10768554 103948965 CHEMBL328229 1 MADPAAGPPPSEGEESTVRFARKGALRQKNVHEVKNHKFTARFFKQPTFCSHCTDFIWGFGKQGFQCQVCCFVVHKRCHEFVTFSCPGADKGPASDDPRSKHKFKIHTYSSPTFCDHCGSLLYGLIHQGMKCDTCMMNVHKRCVMNVPSLCGTDHTERRGRIYIQAHIDRDVLIVLVRDAKNLVPMDPNGLSDPYVKLKLIPDPKSESKQKTKTIKCSLNPEWNETFRFQLKESDKDRRLSVEIWDWDLTSRNDFMGSLSFGISELQKASVDGWFKLLSQEEGEYFNVPVPPEGSEANEELRQKFERAKISQGTKVPEEKTTNTVSKFDNNGNRDRMKLTDFNFLMVLGKGSFGKVMLSERKGTDELYAVKILKKDVVIQDDDVECTMVEKRVLALPGKPPFLTQLHSCFQTMDRLYFVMEYVNGGDLMYHIQQVGRFKEPHAVFYAAEIAIGLFFLQSKGIIYRDLKLDNVMLDSEGHIKIADFGMCKENIWDGVTTKTFCGTPDYIAPEIIAYQPYGKSVDWWAFGVLLYEMLAGQAPFEGEDEDELFQSIMEHNVAYPKSMSKEAVAICKGLMTKHPGKRLGCGPEGERDIKEHAFFRYIDWEKLERKEIQPPYKPKARDKRDTSNFDKEFTRQPVELTPTDKLFIMNLDQNEFAGFSYTNPEFVINV 8SE4,8SE3,8SE2,3PFQ,9C5F,1A25 Protein kinase C beta type KPCB_HUMAN P05771 C5IFJ8 D3DWF5 O43744 P05127 Q15138 Q93060 Q9UE49 Q9UE50 Q9UEH8 Q9UJ30 Q9UJ33 50042836 C[C@@]12[C@@H]([C@@H](C[C@@H](O1)n3c4ccccc4c5c3c6n2c7ccccc7c6c8c5C(=O)NC8)NC)OC InChI=1S/C28H26N4O3/c1-28-26(34-3)17(29-2)12-20(35-28)31-18-10-6-4-8-14(18)22-23-16(13-30-27(23)33)21-15-9-5-7-11-19(15)32(28)25(21)24(22)31/h4-11,17,20,26,29H,12-13H2,1-3H3,(H,30,33) HKSZLNNOFSGOKW-UHFFFAOYSA-N 2579 CHEMBL388978::Staurosporine, 8::Staurosporin, 4::(2S,3R,4R,6R)-3-methoxy-2-methyl-4-(methylamino)-29-oxa-1,7,17-triazaoctacyclo[12.12.2.1^{2,6}.0^{7,28}.0^{8,13}.0^{15,19}.0^{20,27}.0^{21,26}]nonacosa-8(13),9,11,14(28),15(19),20(27),21(26),22,24-nonaen-16-one::Staurosporine::US9206188, Staurosporine::US9226923, Staurosporine::US20240002365, Compound staurosporine::US11958831, Example Staurosporine::US20240254124, Compound Staurosporine::US20240309004, Compound STAUROSPORINE::US12350272, Compound Staurosporine::US12398142, Compound Staurosporine::US12410173, Compound Staurosporine Protein kinase C delta type Homo sapiens 28 ChEMBL 10.1021/jm950588y 10.7270/Q25H7FBV 8709095 Jirousek, MR; Gillig, JR; Gonzalez, CM; Heath, WF; McDonald, JH; Neel, DA; Rito, CJ; Singh, U; Stramm, LE; Melikian-Badalian, A; Baevsky, M; Ballas, LM; Hall, SE; Winneroski, LL; Faul, MM 9/10/1996 11/10/2009 Eli Lilly http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=2579 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=603&target=Protein+kinase+C+delta+type&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=2579&enzyme=Protein+kinase+C+delta+type&column=ki&startPg=0&Increment=50&submit=Search STO 44259 8032349 CHEMBL388978 C02079 1 MAPFLRIAFNSYELGSLQAEDEANQPFCAVKMKEALSTERGKTLVQKKPTMYPEWKSTFDAHIYEGRVIQIVLMRAAEEPVSEVTVGVSVLAERCKKNNGKAEFWLDLQPQAKVLMSVQYFLEDVDCKQSMRSEDEAKFPTMNRRGAIKQAKIHYIKNHEFIATFFGQPTFCSVCKDFVWGLNKQGYKCRQCNAAIHKKCIDKIIGRCTGTAANSRDTIFQKERFNIDMPHRFKVHNYMSPTFCDHCGSLLWGLVKQGLKCEDCGMNVHHKCREKVANLCGINQKLLAEALNQVTQRASRRSDSASSEPVGIYQGFEKKTGVAGEDMQDNSGTYGKIWEGSSKCNINNFIFHKVLGKGSFGKVLLGELKGRGEYFAIKALKKDVVLIDDDVECTMVEKRVLTLAAENPFLTHLICTFQTKDHLFFVMEFLNGGDLMYHIQDKGRFELYRATFYAAEIMCGLQFLHSKGIIYRDLKLDNVLLDRDGHIKIADFGMCKENIFGESRASTFCGTPDYIAPEILQGLKYTFSVDWWSFGVLLYEMLIGQSPFHGDDEDELFESIRVDTPHYPRWITKESKDILEKLFEREPTKRLGVTGNIKIHPFFKTINWTLLEKRRLEPPFRPKVKSPRDYSNFDQEFLNEKARLSYSDKNLIDSMDQSAFAGFSFVNPKFEHLLED 1YRK Protein kinase C delta type KPCD_HUMAN Q05655 B0KZ81 B2R834 Q15144 Q86XJ6 50042837 OC[C@@H]1CCn2cc(C3=C(C(=O)NC3=O)c3cn(CCO1)c1ccccc31)c1ccccc21 |t:8| InChI=1S/C26H23N3O4/c30-15-16-9-10-28-13-19(17-5-1-3-7-21(17)28)23-24(26(32)27-25(23)31)20-14-29(11-12-33-16)22-8-4-2-6-18(20)22/h1-8,13-14,16,30H,9-12,15H2,(H,27,31,32) BGVKOUSMQGMSDY-UHFFFAOYSA-N 50052039 18-hydroxymethyl-(18S)-17-oxa-4,14,21-triazahexacyclo[19.6.1.17,14.02,6.08,13.022,27]nonacosa-1(28),2(6),7(29),8(13),9,11,22(27),23,25-nonaene-3,5-dione::LY-326449::CHEMBL292495 Protein kinase C alpha type Homo sapiens 720 ChEMBL 10.1021/jm950588y 10.7270/Q25H7FBV 8709095 Jirousek, MR; Gillig, JR; Gonzalez, CM; Heath, WF; McDonald, JH; Neel, DA; Rito, CJ; Singh, U; Stramm, LE; Melikian-Badalian, A; Baevsky, M; Ballas, LM; Hall, SE; Winneroski, LL; Faul, MM 9/10/1996 11/10/2009 Eli Lilly http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50052039 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=599&target=Protein+kinase+C+alpha+type&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50052039&enzyme=Protein+kinase+C+alpha+type&column=ki&startPg=0&Increment=50&submit=Search 10455969 103948964 CHEMBL292495 1 MADVFPGNDSTASQDVANRFARKGALRQKNVHEVKDHKFIARFFKQPTFCSHCTDFIWGFGKQGFQCQVCCFVVHKRCHEFVTFSCPGADKGPDTDDPRSKHKFKIHTYGSPTFCDHCGSLLYGLIHQGMKCDTCDMNVHKQCVINVPSLCGMDHTEKRGRIYLKAEVADEKLHVTVRDAKNLIPMDPNGLSDPYVKLKLIPDPKNESKQKTKTIRSTLNPQWNESFTFKLKPSDKDRRLSVEIWDWDRTTRNDFMGSLSFGVSELMKMPASGWYKLLNQEEGEYYNVPIPEGDEEGNMELRQKFEKAKLGPAGNKVISPSEDRKQPSNNLDRVKLTDFNFLMVLGKGSFGKVMLADRKGTEELYAIKILKKDVVIQDDDVECTMVEKRVLALLDKPPFLTQLHSCFQTVDRLYFVMEYVNGGDLMYHIQQVGKFKEPQAVFYAAEISIGLFFLHKRGIIYRDLKLDNVMLDSEGHIKIADFGMCKEHMMDGVTTRTFCGTPDYIAPEIIAYQPYGKSVDWWAYGVLLYEMLAGQPPFDGEDEDELFQSIMEHNVSYPKSLSKEAVSVCKGLMTKHPAKRLGCGPEGERDVREHAFFRRIDWEKLENREIQPPFKPKVCGKGAENFDKFFTRGQPVLTPPDQLVIANIDQSDFEGFSYVNPQFVHPILQSAV 4RA4,4DNL Protein kinase C alpha type KPCA_HUMAN P17252 B5BU22 Q15137 Q32M72 Q96RE4 50042838 CN1CCN(C[C@@H]2CCn3cc(C4=C(C(=O)NC4=O)c4cn(CCO2)c2ccccc42)c2ccccc32)CC1 |t:12| InChI=1S/C31H33N5O3/c1-33-12-14-34(15-13-33)18-21-10-11-35-19-24(22-6-2-4-8-26(22)35)28-29(31(38)32-30(28)37)25-20-36(16-17-39-21)27-9-5-3-7-23(25)27/h2-9,19-21H,10-18H2,1H3,(H,32,37,38) QKXPAKQCFJVAFI-UHFFFAOYSA-N 50052041 18-(4-methylhexahydro-1-pyrazinylmethyl)-(18S)-17-oxa-4,14,21-triazahexacyclo[19.6.1.17,14.02,6.08,13.022,27]nonacosa-1(28),2(6),7(29),8(13),9,11,22(27),23,25-nonaene-3,5-dione::CHEMBL91959 Protein kinase C beta type Homo sapiens 30 ChEMBL 10.1021/jm950588y 10.7270/Q25H7FBV 8709095 Jirousek, MR; Gillig, JR; Gonzalez, CM; Heath, WF; McDonald, JH; Neel, DA; Rito, CJ; Singh, U; Stramm, LE; Melikian-Badalian, A; Baevsky, M; Ballas, LM; Hall, SE; Winneroski, LL; Faul, MM 9/10/1996 11/10/2009 Eli Lilly http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50052041 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=600&target=Protein+kinase+C+beta+type&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50052041&enzyme=Protein+kinase+C+beta+type&column=ki&startPg=0&Increment=50&submit=Search 10768377 103948966 CHEMBL91959 1 MADPAAGPPPSEGEESTVRFARKGALRQKNVHEVKNHKFTARFFKQPTFCSHCTDFIWGFGKQGFQCQVCCFVVHKRCHEFVTFSCPGADKGPASDDPRSKHKFKIHTYSSPTFCDHCGSLLYGLIHQGMKCDTCMMNVHKRCVMNVPSLCGTDHTERRGRIYIQAHIDRDVLIVLVRDAKNLVPMDPNGLSDPYVKLKLIPDPKSESKQKTKTIKCSLNPEWNETFRFQLKESDKDRRLSVEIWDWDLTSRNDFMGSLSFGISELQKASVDGWFKLLSQEEGEYFNVPVPPEGSEANEELRQKFERAKISQGTKVPEEKTTNTVSKFDNNGNRDRMKLTDFNFLMVLGKGSFGKVMLSERKGTDELYAVKILKKDVVIQDDDVECTMVEKRVLALPGKPPFLTQLHSCFQTMDRLYFVMEYVNGGDLMYHIQQVGRFKEPHAVFYAAEIAIGLFFLQSKGIIYRDLKLDNVMLDSEGHIKIADFGMCKENIWDGVTTKTFCGTPDYIAPEIIAYQPYGKSVDWWAFGVLLYEMLAGQAPFEGEDEDELFQSIMEHNVAYPKSMSKEAVAICKGLMTKHPGKRLGCGPEGERDIKEHAFFRYIDWEKLERKEIQPPYKPKARDKRDTSNFDKEFTRQPVELTPTDKLFIMNLDQNEFAGFSYTNPEFVINV 8SE4,8SE3,8SE2,3PFQ,9C5F,1A25 Protein kinase C beta type KPCB_HUMAN P05771 C5IFJ8 D3DWF5 O43744 P05127 Q15138 Q93060 Q9UE49 Q9UE50 Q9UEH8 Q9UJ30 Q9UJ33 50042839 O=C1NC(=O)C2=C1c1cn(CCO[C@H](CN3CCCC3)CCn3cc2c2ccccc32)c2ccccc12 |c:5| InChI=1S/C30H30N4O3/c35-29-27-23-18-33(25-9-3-1-7-21(23)25)14-11-20(17-32-12-5-6-13-32)37-16-15-34-19-24(28(27)30(36)31-29)22-8-2-4-10-26(22)34/h1-4,7-10,18-20H,5-6,11-17H2,(H,31,35,36) WORLFHNBHSSAJQ-UHFFFAOYSA-N 50052038 18-tetrahydro-1H-1-pyrrolylmethyl-(18S)-17-oxa-4,14,21-triazahexacyclo[19.6.1.17,14.02,6.08,13.022,27]nonacosa-1(28),2(6),7(29),8(13),9,11,22(27),23,25-nonaene-3,5-dione::CHEMBL419866 Protein kinase C alpha type Homo sapiens 3500 ChEMBL 10.1021/jm950588y 10.7270/Q25H7FBV 8709095 Jirousek, MR; Gillig, JR; Gonzalez, CM; Heath, WF; McDonald, JH; Neel, DA; Rito, CJ; Singh, U; Stramm, LE; Melikian-Badalian, A; Baevsky, M; Ballas, LM; Hall, SE; Winneroski, LL; Faul, MM 9/10/1996 11/10/2009 Eli Lilly http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50052038 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=599&target=Protein+kinase+C+alpha+type&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50052038&enzyme=Protein+kinase+C+alpha+type&column=ki&startPg=0&Increment=50&submit=Search 11799388 103948963 CHEMBL419866 1 MADVFPGNDSTASQDVANRFARKGALRQKNVHEVKDHKFIARFFKQPTFCSHCTDFIWGFGKQGFQCQVCCFVVHKRCHEFVTFSCPGADKGPDTDDPRSKHKFKIHTYGSPTFCDHCGSLLYGLIHQGMKCDTCDMNVHKQCVINVPSLCGMDHTEKRGRIYLKAEVADEKLHVTVRDAKNLIPMDPNGLSDPYVKLKLIPDPKNESKQKTKTIRSTLNPQWNESFTFKLKPSDKDRRLSVEIWDWDRTTRNDFMGSLSFGVSELMKMPASGWYKLLNQEEGEYYNVPIPEGDEEGNMELRQKFEKAKLGPAGNKVISPSEDRKQPSNNLDRVKLTDFNFLMVLGKGSFGKVMLADRKGTEELYAIKILKKDVVIQDDDVECTMVEKRVLALLDKPPFLTQLHSCFQTVDRLYFVMEYVNGGDLMYHIQQVGKFKEPQAVFYAAEISIGLFFLHKRGIIYRDLKLDNVMLDSEGHIKIADFGMCKEHMMDGVTTRTFCGTPDYIAPEIIAYQPYGKSVDWWAYGVLLYEMLAGQPPFDGEDEDELFQSIMEHNVSYPKSLSKEAVSVCKGLMTKHPAKRLGCGPEGERDVREHAFFRRIDWEKLENREIQPPFKPKVCGKGAENFDKFFTRGQPVLTPPDQLVIANIDQSDFEGFSYVNPQFVHPILQSAV 4RA4,4DNL Protein kinase C alpha type KPCA_HUMAN P17252 B5BU22 Q15137 Q32M72 Q96RE4 50042840 C[C@@]12[C@@H]([C@@H](C[C@@H](O1)n3c4ccccc4c5c3c6n2c7ccccc7c6c8c5C(=O)NC8)NC)OC InChI=1S/C28H26N4O3/c1-28-26(34-3)17(29-2)12-20(35-28)31-18-10-6-4-8-14(18)22-23-16(13-30-27(23)33)21-15-9-5-7-11-19(15)32(28)25(21)24(22)31/h4-11,17,20,26,29H,12-13H2,1-3H3,(H,30,33) HKSZLNNOFSGOKW-UHFFFAOYSA-N 2579 CHEMBL388978::Staurosporine, 8::Staurosporin, 4::(2S,3R,4R,6R)-3-methoxy-2-methyl-4-(methylamino)-29-oxa-1,7,17-triazaoctacyclo[12.12.2.1^{2,6}.0^{7,28}.0^{8,13}.0^{15,19}.0^{20,27}.0^{21,26}]nonacosa-8(13),9,11,14(28),15(19),20(27),21(26),22,24-nonaen-16-one::Staurosporine::US9206188, Staurosporine::US9226923, Staurosporine::US20240002365, Compound staurosporine::US11958831, Example Staurosporine::US20240254124, Compound Staurosporine::US20240309004, Compound STAUROSPORINE::US12350272, Compound Staurosporine::US12398142, Compound Staurosporine::US12410173, Compound Staurosporine Protein kinase C epsilon type Homo sapiens 18 ChEMBL 10.1021/jm950588y 10.7270/Q25H7FBV 8709095 Jirousek, MR; Gillig, JR; Gonzalez, CM; Heath, WF; McDonald, JH; Neel, DA; Rito, CJ; Singh, U; Stramm, LE; Melikian-Badalian, A; Baevsky, M; Ballas, LM; Hall, SE; Winneroski, LL; Faul, MM 9/10/1996 11/10/2009 Eli Lilly http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=2579 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=604&target=Protein+kinase+C+epsilon+type&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=2579&enzyme=Protein+kinase+C+epsilon+type&column=ki&startPg=0&Increment=50&submit=Search STO 44259 8032349 CHEMBL388978 C02079 1 MVVFNGLLKIKICEAVSLKPTAWSLRHAVGPRPQTFLLDPYIALNVDDSRIGQTATKQKTNSPAWHDEFVTDVCNGRKIELAVFHDAPIGYDDFVANCTIQFEELLQNGSRHFEDWIDLEPEGRVYVIIDLSGSSGEAPKDNEERVFRERMRPRKRQGAVRRRVHQVNGHKFMATYLRQPTYCSHCRDFIWGVIGKQGYQCQVCTCVVHKRCHELIITKCAGLKKQETPDQVGSQRFSVNMPHKFGIHNYKVPTFCDHCGSLLWGLLRQGLQCKVCKMNVHRRCETNVAPNCGVDARGIAKVLADLGVTPDKITNSGQRRKKLIAGAESPQPASGSSPSEEDRSKSAPTSPCDQEIKELENNIRKALSFDNRGEEHRAASSPDGQLMSPGENGEVRQGQAKRLGLDEFNFIKVLGKGSFGKVMLAELKGKDEVYAVKVLKKDVILQDDDVDCTMTEKRILALARKHPYLTQLYCCFQTKDRLFFVMEYVNGGDLMFQIQRSRKFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILLDAEGHCKLADFGMCKEGILNGVTTTTFCGTPDYIAPEILQELEYGPSVDWWALGVLMYEMMAGQPPFEADNEDDLFESILHDDVLYPVWLSKEAVSILKAFMTKNPHKRLGCVASQNGEDAIKQHPFFKEIDWVLLEQKKIKPPFKPRIKTKRDVNNFDQDFTREEPVLTLVDEAIVKQINQEEFKGFSYFGEDLMP Protein kinase C epsilon type KPCE_HUMAN Q02156 B0LPH7 Q32MQ3 Q53SL4 Q53SM5 Q9UE81 50042841 C[C@@]12[C@@H]([C@@H](C[C@@H](O1)n3c4ccccc4c5c3c6n2c7ccccc7c6c8c5C(=O)NC8)NC)OC InChI=1S/C28H26N4O3/c1-28-26(34-3)17(29-2)12-20(35-28)31-18-10-6-4-8-14(18)22-23-16(13-30-27(23)33)21-15-9-5-7-11-19(15)32(28)25(21)24(22)31/h4-11,17,20,26,29H,12-13H2,1-3H3,(H,30,33) HKSZLNNOFSGOKW-UHFFFAOYSA-N 2579 CHEMBL388978::Staurosporine, 8::Staurosporin, 4::(2S,3R,4R,6R)-3-methoxy-2-methyl-4-(methylamino)-29-oxa-1,7,17-triazaoctacyclo[12.12.2.1^{2,6}.0^{7,28}.0^{8,13}.0^{15,19}.0^{20,27}.0^{21,26}]nonacosa-8(13),9,11,14(28),15(19),20(27),21(26),22,24-nonaen-16-one::Staurosporine::US9206188, Staurosporine::US9226923, Staurosporine::US20240002365, Compound staurosporine::US11958831, Example Staurosporine::US20240254124, Compound Staurosporine::US20240309004, Compound STAUROSPORINE::US12350272, Compound Staurosporine::US12398142, Compound Staurosporine::US12410173, Compound Staurosporine Protein kinase C alpha type Homo sapiens 45 ChEMBL 10.1021/jm950588y 10.7270/Q25H7FBV 8709095 Jirousek, MR; Gillig, JR; Gonzalez, CM; Heath, WF; McDonald, JH; Neel, DA; Rito, CJ; Singh, U; Stramm, LE; Melikian-Badalian, A; Baevsky, M; Ballas, LM; Hall, SE; Winneroski, LL; Faul, MM 9/10/1996 11/10/2009 Eli Lilly http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=2579 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=599&target=Protein+kinase+C+alpha+type&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=2579&enzyme=Protein+kinase+C+alpha+type&column=ki&startPg=0&Increment=50&submit=Search STO 44259 8032349 CHEMBL388978 C02079 1 MADVFPGNDSTASQDVANRFARKGALRQKNVHEVKDHKFIARFFKQPTFCSHCTDFIWGFGKQGFQCQVCCFVVHKRCHEFVTFSCPGADKGPDTDDPRSKHKFKIHTYGSPTFCDHCGSLLYGLIHQGMKCDTCDMNVHKQCVINVPSLCGMDHTEKRGRIYLKAEVADEKLHVTVRDAKNLIPMDPNGLSDPYVKLKLIPDPKNESKQKTKTIRSTLNPQWNESFTFKLKPSDKDRRLSVEIWDWDRTTRNDFMGSLSFGVSELMKMPASGWYKLLNQEEGEYYNVPIPEGDEEGNMELRQKFEKAKLGPAGNKVISPSEDRKQPSNNLDRVKLTDFNFLMVLGKGSFGKVMLADRKGTEELYAIKILKKDVVIQDDDVECTMVEKRVLALLDKPPFLTQLHSCFQTVDRLYFVMEYVNGGDLMYHIQQVGKFKEPQAVFYAAEISIGLFFLHKRGIIYRDLKLDNVMLDSEGHIKIADFGMCKEHMMDGVTTRTFCGTPDYIAPEIIAYQPYGKSVDWWAYGVLLYEMLAGQPPFDGEDEDELFQSIMEHNVSYPKSLSKEAVSVCKGLMTKHPAKRLGCGPEGERDVREHAFFRRIDWEKLENREIQPPFKPKVCGKGAENFDKFFTRGQPVLTPPDQLVIANIDQSDFEGFSYVNPQFVHPILQSAV 4RA4,4DNL Protein kinase C alpha type KPCA_HUMAN P17252 B5BU22 Q15137 Q32M72 Q96RE4 50042842 NC[C@@H]1CCn2cc(C3=C(C(=O)NC3=O)c3cn(CCO1)c1ccccc31)c1ccccc21 |t:8| InChI=1S/C26H24N4O3/c27-13-16-9-10-29-14-19(17-5-1-3-7-21(17)29)23-24(26(32)28-25(23)31)20-15-30(11-12-33-16)22-8-4-2-6-18(20)22/h1-8,14-16H,9-13,27H2,(H,28,31,32) JPLUPRIZLHXUPQ-UHFFFAOYSA-N 50052037 18-aminomethyl-(18S)-17-oxa-4,14,21-triazahexacyclo[19.6.1.17,14.02,6.08,13.022,27]nonacosa-1(28),2(6),7(29),8(13),9,11,22(27),23,25-nonaene-3,5-dione::CHEMBL316239 Protein kinase C beta type Homo sapiens 33 ChEMBL 10.1021/jm950588y 10.7270/Q25H7FBV 8709095 Jirousek, MR; Gillig, JR; Gonzalez, CM; Heath, WF; McDonald, JH; Neel, DA; Rito, CJ; Singh, U; Stramm, LE; Melikian-Badalian, A; Baevsky, M; Ballas, LM; Hall, SE; Winneroski, LL; Faul, MM 9/10/1996 11/10/2009 Eli Lilly http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50052037 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=600&target=Protein+kinase+C+beta+type&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50052037&enzyme=Protein+kinase+C+beta+type&column=ki&startPg=0&Increment=50&submit=Search 10527068 103948962 CHEMBL316239 1 MADPAAGPPPSEGEESTVRFARKGALRQKNVHEVKNHKFTARFFKQPTFCSHCTDFIWGFGKQGFQCQVCCFVVHKRCHEFVTFSCPGADKGPASDDPRSKHKFKIHTYSSPTFCDHCGSLLYGLIHQGMKCDTCMMNVHKRCVMNVPSLCGTDHTERRGRIYIQAHIDRDVLIVLVRDAKNLVPMDPNGLSDPYVKLKLIPDPKSESKQKTKTIKCSLNPEWNETFRFQLKESDKDRRLSVEIWDWDLTSRNDFMGSLSFGISELQKASVDGWFKLLSQEEGEYFNVPVPPEGSEANEELRQKFERAKISQGTKVPEEKTTNTVSKFDNNGNRDRMKLTDFNFLMVLGKGSFGKVMLSERKGTDELYAVKILKKDVVIQDDDVECTMVEKRVLALPGKPPFLTQLHSCFQTMDRLYFVMEYVNGGDLMYHIQQVGRFKEPHAVFYAAEIAIGLFFLQSKGIIYRDLKLDNVMLDSEGHIKIADFGMCKENIWDGVTTKTFCGTPDYIAPEIIAYQPYGKSVDWWAFGVLLYEMLAGQAPFEGEDEDELFQSIMEHNVAYPKSMSKEAVAICKGLMTKHPGKRLGCGPEGERDIKEHAFFRYIDWEKLERKEIQPPYKPKARDKRDTSNFDKEFTRQPVELTPTDKLFIMNLDQNEFAGFSYTNPEFVINV 8SE4,8SE3,8SE2,3PFQ,9C5F,1A25 Protein kinase C beta type KPCB_HUMAN P05771 C5IFJ8 D3DWF5 O43744 P05127 Q15138 Q93060 Q9UE49 Q9UE50 Q9UEH8 Q9UJ30 Q9UJ33 50042843 CNC[C@@H]1CCn2cc(C3=C(C(=O)NC3=O)c3cn(CCO1)c1ccccc31)c1ccccc21 |t:9| InChI=1S/C27H26N4O3/c1-28-14-17-10-11-30-15-20(18-6-2-4-8-22(18)30)24-25(27(33)29-26(24)32)21-16-31(12-13-34-17)23-9-5-3-7-19(21)23/h2-9,15-17,28H,10-14H2,1H3,(H,29,32,33) ZEYTZKVCOZMUKL-UHFFFAOYSA-N 50052034 18-methylaminomethyl-(18S)-17-oxa-4,14,21-triazahexacyclo[19.6.1.17,14.02,6.08,13.022,27]nonacosa-1(28),2(6),7(29),8(13),9,11,22(27),23,25-nonaene-3,5-dione::CHEMBL311543 Protein kinase C beta type Homo sapiens 5 ChEMBL 10.1021/jm950588y 10.7270/Q25H7FBV 8709095 Jirousek, MR; Gillig, JR; Gonzalez, CM; Heath, WF; McDonald, JH; Neel, DA; Rito, CJ; Singh, U; Stramm, LE; Melikian-Badalian, A; Baevsky, M; Ballas, LM; Hall, SE; Winneroski, LL; Faul, MM 9/10/1996 11/10/2009 Eli Lilly http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50052034 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=600&target=Protein+kinase+C+beta+type&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50052034&enzyme=Protein+kinase+C+beta+type&column=ki&startPg=0&Increment=50&submit=Search 10671412 103948959 CHEMBL311543 1 MADPAAGPPPSEGEESTVRFARKGALRQKNVHEVKNHKFTARFFKQPTFCSHCTDFIWGFGKQGFQCQVCCFVVHKRCHEFVTFSCPGADKGPASDDPRSKHKFKIHTYSSPTFCDHCGSLLYGLIHQGMKCDTCMMNVHKRCVMNVPSLCGTDHTERRGRIYIQAHIDRDVLIVLVRDAKNLVPMDPNGLSDPYVKLKLIPDPKSESKQKTKTIKCSLNPEWNETFRFQLKESDKDRRLSVEIWDWDLTSRNDFMGSLSFGISELQKASVDGWFKLLSQEEGEYFNVPVPPEGSEANEELRQKFERAKISQGTKVPEEKTTNTVSKFDNNGNRDRMKLTDFNFLMVLGKGSFGKVMLSERKGTDELYAVKILKKDVVIQDDDVECTMVEKRVLALPGKPPFLTQLHSCFQTMDRLYFVMEYVNGGDLMYHIQQVGRFKEPHAVFYAAEIAIGLFFLQSKGIIYRDLKLDNVMLDSEGHIKIADFGMCKENIWDGVTTKTFCGTPDYIAPEIIAYQPYGKSVDWWAFGVLLYEMLAGQAPFEGEDEDELFQSIMEHNVAYPKSMSKEAVAICKGLMTKHPGKRLGCGPEGERDIKEHAFFRYIDWEKLERKEIQPPYKPKARDKRDTSNFDKEFTRQPVELTPTDKLFIMNLDQNEFAGFSYTNPEFVINV 8SE4,8SE3,8SE2,3PFQ,9C5F,1A25 Protein kinase C beta type KPCB_HUMAN P05771 C5IFJ8 D3DWF5 O43744 P05127 Q15138 Q93060 Q9UE49 Q9UE50 Q9UEH8 Q9UJ30 Q9UJ33 50042844 O=C1NC(=O)C2=C1c1cn(CCO[C@H](CNS(=O)(=O)c3ccccc3)CCn3cc2c2ccccc32)c2ccccc12 |c:5| InChI=1S/C32H28N4O5S/c37-31-29-25-19-35(27-12-6-4-10-23(25)27)15-14-21(18-33-42(39,40)22-8-2-1-3-9-22)41-17-16-36-20-26(30(29)32(38)34-31)24-11-5-7-13-28(24)36/h1-13,19-21,33H,14-18H2,(H,34,37,38) ADVDNJCNXOTAHZ-UHFFFAOYSA-N 50052036 3,5-dioxo-17-phenylsulfonamidomethyl-(17S)-18-oxa-4,14,21-triazahexacyclo[19.6.1.17,14.02,6.08,13.022,27]nonacosa-1(28),2(6),7(29),8(13),9,11,22(27),23,25-nonaene::CHEMBL315389 Protein kinase C beta type Homo sapiens 44 ChEMBL 10.1021/jm950588y 10.7270/Q25H7FBV 8709095 Jirousek, MR; Gillig, JR; Gonzalez, CM; Heath, WF; McDonald, JH; Neel, DA; Rito, CJ; Singh, U; Stramm, LE; Melikian-Badalian, A; Baevsky, M; Ballas, LM; Hall, SE; Winneroski, LL; Faul, MM 9/10/1996 11/10/2009 Eli Lilly http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50052036 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=600&target=Protein+kinase+C+beta+type&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50052036&enzyme=Protein+kinase+C+beta+type&column=ki&startPg=0&Increment=50&submit=Search 10650891 103948961 CHEMBL315389 1 MADPAAGPPPSEGEESTVRFARKGALRQKNVHEVKNHKFTARFFKQPTFCSHCTDFIWGFGKQGFQCQVCCFVVHKRCHEFVTFSCPGADKGPASDDPRSKHKFKIHTYSSPTFCDHCGSLLYGLIHQGMKCDTCMMNVHKRCVMNVPSLCGTDHTERRGRIYIQAHIDRDVLIVLVRDAKNLVPMDPNGLSDPYVKLKLIPDPKSESKQKTKTIKCSLNPEWNETFRFQLKESDKDRRLSVEIWDWDLTSRNDFMGSLSFGISELQKASVDGWFKLLSQEEGEYFNVPVPPEGSEANEELRQKFERAKISQGTKVPEEKTTNTVSKFDNNGNRDRMKLTDFNFLMVLGKGSFGKVMLSERKGTDELYAVKILKKDVVIQDDDVECTMVEKRVLALPGKPPFLTQLHSCFQTMDRLYFVMEYVNGGDLMYHIQQVGRFKEPHAVFYAAEIAIGLFFLQSKGIIYRDLKLDNVMLDSEGHIKIADFGMCKENIWDGVTTKTFCGTPDYIAPEIIAYQPYGKSVDWWAFGVLLYEMLAGQAPFEGEDEDELFQSIMEHNVAYPKSMSKEAVAICKGLMTKHPGKRLGCGPEGERDIKEHAFFRYIDWEKLERKEIQPPYKPKARDKRDTSNFDKEFTRQPVELTPTDKLFIMNLDQNEFAGFSYTNPEFVINV 8SE4,8SE3,8SE2,3PFQ,9C5F,1A25 Protein kinase C beta type KPCB_HUMAN P05771 C5IFJ8 D3DWF5 O43744 P05127 Q15138 Q93060 Q9UE49 Q9UE50 Q9UEH8 Q9UJ30 Q9UJ33 50042845 OC[C@@H]1CCn2cc(C3=C(C(=O)NC3=O)c3cn(CCO1)c1ccccc31)c1ccccc21 |t:8| InChI=1S/C26H23N3O4/c30-15-16-9-10-28-13-19(17-5-1-3-7-21(17)28)23-24(26(32)27-25(23)31)20-14-29(11-12-33-16)22-8-4-2-6-18(20)22/h1-8,13-14,16,30H,9-12,15H2,(H,27,31,32) BGVKOUSMQGMSDY-UHFFFAOYSA-N 50052039 18-hydroxymethyl-(18S)-17-oxa-4,14,21-triazahexacyclo[19.6.1.17,14.02,6.08,13.022,27]nonacosa-1(28),2(6),7(29),8(13),9,11,22(27),23,25-nonaene-3,5-dione::LY-326449::CHEMBL292495 Protein kinase C eta type Homo sapiens 300 ChEMBL 10.1021/jm950588y 10.7270/Q25H7FBV 8709095 Jirousek, MR; Gillig, JR; Gonzalez, CM; Heath, WF; McDonald, JH; Neel, DA; Rito, CJ; Singh, U; Stramm, LE; Melikian-Badalian, A; Baevsky, M; Ballas, LM; Hall, SE; Winneroski, LL; Faul, MM 9/10/1996 11/10/2009 Eli Lilly http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50052039 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=605&target=Protein+kinase+C+eta+type&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50052039&enzyme=Protein+kinase+C+eta+type&column=ki&startPg=0&Increment=50&submit=Search 10455969 103948964 CHEMBL292495 1 MSSGTMKFNGYLRVRIGEAVGLQPTRWSLRHSLFKKGHQLLDPYLTVSVDQVRVGQTSTKQKTNKPTYNEEFCANVTDGGHLELAVFHETPLGYDHFVANCTLQFQELLRTTGASDTFEGWVDLEPEGKVFVVITLTGSFTEATLQRDRIFKHFTRKRQRAMRRRVHQINGHKFMATYLRQPTYCSHCREFIWGVFGKQGYQCQVCTCVVHKRCHHLIVTACTCQNNINKVDSKIAEQRFGINIPHKFSIHNYKVPTFCDHCGSLLWGIMRQGLQCKICKMNVHIRCQANVAPNCGVNAVELAKTLAGMGLQPGNISPTSKLVSRSTLRRQGKESSKEGNGIGVNSSNRLGIDNFEFIRVLGKGSFGKVMLARVKETGDLYAVKVLKKDVILQDDDVECTMTEKRILSLARNHPFLTQLFCCFQTPDRLFFVMEFVNGGDLMFHIQKSRRFDEARARFYAAEIISALMFLHDKGIIYRDLKLDNVLLDHEGHCKLADFGMCKEGICNGVTTATFCGTPDYIAPEILQEMLYGPAVDWWAMGVLLYEMLCGHAPFEAENEDDLFEAILNDEVVYPTWLHEDATGILKSFMTKNPTMRLGSLTQGGEHAILRHPFFKEIDWAQLNHRQIEPPFRPRIKSREDVSNFDPDFIKEEPVLTPIDEGHLPMINQDEFRNFSYVSPELQP 2FK9 Protein kinase C eta type KPCL_HUMAN P24723 B4DJN5 Q16246 Q8NE03 50042846 CNC[C@@H]1CCn2cc(C3=C(C(=O)NC3=O)c3cn(CCO1)c1ccccc31)c1ccccc21 |t:9| InChI=1S/C27H26N4O3/c1-28-14-17-10-11-30-15-20(18-6-2-4-8-22(18)30)24-25(27(33)29-26(24)32)21-16-31(12-13-34-17)23-9-5-3-7-19(21)23/h2-9,15-17,28H,10-14H2,1H3,(H,29,32,33) ZEYTZKVCOZMUKL-UHFFFAOYSA-N 50052034 18-methylaminomethyl-(18S)-17-oxa-4,14,21-triazahexacyclo[19.6.1.17,14.02,6.08,13.022,27]nonacosa-1(28),2(6),7(29),8(13),9,11,22(27),23,25-nonaene-3,5-dione::CHEMBL311543 Protein kinase C eta type Homo sapiens 31 ChEMBL 10.1021/jm950588y 10.7270/Q25H7FBV 8709095 Jirousek, MR; Gillig, JR; Gonzalez, CM; Heath, WF; McDonald, JH; Neel, DA; Rito, CJ; Singh, U; Stramm, LE; Melikian-Badalian, A; Baevsky, M; Ballas, LM; Hall, SE; Winneroski, LL; Faul, MM 9/10/1996 11/10/2009 Eli Lilly http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50052034 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=605&target=Protein+kinase+C+eta+type&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50052034&enzyme=Protein+kinase+C+eta+type&column=ki&startPg=0&Increment=50&submit=Search 10671412 103948959 CHEMBL311543 1 MSSGTMKFNGYLRVRIGEAVGLQPTRWSLRHSLFKKGHQLLDPYLTVSVDQVRVGQTSTKQKTNKPTYNEEFCANVTDGGHLELAVFHETPLGYDHFVANCTLQFQELLRTTGASDTFEGWVDLEPEGKVFVVITLTGSFTEATLQRDRIFKHFTRKRQRAMRRRVHQINGHKFMATYLRQPTYCSHCREFIWGVFGKQGYQCQVCTCVVHKRCHHLIVTACTCQNNINKVDSKIAEQRFGINIPHKFSIHNYKVPTFCDHCGSLLWGIMRQGLQCKICKMNVHIRCQANVAPNCGVNAVELAKTLAGMGLQPGNISPTSKLVSRSTLRRQGKESSKEGNGIGVNSSNRLGIDNFEFIRVLGKGSFGKVMLARVKETGDLYAVKVLKKDVILQDDDVECTMTEKRILSLARNHPFLTQLFCCFQTPDRLFFVMEFVNGGDLMFHIQKSRRFDEARARFYAAEIISALMFLHDKGIIYRDLKLDNVLLDHEGHCKLADFGMCKEGICNGVTTATFCGTPDYIAPEILQEMLYGPAVDWWAMGVLLYEMLCGHAPFEAENEDDLFEAILNDEVVYPTWLHEDATGILKSFMTKNPTMRLGSLTQGGEHAILRHPFFKEIDWAQLNHRQIEPPFRPRIKSREDVSNFDPDFIKEEPVLTPIDEGHLPMINQDEFRNFSYVSPELQP 2FK9 Protein kinase C eta type KPCL_HUMAN P24723 B4DJN5 Q16246 Q8NE03 50042847 O=C1NC(=O)C2=C1c1cn(CCO[C@H](CNS(=O)(=O)c3ccccc3)CCn3cc2c2ccccc32)c2ccccc12 |c:5| InChI=1S/C32H28N4O5S/c37-31-29-25-19-35(27-12-6-4-10-23(25)27)15-14-21(18-33-42(39,40)22-8-2-1-3-9-22)41-17-16-36-20-26(30(29)32(38)34-31)24-11-5-7-13-28(24)36/h1-13,19-21,33H,14-18H2,(H,34,37,38) ADVDNJCNXOTAHZ-UHFFFAOYSA-N 50052036 3,5-dioxo-17-phenylsulfonamidomethyl-(17S)-18-oxa-4,14,21-triazahexacyclo[19.6.1.17,14.02,6.08,13.022,27]nonacosa-1(28),2(6),7(29),8(13),9,11,22(27),23,25-nonaene::CHEMBL315389 Protein kinase C eta type Homo sapiens 1900 ChEMBL 10.1021/jm950588y 10.7270/Q25H7FBV 8709095 Jirousek, MR; Gillig, JR; Gonzalez, CM; Heath, WF; McDonald, JH; Neel, DA; Rito, CJ; Singh, U; Stramm, LE; Melikian-Badalian, A; Baevsky, M; Ballas, LM; Hall, SE; Winneroski, LL; Faul, MM 9/10/1996 11/10/2009 Eli Lilly http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50052036 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=605&target=Protein+kinase+C+eta+type&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50052036&enzyme=Protein+kinase+C+eta+type&column=ki&startPg=0&Increment=50&submit=Search 10650891 103948961 CHEMBL315389 1 MSSGTMKFNGYLRVRIGEAVGLQPTRWSLRHSLFKKGHQLLDPYLTVSVDQVRVGQTSTKQKTNKPTYNEEFCANVTDGGHLELAVFHETPLGYDHFVANCTLQFQELLRTTGASDTFEGWVDLEPEGKVFVVITLTGSFTEATLQRDRIFKHFTRKRQRAMRRRVHQINGHKFMATYLRQPTYCSHCREFIWGVFGKQGYQCQVCTCVVHKRCHHLIVTACTCQNNINKVDSKIAEQRFGINIPHKFSIHNYKVPTFCDHCGSLLWGIMRQGLQCKICKMNVHIRCQANVAPNCGVNAVELAKTLAGMGLQPGNISPTSKLVSRSTLRRQGKESSKEGNGIGVNSSNRLGIDNFEFIRVLGKGSFGKVMLARVKETGDLYAVKVLKKDVILQDDDVECTMTEKRILSLARNHPFLTQLFCCFQTPDRLFFVMEFVNGGDLMFHIQKSRRFDEARARFYAAEIISALMFLHDKGIIYRDLKLDNVLLDHEGHCKLADFGMCKEGICNGVTTATFCGTPDYIAPEILQEMLYGPAVDWWAMGVLLYEMLCGHAPFEAENEDDLFEAILNDEVVYPTWLHEDATGILKSFMTKNPTMRLGSLTQGGEHAILRHPFFKEIDWAQLNHRQIEPPFRPRIKSREDVSNFDPDFIKEEPVLTPIDEGHLPMINQDEFRNFSYVSPELQP 2FK9 Protein kinase C eta type KPCL_HUMAN P24723 B4DJN5 Q16246 Q8NE03 50042848 CN(C)C[C@@H]1CCn2cc(C3=C(C(=O)NC3=O)c3cn(CCO1)c1ccccc31)c1ccccc21 |r,t:10| InChI=1S/C28H28N4O3/c1-30(2)15-18-11-12-31-16-21(19-7-3-5-9-23(19)31)25-26(28(34)29-27(25)33)22-17-32(13-14-35-18)24-10-6-4-8-20(22)24/h3-10,16-18H,11-15H2,1-2H3,(H,29,33,34) ZCBUQCWBWNUWSU-UHFFFAOYSA-N 17055 (9S)-9-[(dimethylamino)methyl]-6,7,10,11-tetrahydro-9H,18H-5,21:12,17-di(metheno)dibenzo[e,k]pyrrolo[3,4-h][1,4,13]oxadiazacyclohexadecine-18,20(19H)-dione::(18S)-18-[(dimethylamino)methyl]-17-oxa-4,14,21-triazahexacyclo[19.6.1.1^{7,14}.0^{2,6}.0^{8,13}.0^{22,27}]nonacosa-1(28),2(6),7(29),8(13),9,11,22(27),23,25-nonaene-3,5-dione::K00587a::Ruboxistaurin::LY-333531::cid_153999::LY 333531::LY333531 Protein kinase C beta type Homo sapiens 5.9 ChEMBL 10.1021/jm950588y 10.7270/Q25H7FBV 8709095 Jirousek, MR; Gillig, JR; Gonzalez, CM; Heath, WF; McDonald, JH; Neel, DA; Rito, CJ; Singh, U; Stramm, LE; Melikian-Badalian, A; Baevsky, M; Ballas, LM; Hall, SE; Winneroski, LL; Faul, MM 9/10/1996 11/10/2009 Eli Lilly http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=17055 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=600&target=Protein+kinase+C+beta+type&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=17055&enzyme=Protein+kinase+C+beta+type&column=ki&startPg=0&Increment=50&submit=Search 153999 46517285 1 MADPAAGPPPSEGEESTVRFARKGALRQKNVHEVKNHKFTARFFKQPTFCSHCTDFIWGFGKQGFQCQVCCFVVHKRCHEFVTFSCPGADKGPASDDPRSKHKFKIHTYSSPTFCDHCGSLLYGLIHQGMKCDTCMMNVHKRCVMNVPSLCGTDHTERRGRIYIQAHIDRDVLIVLVRDAKNLVPMDPNGLSDPYVKLKLIPDPKSESKQKTKTIKCSLNPEWNETFRFQLKESDKDRRLSVEIWDWDLTSRNDFMGSLSFGISELQKASVDGWFKLLSQEEGEYFNVPVPPEGSEANEELRQKFERAKISQGTKVPEEKTTNTVSKFDNNGNRDRMKLTDFNFLMVLGKGSFGKVMLSERKGTDELYAVKILKKDVVIQDDDVECTMVEKRVLALPGKPPFLTQLHSCFQTMDRLYFVMEYVNGGDLMYHIQQVGRFKEPHAVFYAAEIAIGLFFLQSKGIIYRDLKLDNVMLDSEGHIKIADFGMCKENIWDGVTTKTFCGTPDYIAPEIIAYQPYGKSVDWWAFGVLLYEMLAGQAPFEGEDEDELFQSIMEHNVAYPKSMSKEAVAICKGLMTKHPGKRLGCGPEGERDIKEHAFFRYIDWEKLERKEIQPPYKPKARDKRDTSNFDKEFTRQPVELTPTDKLFIMNLDQNEFAGFSYTNPEFVINV 8SE4,8SE3,8SE2,3PFQ,9C5F,1A25 Protein kinase C beta type KPCB_HUMAN P05771 C5IFJ8 D3DWF5 O43744 P05127 Q15138 Q93060 Q9UE49 Q9UE50 Q9UEH8 Q9UJ30 Q9UJ33 50042849 CN(C)C[C@@H]1CCn2cc(C3=C(C(=O)NC3=O)c3cn(CCO1)c1ccccc31)c1ccccc21 |r,t:10| InChI=1S/C28H28N4O3/c1-30(2)15-18-11-12-31-16-21(19-7-3-5-9-23(19)31)25-26(28(34)29-27(25)33)22-17-32(13-14-35-18)24-10-6-4-8-20(22)24/h3-10,16-18H,11-15H2,1-2H3,(H,29,33,34) ZCBUQCWBWNUWSU-UHFFFAOYSA-N 17055 (9S)-9-[(dimethylamino)methyl]-6,7,10,11-tetrahydro-9H,18H-5,21:12,17-di(metheno)dibenzo[e,k]pyrrolo[3,4-h][1,4,13]oxadiazacyclohexadecine-18,20(19H)-dione::(18S)-18-[(dimethylamino)methyl]-17-oxa-4,14,21-triazahexacyclo[19.6.1.1^{7,14}.0^{2,6}.0^{8,13}.0^{22,27}]nonacosa-1(28),2(6),7(29),8(13),9,11,22(27),23,25-nonaene-3,5-dione::K00587a::Ruboxistaurin::LY-333531::cid_153999::LY 333531::LY333531 Protein kinase C alpha type Homo sapiens 360 ChEMBL 10.1021/jm950588y 10.7270/Q25H7FBV 8709095 Jirousek, MR; Gillig, JR; Gonzalez, CM; Heath, WF; McDonald, JH; Neel, DA; Rito, CJ; Singh, U; Stramm, LE; Melikian-Badalian, A; Baevsky, M; Ballas, LM; Hall, SE; Winneroski, LL; Faul, MM 9/10/1996 11/10/2009 Eli Lilly http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=17055 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=599&target=Protein+kinase+C+alpha+type&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=17055&enzyme=Protein+kinase+C+alpha+type&column=ki&startPg=0&Increment=50&submit=Search 153999 46517285 1 MADVFPGNDSTASQDVANRFARKGALRQKNVHEVKDHKFIARFFKQPTFCSHCTDFIWGFGKQGFQCQVCCFVVHKRCHEFVTFSCPGADKGPDTDDPRSKHKFKIHTYGSPTFCDHCGSLLYGLIHQGMKCDTCDMNVHKQCVINVPSLCGMDHTEKRGRIYLKAEVADEKLHVTVRDAKNLIPMDPNGLSDPYVKLKLIPDPKNESKQKTKTIRSTLNPQWNESFTFKLKPSDKDRRLSVEIWDWDRTTRNDFMGSLSFGVSELMKMPASGWYKLLNQEEGEYYNVPIPEGDEEGNMELRQKFEKAKLGPAGNKVISPSEDRKQPSNNLDRVKLTDFNFLMVLGKGSFGKVMLADRKGTEELYAIKILKKDVVIQDDDVECTMVEKRVLALLDKPPFLTQLHSCFQTVDRLYFVMEYVNGGDLMYHIQQVGKFKEPQAVFYAAEISIGLFFLHKRGIIYRDLKLDNVMLDSEGHIKIADFGMCKEHMMDGVTTRTFCGTPDYIAPEIIAYQPYGKSVDWWAYGVLLYEMLAGQPPFDGEDEDELFQSIMEHNVSYPKSLSKEAVSVCKGLMTKHPAKRLGCGPEGERDVREHAFFRRIDWEKLENREIQPPFKPKVCGKGAENFDKFFTRGQPVLTPPDQLVIANIDQSDFEGFSYVNPQFVHPILQSAV 4RA4,4DNL Protein kinase C alpha type KPCA_HUMAN P17252 B5BU22 Q15137 Q32M72 Q96RE4 50042850 C[C@@]12[C@@H]([C@@H](C[C@@H](O1)n3c4ccccc4c5c3c6n2c7ccccc7c6c8c5C(=O)NC8)NC)OC InChI=1S/C28H26N4O3/c1-28-26(34-3)17(29-2)12-20(35-28)31-18-10-6-4-8-14(18)22-23-16(13-30-27(23)33)21-15-9-5-7-11-19(15)32(28)25(21)24(22)31/h4-11,17,20,26,29H,12-13H2,1-3H3,(H,30,33) HKSZLNNOFSGOKW-UHFFFAOYSA-N 2579 CHEMBL388978::Staurosporine, 8::Staurosporin, 4::(2S,3R,4R,6R)-3-methoxy-2-methyl-4-(methylamino)-29-oxa-1,7,17-triazaoctacyclo[12.12.2.1^{2,6}.0^{7,28}.0^{8,13}.0^{15,19}.0^{20,27}.0^{21,26}]nonacosa-8(13),9,11,14(28),15(19),20(27),21(26),22,24-nonaen-16-one::Staurosporine::US9206188, Staurosporine::US9226923, Staurosporine::US20240002365, Compound staurosporine::US11958831, Example Staurosporine::US20240254124, Compound Staurosporine::US20240309004, Compound STAUROSPORINE::US12350272, Compound Staurosporine::US12398142, Compound Staurosporine::US12410173, Compound Staurosporine Protein kinase C beta type Homo sapiens 23 ChEMBL 10.1021/jm950588y 10.7270/Q25H7FBV 8709095 Jirousek, MR; Gillig, JR; Gonzalez, CM; Heath, WF; McDonald, JH; Neel, DA; Rito, CJ; Singh, U; Stramm, LE; Melikian-Badalian, A; Baevsky, M; Ballas, LM; Hall, SE; Winneroski, LL; Faul, MM 9/10/1996 11/10/2009 Eli Lilly http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=2579 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=600&target=Protein+kinase+C+beta+type&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=2579&enzyme=Protein+kinase+C+beta+type&column=ki&startPg=0&Increment=50&submit=Search STO 44259 8032349 CHEMBL388978 C02079 1 MADPAAGPPPSEGEESTVRFARKGALRQKNVHEVKNHKFTARFFKQPTFCSHCTDFIWGFGKQGFQCQVCCFVVHKRCHEFVTFSCPGADKGPASDDPRSKHKFKIHTYSSPTFCDHCGSLLYGLIHQGMKCDTCMMNVHKRCVMNVPSLCGTDHTERRGRIYIQAHIDRDVLIVLVRDAKNLVPMDPNGLSDPYVKLKLIPDPKSESKQKTKTIKCSLNPEWNETFRFQLKESDKDRRLSVEIWDWDLTSRNDFMGSLSFGISELQKASVDGWFKLLSQEEGEYFNVPVPPEGSEANEELRQKFERAKISQGTKVPEEKTTNTVSKFDNNGNRDRMKLTDFNFLMVLGKGSFGKVMLSERKGTDELYAVKILKKDVVIQDDDVECTMVEKRVLALPGKPPFLTQLHSCFQTMDRLYFVMEYVNGGDLMYHIQQVGRFKEPHAVFYAAEIAIGLFFLQSKGIIYRDLKLDNVMLDSEGHIKIADFGMCKENIWDGVTTKTFCGTPDYIAPEIIAYQPYGKSVDWWAFGVLLYEMLAGQAPFEGEDEDELFQSIMEHNVAYPKSMSKEAVAICKGLMTKHPGKRLGCGPEGERDIKEHAFFRYIDWEKLERKEIQPPYKPKARDKRDTSNFDKEFTRQPVELTPTDKLFIMNLDQNEFAGFSYTNPEFVINV 8SE4,8SE3,8SE2,3PFQ,9C5F,1A25 Protein kinase C beta type KPCB_HUMAN P05771 C5IFJ8 D3DWF5 O43744 P05127 Q15138 Q93060 Q9UE49 Q9UE50 Q9UEH8 Q9UJ30 Q9UJ33 50042851 O=C1NC(=O)C2=C1c1cn(CCO[C@H](CN3CCOCC3)CCn3cc2c2ccccc32)c2ccccc12 |c:5| InChI=1S/C30H30N4O4/c35-29-27-23-18-33(25-7-3-1-5-21(23)25)10-9-20(17-32-11-14-37-15-12-32)38-16-13-34-19-24(28(27)30(36)31-29)22-6-2-4-8-26(22)34/h1-8,18-20H,9-17H2,(H,31,35,36) CLHMTFQYMLYQME-UHFFFAOYSA-N 50052035 18-(1,4-oxazinan-4-ylmethyl)-(18S)-17-oxa-4,14,21-triazahexacyclo[19.6.1.17,14.02,6.08,13.022,27]nonacosa-1(28),2(6),7(29),8(13),9,11,22(27),23,25-nonaene-3,5-dione::CHEMBL315357 Protein kinase C beta type Homo sapiens 49 ChEMBL 10.1021/jm950588y 10.7270/Q25H7FBV 8709095 Jirousek, MR; Gillig, JR; Gonzalez, CM; Heath, WF; McDonald, JH; Neel, DA; Rito, CJ; Singh, U; Stramm, LE; Melikian-Badalian, A; Baevsky, M; Ballas, LM; Hall, SE; Winneroski, LL; Faul, MM 9/10/1996 11/10/2009 Eli Lilly http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50052035 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=600&target=Protein+kinase+C+beta+type&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50052035&enzyme=Protein+kinase+C+beta+type&column=ki&startPg=0&Increment=50&submit=Search 10673286 103948960 CHEMBL315357 1 MADPAAGPPPSEGEESTVRFARKGALRQKNVHEVKNHKFTARFFKQPTFCSHCTDFIWGFGKQGFQCQVCCFVVHKRCHEFVTFSCPGADKGPASDDPRSKHKFKIHTYSSPTFCDHCGSLLYGLIHQGMKCDTCMMNVHKRCVMNVPSLCGTDHTERRGRIYIQAHIDRDVLIVLVRDAKNLVPMDPNGLSDPYVKLKLIPDPKSESKQKTKTIKCSLNPEWNETFRFQLKESDKDRRLSVEIWDWDLTSRNDFMGSLSFGISELQKASVDGWFKLLSQEEGEYFNVPVPPEGSEANEELRQKFERAKISQGTKVPEEKTTNTVSKFDNNGNRDRMKLTDFNFLMVLGKGSFGKVMLSERKGTDELYAVKILKKDVVIQDDDVECTMVEKRVLALPGKPPFLTQLHSCFQTMDRLYFVMEYVNGGDLMYHIQQVGRFKEPHAVFYAAEIAIGLFFLQSKGIIYRDLKLDNVMLDSEGHIKIADFGMCKENIWDGVTTKTFCGTPDYIAPEIIAYQPYGKSVDWWAFGVLLYEMLAGQAPFEGEDEDELFQSIMEHNVAYPKSMSKEAVAICKGLMTKHPGKRLGCGPEGERDIKEHAFFRYIDWEKLERKEIQPPYKPKARDKRDTSNFDKEFTRQPVELTPTDKLFIMNLDQNEFAGFSYTNPEFVINV 8SE4,8SE3,8SE2,3PFQ,9C5F,1A25 Protein kinase C beta type KPCB_HUMAN P05771 C5IFJ8 D3DWF5 O43744 P05127 Q15138 Q93060 Q9UE49 Q9UE50 Q9UEH8 Q9UJ30 Q9UJ33 50042852 C[C@@]12[C@@H]([C@@H](C[C@@H](O1)n3c4ccccc4c5c3c6n2c7ccccc7c6c8c5C(=O)NC8)NC)OC InChI=1S/C28H26N4O3/c1-28-26(34-3)17(29-2)12-20(35-28)31-18-10-6-4-8-14(18)22-23-16(13-30-27(23)33)21-15-9-5-7-11-19(15)32(28)25(21)24(22)31/h4-11,17,20,26,29H,12-13H2,1-3H3,(H,30,33) HKSZLNNOFSGOKW-UHFFFAOYSA-N 2579 CHEMBL388978::Staurosporine, 8::Staurosporin, 4::(2S,3R,4R,6R)-3-methoxy-2-methyl-4-(methylamino)-29-oxa-1,7,17-triazaoctacyclo[12.12.2.1^{2,6}.0^{7,28}.0^{8,13}.0^{15,19}.0^{20,27}.0^{21,26}]nonacosa-8(13),9,11,14(28),15(19),20(27),21(26),22,24-nonaen-16-one::Staurosporine::US9206188, Staurosporine::US9226923, Staurosporine::US20240002365, Compound staurosporine::US11958831, Example Staurosporine::US20240254124, Compound Staurosporine::US20240309004, Compound STAUROSPORINE::US12350272, Compound Staurosporine::US12398142, Compound Staurosporine::US12410173, Compound Staurosporine Protein kinase C eta type Homo sapiens 5 ChEMBL 10.1021/jm950588y 10.7270/Q25H7FBV 8709095 Jirousek, MR; Gillig, JR; Gonzalez, CM; Heath, WF; McDonald, JH; Neel, DA; Rito, CJ; Singh, U; Stramm, LE; Melikian-Badalian, A; Baevsky, M; Ballas, LM; Hall, SE; Winneroski, LL; Faul, MM 9/10/1996 11/10/2009 Eli Lilly http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=2579 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=605&target=Protein+kinase+C+eta+type&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=2579&enzyme=Protein+kinase+C+eta+type&column=ki&startPg=0&Increment=50&submit=Search STO 44259 8032349 CHEMBL388978 C02079 1 MSSGTMKFNGYLRVRIGEAVGLQPTRWSLRHSLFKKGHQLLDPYLTVSVDQVRVGQTSTKQKTNKPTYNEEFCANVTDGGHLELAVFHETPLGYDHFVANCTLQFQELLRTTGASDTFEGWVDLEPEGKVFVVITLTGSFTEATLQRDRIFKHFTRKRQRAMRRRVHQINGHKFMATYLRQPTYCSHCREFIWGVFGKQGYQCQVCTCVVHKRCHHLIVTACTCQNNINKVDSKIAEQRFGINIPHKFSIHNYKVPTFCDHCGSLLWGIMRQGLQCKICKMNVHIRCQANVAPNCGVNAVELAKTLAGMGLQPGNISPTSKLVSRSTLRRQGKESSKEGNGIGVNSSNRLGIDNFEFIRVLGKGSFGKVMLARVKETGDLYAVKVLKKDVILQDDDVECTMTEKRILSLARNHPFLTQLFCCFQTPDRLFFVMEFVNGGDLMFHIQKSRRFDEARARFYAAEIISALMFLHDKGIIYRDLKLDNVLLDHEGHCKLADFGMCKEGICNGVTTATFCGTPDYIAPEILQEMLYGPAVDWWAMGVLLYEMLCGHAPFEAENEDDLFEAILNDEVVYPTWLHEDATGILKSFMTKNPTMRLGSLTQGGEHAILRHPFFKEIDWAQLNHRQIEPPFRPRIKSREDVSNFDPDFIKEEPVLTPIDEGHLPMINQDEFRNFSYVSPELQP 2FK9 Protein kinase C eta type KPCL_HUMAN P24723 B4DJN5 Q16246 Q8NE03 50063742 OC[C@@H]1CCn2cc(C3=C(C(=O)NC3=O)c3cn(CCO1)c1ccccc31)c1ccccc21 |t:8| InChI=1S/C26H23N3O4/c30-15-16-9-10-28-13-19(17-5-1-3-7-21(17)28)23-24(26(32)27-25(23)31)20-14-29(11-12-33-16)22-8-4-2-6-18(20)22/h1-8,13-14,16,30H,9-12,15H2,(H,27,31,32) BGVKOUSMQGMSDY-UHFFFAOYSA-N 50052039 18-hydroxymethyl-(18S)-17-oxa-4,14,21-triazahexacyclo[19.6.1.17,14.02,6.08,13.022,27]nonacosa-1(28),2(6),7(29),8(13),9,11,22(27),23,25-nonaene-3,5-dione::LY-326449::CHEMBL292495 Protein kinase C beta type Homo sapiens 28 ChEMBL 10.1021/jm950588y 10.7270/Q25H7FBV 8709095 Jirousek, MR; Gillig, JR; Gonzalez, CM; Heath, WF; McDonald, JH; Neel, DA; Rito, CJ; Singh, U; Stramm, LE; Melikian-Badalian, A; Baevsky, M; Ballas, LM; Hall, SE; Winneroski, LL; Faul, MM 9/10/1996 11/10/2009 Eli Lilly http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50052039 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=600&target=Protein+kinase+C+beta+type&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50052039&enzyme=Protein+kinase+C+beta+type&column=ki&startPg=0&Increment=50&submit=Search 10455969 103948964 CHEMBL292495 1 MADPAAGPPPSEGEESTVRFARKGALRQKNVHEVKNHKFTARFFKQPTFCSHCTDFIWGFGKQGFQCQVCCFVVHKRCHEFVTFSCPGADKGPASDDPRSKHKFKIHTYSSPTFCDHCGSLLYGLIHQGMKCDTCMMNVHKRCVMNVPSLCGTDHTERRGRIYIQAHIDRDVLIVLVRDAKNLVPMDPNGLSDPYVKLKLIPDPKSESKQKTKTIKCSLNPEWNETFRFQLKESDKDRRLSVEIWDWDLTSRNDFMGSLSFGISELQKASVDGWFKLLSQEEGEYFNVPVPPEGSEANEELRQKFERAKISQGTKVPEEKTTNTVSKFDNNGNRDRMKLTDFNFLMVLGKGSFGKVMLSERKGTDELYAVKILKKDVVIQDDDVECTMVEKRVLALPGKPPFLTQLHSCFQTMDRLYFVMEYVNGGDLMYHIQQVGRFKEPHAVFYAAEIAIGLFFLQSKGIIYRDLKLDNVMLDSEGHIKIADFGMCKENIWDGVTTKTFCGTPDYIAPEIIAYQPYGKSVDWWAFGVLLYEMLAGQAPFEGEDEDELFQSIMEHNVAYPKSMSKEAVAICKGLMTKHPGKRLGCGPEGERDIKEHAFFRYIDWEKLERKEIQPPYKPKARDKRDTSNFDKEFTRQPVELTPTDKLFIMNLDQNEFAGFSYTNPEFVINV 8SE4,8SE3,8SE2,3PFQ,9C5F,1A25 Protein kinase C beta type KPCB_HUMAN P05771 C5IFJ8 D3DWF5 O43744 P05127 Q15138 Q93060 Q9UE49 Q9UE50 Q9UEH8 Q9UJ30 Q9UJ33 50085266 O=C1NC(=O)C2=C1c1cn(CCO[C@H](CN3CCOCC3)CCn3cc2c2ccccc32)c2ccccc12 |c:5| InChI=1S/C30H30N4O4/c35-29-27-23-18-33(25-7-3-1-5-21(23)25)10-9-20(17-32-11-14-37-15-12-32)38-16-13-34-19-24(28(27)30(36)31-29)22-6-2-4-8-26(22)34/h1-8,18-20H,9-17H2,(H,31,35,36) CLHMTFQYMLYQME-UHFFFAOYSA-N 50052035 18-(1,4-oxazinan-4-ylmethyl)-(18S)-17-oxa-4,14,21-triazahexacyclo[19.6.1.17,14.02,6.08,13.022,27]nonacosa-1(28),2(6),7(29),8(13),9,11,22(27),23,25-nonaene-3,5-dione::CHEMBL315357 Protein kinase C epsilon type Homo sapiens >5000 ChEMBL 10.1021/jm950588y 10.7270/Q25H7FBV 8709095 Jirousek, MR; Gillig, JR; Gonzalez, CM; Heath, WF; McDonald, JH; Neel, DA; Rito, CJ; Singh, U; Stramm, LE; Melikian-Badalian, A; Baevsky, M; Ballas, LM; Hall, SE; Winneroski, LL; Faul, MM 9/10/1996 11/10/2009 Eli Lilly http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50052035 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=604&target=Protein+kinase+C+epsilon+type&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50052035&enzyme=Protein+kinase+C+epsilon+type&column=ki&startPg=0&Increment=50&submit=Search 10673286 103948960 CHEMBL315357 1 MVVFNGLLKIKICEAVSLKPTAWSLRHAVGPRPQTFLLDPYIALNVDDSRIGQTATKQKTNSPAWHDEFVTDVCNGRKIELAVFHDAPIGYDDFVANCTIQFEELLQNGSRHFEDWIDLEPEGRVYVIIDLSGSSGEAPKDNEERVFRERMRPRKRQGAVRRRVHQVNGHKFMATYLRQPTYCSHCRDFIWGVIGKQGYQCQVCTCVVHKRCHELIITKCAGLKKQETPDQVGSQRFSVNMPHKFGIHNYKVPTFCDHCGSLLWGLLRQGLQCKVCKMNVHRRCETNVAPNCGVDARGIAKVLADLGVTPDKITNSGQRRKKLIAGAESPQPASGSSPSEEDRSKSAPTSPCDQEIKELENNIRKALSFDNRGEEHRAASSPDGQLMSPGENGEVRQGQAKRLGLDEFNFIKVLGKGSFGKVMLAELKGKDEVYAVKVLKKDVILQDDDVDCTMTEKRILALARKHPYLTQLYCCFQTKDRLFFVMEYVNGGDLMFQIQRSRKFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILLDAEGHCKLADFGMCKEGILNGVTTTTFCGTPDYIAPEILQELEYGPSVDWWALGVLMYEMMAGQPPFEADNEDDLFESILHDDVLYPVWLSKEAVSILKAFMTKNPHKRLGCVASQNGEDAIKQHPFFKEIDWVLLEQKKIKPPFKPRIKTKRDVNNFDQDFTREEPVLTLVDEAIVKQINQEEFKGFSYFGEDLMP Protein kinase C epsilon type KPCE_HUMAN Q02156 B0LPH7 Q32MQ3 Q53SL4 Q53SM5 Q9UE81 50085268 O=C1NC(=O)C2=C1c1cn(CCO[C@H](CNS(=O)(=O)c3ccccc3)CCn3cc2c2ccccc32)c2ccccc12 |c:5| InChI=1S/C32H28N4O5S/c37-31-29-25-19-35(27-12-6-4-10-23(25)27)15-14-21(18-33-42(39,40)22-8-2-1-3-9-22)41-17-16-36-20-26(30(29)32(38)34-31)24-11-5-7-13-28(24)36/h1-13,19-21,33H,14-18H2,(H,34,37,38) ADVDNJCNXOTAHZ-UHFFFAOYSA-N 50052036 3,5-dioxo-17-phenylsulfonamidomethyl-(17S)-18-oxa-4,14,21-triazahexacyclo[19.6.1.17,14.02,6.08,13.022,27]nonacosa-1(28),2(6),7(29),8(13),9,11,22(27),23,25-nonaene::CHEMBL315389 Protein kinase C gamma type Homo sapiens >5000 ChEMBL 10.1021/jm950588y 10.7270/Q25H7FBV 8709095 Jirousek, MR; Gillig, JR; Gonzalez, CM; Heath, WF; McDonald, JH; Neel, DA; Rito, CJ; Singh, U; Stramm, LE; Melikian-Badalian, A; Baevsky, M; Ballas, LM; Hall, SE; Winneroski, LL; Faul, MM 9/10/1996 11/10/2009 Eli Lilly http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50052036 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=602&target=Protein+kinase+C+gamma+type&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50052036&enzyme=Protein+kinase+C+gamma+type&column=ki&startPg=0&Increment=50&submit=Search 10650891 103948961 CHEMBL315389 1 MAGLGPGVGDSEGGPRPLFCRKGALRQKVVHEVKSHKFTARFFKQPTFCSHCTDFIWGIGKQGLQCQVCSFVVHRRCHEFVTFECPGAGKGPQTDDPRNKHKFRLHSYSSPTFCDHCGSLLYGLVHQGMKCSCCEMNVHRRCVRSVPSLCGVDHTERRGRLQLEIRAPTADEIHVTVGEARNLIPMDPNGLSDPYVKLKLIPDPRNLTKQKTRTVKATLNPVWNETFVFNLKPGDVERRLSVEVWDWDRTSRNDFMGAMSFGVSELLKAPVDGWYKLLNQEEGEYYNVPVADADNCSLLQKFEACNYPLELYERVRMGPSSSPIPSPSPSPTDPKRCFFGASPGRLHISDFSFLMVLGKGSFGKVMLAERRGSDELYAIKILKKDVIVQDDDVDCTLVEKRVLALGGRGPGGRPHFLTQLHSTFQTPDRLYFVMEYVTGGDLMYHIQQLGKFKEPHAAFYAAEIAIGLFFLHNQGIIYRDLKLDNVMLDAEGHIKITDFGMCKENVFPGTTTRTFCGTPDYIAPEIIAYQPYGKSVDWWSFGVLLYEMLAGQPPFDGEDEEELFQAIMEQTVTYPKSLSREAVAICKGFLTKHPGKRLGSGPDGEPTIRAHGFFRWIDWERLERLEIPPPFRPRPCGRSGENFDKFFTRAAPALTPPDRLVLASIDQADFQGFTYVNPDFVHPDARSPTSPVPVPVM 2UZP Protein kinase C gamma type KPCG_HUMAN P05129 B7Z8Q0 50085274 O=C1NC(=O)C2=C1c1cn(CCO[C@H](CN3CCOCC3)CCn3cc2c2ccccc32)c2ccccc12 |c:5| InChI=1S/C30H30N4O4/c35-29-27-23-18-33(25-7-3-1-5-21(23)25)10-9-20(17-32-11-14-37-15-12-32)38-16-13-34-19-24(28(27)30(36)31-29)22-6-2-4-8-26(22)34/h1-8,18-20H,9-17H2,(H,31,35,36) CLHMTFQYMLYQME-UHFFFAOYSA-N 50052035 18-(1,4-oxazinan-4-ylmethyl)-(18S)-17-oxa-4,14,21-triazahexacyclo[19.6.1.17,14.02,6.08,13.022,27]nonacosa-1(28),2(6),7(29),8(13),9,11,22(27),23,25-nonaene-3,5-dione::CHEMBL315357 Protein kinase C zeta type Homo sapiens >5000 ChEMBL 10.1021/jm950588y 10.7270/Q25H7FBV 8709095 Jirousek, MR; Gillig, JR; Gonzalez, CM; Heath, WF; McDonald, JH; Neel, DA; Rito, CJ; Singh, U; Stramm, LE; Melikian-Badalian, A; Baevsky, M; Ballas, LM; Hall, SE; Winneroski, LL; Faul, MM 9/10/1996 11/10/2009 Eli Lilly http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50052035 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=606&target=Protein+kinase+C+zeta+type&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50052035&enzyme=Protein+kinase+C+zeta+type&column=ki&startPg=0&Increment=50&submit=Search 10673286 103948960 CHEMBL315357 1 MPSRTGPKMEGSGGRVRLKAHYGGDIFITSVDAATTFEELCEEVRDMCRLHQQHPLTLKWVDSEGDPCTVSSQMELEEAFRLARQCRDEGLIIHVFPSTPEQPGLPCPGEDKSIYRRGARRWRKLYRANGHLFQAKRFNRRAYCGQCSERIWGLARQGYRCINCKLLVHKRCHGLVPLTCRKHMDSVMPSQEPPVDDKNEDADLPSEETDGIAYISSSRKHDSIKDDSEDLKPVIDGMDGIKISQGLGLQDFDLIRVIGRGSYAKVLLVRLKKNDQIYAMKVVKKELVHDDEDIDWVQTEKHVFEQASSNPFLVGLHSCFQTTSRLFLVIEYVNGGDLMFHMQRQRKLPEEHARFYAAEICIALNFLHERGIIYRDLKLDNVLLDADGHIKLTDYGMCKEGLGPGDTTSTFCGTPNYIAPEILRGEEYGFSVDWWALGVLMFEMMAGRSPFDIITDNPDMNTEDYLFQVILEKPIRIPRFLSVKASHVLKGFLNKDPKERLGCRPQTGFSDIKSHAFFRSIDWDLLEKKQALPPFQPQITDDYGLDNFDTQFTSEPVQLTPDDEDAIKRIDQSEFEGFEYINPLLLSTEESV Protein kinase C zeta type KPCZ_HUMAN Q05513 A8K4N0 A8MU64 B7Z2J7 E9PCW2 Q15207 Q5SYT5 Q969S4 50085275 O=C1NC(=O)C2=C1c1cn(CCO[C@H](CNS(=O)(=O)c3ccccc3)CCn3cc2c2ccccc32)c2ccccc12 |c:5| InChI=1S/C32H28N4O5S/c37-31-29-25-19-35(27-12-6-4-10-23(25)27)15-14-21(18-33-42(39,40)22-8-2-1-3-9-22)41-17-16-36-20-26(30(29)32(38)34-31)24-11-5-7-13-28(24)36/h1-13,19-21,33H,14-18H2,(H,34,37,38) ADVDNJCNXOTAHZ-UHFFFAOYSA-N 50052036 3,5-dioxo-17-phenylsulfonamidomethyl-(17S)-18-oxa-4,14,21-triazahexacyclo[19.6.1.17,14.02,6.08,13.022,27]nonacosa-1(28),2(6),7(29),8(13),9,11,22(27),23,25-nonaene::CHEMBL315389 Protein kinase C beta type Homo sapiens 170 ChEMBL 10.1021/jm950588y 10.7270/Q25H7FBV 8709095 Jirousek, MR; Gillig, JR; Gonzalez, CM; Heath, WF; McDonald, JH; Neel, DA; Rito, CJ; Singh, U; Stramm, LE; Melikian-Badalian, A; Baevsky, M; Ballas, LM; Hall, SE; Winneroski, LL; Faul, MM 9/10/1996 11/10/2009 Eli Lilly http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50052036 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=600&target=Protein+kinase+C+beta+type&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50052036&enzyme=Protein+kinase+C+beta+type&column=ki&startPg=0&Increment=50&submit=Search 10650891 103948961 CHEMBL315389 1 MADPAAGPPPSEGEESTVRFARKGALRQKNVHEVKNHKFTARFFKQPTFCSHCTDFIWGFGKQGFQCQVCCFVVHKRCHEFVTFSCPGADKGPASDDPRSKHKFKIHTYSSPTFCDHCGSLLYGLIHQGMKCDTCMMNVHKRCVMNVPSLCGTDHTERRGRIYIQAHIDRDVLIVLVRDAKNLVPMDPNGLSDPYVKLKLIPDPKSESKQKTKTIKCSLNPEWNETFRFQLKESDKDRRLSVEIWDWDLTSRNDFMGSLSFGISELQKASVDGWFKLLSQEEGEYFNVPVPPEGSEANEELRQKFERAKISQGTKVPEEKTTNTVSKFDNNGNRDRMKLTDFNFLMVLGKGSFGKVMLSERKGTDELYAVKILKKDVVIQDDDVECTMVEKRVLALPGKPPFLTQLHSCFQTMDRLYFVMEYVNGGDLMYHIQQVGRFKEPHAVFYAAEIAIGLFFLQSKGIIYRDLKLDNVMLDSEGHIKIADFGMCKENIWDGVTTKTFCGTPDYIAPEIIAYQPYGKSVDWWAFGVLLYEMLAGQAPFEGEDEDELFQSIMEHNVAYPKSMSKEAVAICKGLMTKHPGKRLGCGPEGERDIKEHAFFRYIDWEKLERKEIQPPYKPKARDKRDTSNFDKEFTRQPVELTPTDKLFIMNLDQNEFAGFSYTNPEFVINV 8SE4,8SE3,8SE2,3PFQ,9C5F,1A25 Protein kinase C beta type KPCB_HUMAN P05771 C5IFJ8 D3DWF5 O43744 P05127 Q15138 Q93060 Q9UE49 Q9UE50 Q9UEH8 Q9UJ30 Q9UJ33 50085276 NC[C@@H]1CCn2cc(C3=C(C(=O)NC3=O)c3cn(CCO1)c1ccccc31)c1ccccc21 |t:8| InChI=1S/C26H24N4O3/c27-13-16-9-10-29-14-19(17-5-1-3-7-21(17)29)23-24(26(32)28-25(23)31)20-15-30(11-12-33-16)22-8-4-2-6-18(20)22/h1-8,14-16H,9-13,27H2,(H,28,31,32) JPLUPRIZLHXUPQ-UHFFFAOYSA-N 50052037 18-aminomethyl-(18S)-17-oxa-4,14,21-triazahexacyclo[19.6.1.17,14.02,6.08,13.022,27]nonacosa-1(28),2(6),7(29),8(13),9,11,22(27),23,25-nonaene-3,5-dione::CHEMBL316239 Proto-oncogene tyrosine-protein kinase Src Homo sapiens 89000 ChEMBL 10.1021/jm950588y 10.7270/Q25H7FBV 8709095 Jirousek, MR; Gillig, JR; Gonzalez, CM; Heath, WF; McDonald, JH; Neel, DA; Rito, CJ; Singh, U; Stramm, LE; Melikian-Badalian, A; Baevsky, M; Ballas, LM; Hall, SE; Winneroski, LL; Faul, MM 9/10/1996 11/10/2009 Eli Lilly http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50052037 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=13&target=Proto-oncogene+tyrosine-protein+kinase+Src&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50052037&enzyme=Proto-oncogene+tyrosine-protein+kinase+Src&column=ki&startPg=0&Increment=50&submit=Search 10527068 103948962 CHEMBL316239 1 MGSNKSKPKDASQRRRSLEPAENVHGAGGGAFPASQTPSKPASADGHRGPSAAFAPAAAEPKLFGGFNSSDTVTSPQRAGPLAGGVTTFVALYDYESRTETDLSFKKGERLQIVNNTEGDWWLAHSLSTGQTGYIPSNYVAPSDSIQAEEWYFGKITRRESERLLLNAENPRGTFLVRESETTKGAYCLSVSDFDNAKGLNVKHYKIRKLDSGGFYITSRTQFNSLQQLVAYYSKHADGLCHRLTTVCPTSKPQTQGLAKDAWEIPRESLRLEVKLGQGCFGEVWMGTWNGTTRVAIKTLKPGTMSPEAFLQEAQVMKKLRHEKLVQLYAVVSEEPIYIVTEYMSKGSLLDFLKGETGKYLRLPQLVDMAAQIASGMAYVERMNYVHRDLRAANILVGENLVCKVADFGLARLIEDNEYTARQGAKFPIKWTAPEAALYGRFTIKSDVWSFGILLTELTTKGRVPYPGMVNREVLDQVERGYRMPCPPECPESLHDLMCQCWRKEPEERPTFEYLQAFLEDYFTSTEPQYQPGENL 8JN9,8JN8,2H8H,2SRC,1Y57,1FMK,2PTK,9NS0,8JF3,6ATE,4MXO,4MXX,2BDJ,2BDF,8HAQ,6E6E,1YI6 Proto-oncogene tyrosine-protein kinase Src SRC_HUMAN P12931 E1P5V4 Q76P87 Q86VB9 Q9H5A8 50085279 NC[C@@H]1CCn2cc(C3=C(C(=O)NC3=O)c3cn(CCO1)c1ccccc31)c1ccccc21 |t:8| InChI=1S/C26H24N4O3/c27-13-16-9-10-29-14-19(17-5-1-3-7-21(17)29)23-24(26(32)28-25(23)31)20-15-30(11-12-33-16)22-8-4-2-6-18(20)22/h1-8,14-16H,9-13,27H2,(H,28,31,32) JPLUPRIZLHXUPQ-UHFFFAOYSA-N 50052037 18-aminomethyl-(18S)-17-oxa-4,14,21-triazahexacyclo[19.6.1.17,14.02,6.08,13.022,27]nonacosa-1(28),2(6),7(29),8(13),9,11,22(27),23,25-nonaene-3,5-dione::CHEMBL316239 Protein kinase C gamma type Homo sapiens 2100 ChEMBL 10.1021/jm950588y 10.7270/Q25H7FBV 8709095 Jirousek, MR; Gillig, JR; Gonzalez, CM; Heath, WF; McDonald, JH; Neel, DA; Rito, CJ; Singh, U; Stramm, LE; Melikian-Badalian, A; Baevsky, M; Ballas, LM; Hall, SE; Winneroski, LL; Faul, MM 9/10/1996 11/10/2009 Eli Lilly http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50052037 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=602&target=Protein+kinase+C+gamma+type&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50052037&enzyme=Protein+kinase+C+gamma+type&column=ki&startPg=0&Increment=50&submit=Search 10527068 103948962 CHEMBL316239 1 MAGLGPGVGDSEGGPRPLFCRKGALRQKVVHEVKSHKFTARFFKQPTFCSHCTDFIWGIGKQGLQCQVCSFVVHRRCHEFVTFECPGAGKGPQTDDPRNKHKFRLHSYSSPTFCDHCGSLLYGLVHQGMKCSCCEMNVHRRCVRSVPSLCGVDHTERRGRLQLEIRAPTADEIHVTVGEARNLIPMDPNGLSDPYVKLKLIPDPRNLTKQKTRTVKATLNPVWNETFVFNLKPGDVERRLSVEVWDWDRTSRNDFMGAMSFGVSELLKAPVDGWYKLLNQEEGEYYNVPVADADNCSLLQKFEACNYPLELYERVRMGPSSSPIPSPSPSPTDPKRCFFGASPGRLHISDFSFLMVLGKGSFGKVMLAERRGSDELYAIKILKKDVIVQDDDVDCTLVEKRVLALGGRGPGGRPHFLTQLHSTFQTPDRLYFVMEYVTGGDLMYHIQQLGKFKEPHAAFYAAEIAIGLFFLHNQGIIYRDLKLDNVMLDAEGHIKITDFGMCKENVFPGTTTRTFCGTPDYIAPEIIAYQPYGKSVDWWSFGVLLYEMLAGQPPFDGEDEEELFQAIMEQTVTYPKSLSREAVAICKGFLTKHPGKRLGSGPDGEPTIRAHGFFRWIDWERLERLEIPPPFRPRPCGRSGENFDKFFTRAAPALTPPDRLVLASIDQADFQGFTYVNPDFVHPDARSPTSPVPVPVM 2UZP Protein kinase C gamma type KPCG_HUMAN P05129 B7Z8Q0 50085284 NC[C@@H]1CCn2cc(C3=C(C(=O)NC3=O)c3cn(CCO1)c1ccccc31)c1ccccc21 |t:8| InChI=1S/C26H24N4O3/c27-13-16-9-10-29-14-19(17-5-1-3-7-21(17)29)23-24(26(32)28-25(23)31)20-15-30(11-12-33-16)22-8-4-2-6-18(20)22/h1-8,14-16H,9-13,27H2,(H,28,31,32) JPLUPRIZLHXUPQ-UHFFFAOYSA-N 50052037 18-aminomethyl-(18S)-17-oxa-4,14,21-triazahexacyclo[19.6.1.17,14.02,6.08,13.022,27]nonacosa-1(28),2(6),7(29),8(13),9,11,22(27),23,25-nonaene-3,5-dione::CHEMBL316239 Protein kinase C zeta type Homo sapiens 44000 ChEMBL 10.1021/jm950588y 10.7270/Q25H7FBV 8709095 Jirousek, MR; Gillig, JR; Gonzalez, CM; Heath, WF; McDonald, JH; Neel, DA; Rito, CJ; Singh, U; Stramm, LE; Melikian-Badalian, A; Baevsky, M; Ballas, LM; Hall, SE; Winneroski, LL; Faul, MM 9/10/1996 11/10/2009 Eli Lilly http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50052037 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=606&target=Protein+kinase+C+zeta+type&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50052037&enzyme=Protein+kinase+C+zeta+type&column=ki&startPg=0&Increment=50&submit=Search 10527068 103948962 CHEMBL316239 1 MPSRTGPKMEGSGGRVRLKAHYGGDIFITSVDAATTFEELCEEVRDMCRLHQQHPLTLKWVDSEGDPCTVSSQMELEEAFRLARQCRDEGLIIHVFPSTPEQPGLPCPGEDKSIYRRGARRWRKLYRANGHLFQAKRFNRRAYCGQCSERIWGLARQGYRCINCKLLVHKRCHGLVPLTCRKHMDSVMPSQEPPVDDKNEDADLPSEETDGIAYISSSRKHDSIKDDSEDLKPVIDGMDGIKISQGLGLQDFDLIRVIGRGSYAKVLLVRLKKNDQIYAMKVVKKELVHDDEDIDWVQTEKHVFEQASSNPFLVGLHSCFQTTSRLFLVIEYVNGGDLMFHMQRQRKLPEEHARFYAAEICIALNFLHERGIIYRDLKLDNVLLDADGHIKLTDYGMCKEGLGPGDTTSTFCGTPNYIAPEILRGEEYGFSVDWWALGVLMFEMMAGRSPFDIITDNPDMNTEDYLFQVILEKPIRIPRFLSVKASHVLKGFLNKDPKERLGCRPQTGFSDIKSHAFFRSIDWDLLEKKQALPPFQPQITDDYGLDNFDTQFTSEPVQLTPDDEDAIKRIDQSEFEGFEYINPLLLSTEESV Protein kinase C zeta type KPCZ_HUMAN Q05513 A8K4N0 A8MU64 B7Z2J7 E9PCW2 Q15207 Q5SYT5 Q969S4 50085285 OC[C@@H]1CCn2cc(C3=C(C(=O)NC3=O)c3cn(CCO1)c1ccccc31)c1ccccc21 |t:8| InChI=1S/C26H23N3O4/c30-15-16-9-10-28-13-19(17-5-1-3-7-21(17)28)23-24(26(32)27-25(23)31)20-14-29(11-12-33-16)22-8-4-2-6-18(20)22/h1-8,13-14,16,30H,9-12,15H2,(H,27,31,32) BGVKOUSMQGMSDY-UHFFFAOYSA-N 50052039 18-hydroxymethyl-(18S)-17-oxa-4,14,21-triazahexacyclo[19.6.1.17,14.02,6.08,13.022,27]nonacosa-1(28),2(6),7(29),8(13),9,11,22(27),23,25-nonaene-3,5-dione::LY-326449::CHEMBL292495 Proto-oncogene tyrosine-protein kinase Src Homo sapiens >100000 ChEMBL 10.1021/jm950588y 10.7270/Q25H7FBV 8709095 Jirousek, MR; Gillig, JR; Gonzalez, CM; Heath, WF; McDonald, JH; Neel, DA; Rito, CJ; Singh, U; Stramm, LE; Melikian-Badalian, A; Baevsky, M; Ballas, LM; Hall, SE; Winneroski, LL; Faul, MM 9/10/1996 11/10/2009 Eli Lilly http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50052039 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=13&target=Proto-oncogene+tyrosine-protein+kinase+Src&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50052039&enzyme=Proto-oncogene+tyrosine-protein+kinase+Src&column=ki&startPg=0&Increment=50&submit=Search 10455969 103948964 CHEMBL292495 1 MGSNKSKPKDASQRRRSLEPAENVHGAGGGAFPASQTPSKPASADGHRGPSAAFAPAAAEPKLFGGFNSSDTVTSPQRAGPLAGGVTTFVALYDYESRTETDLSFKKGERLQIVNNTEGDWWLAHSLSTGQTGYIPSNYVAPSDSIQAEEWYFGKITRRESERLLLNAENPRGTFLVRESETTKGAYCLSVSDFDNAKGLNVKHYKIRKLDSGGFYITSRTQFNSLQQLVAYYSKHADGLCHRLTTVCPTSKPQTQGLAKDAWEIPRESLRLEVKLGQGCFGEVWMGTWNGTTRVAIKTLKPGTMSPEAFLQEAQVMKKLRHEKLVQLYAVVSEEPIYIVTEYMSKGSLLDFLKGETGKYLRLPQLVDMAAQIASGMAYVERMNYVHRDLRAANILVGENLVCKVADFGLARLIEDNEYTARQGAKFPIKWTAPEAALYGRFTIKSDVWSFGILLTELTTKGRVPYPGMVNREVLDQVERGYRMPCPPECPESLHDLMCQCWRKEPEERPTFEYLQAFLEDYFTSTEPQYQPGENL 8JN9,8JN8,2H8H,2SRC,1Y57,1FMK,2PTK,9NS0,8JF3,6ATE,4MXO,4MXX,2BDJ,2BDF,8HAQ,6E6E,1YI6 Proto-oncogene tyrosine-protein kinase Src SRC_HUMAN P12931 E1P5V4 Q76P87 Q86VB9 Q9H5A8 50085286 O=C1NC(=O)C2=C1c1cn(CCO[C@H](CNS(=O)(=O)c3ccccc3)CCn3cc2c2ccccc32)c2ccccc12 |c:5| InChI=1S/C32H28N4O5S/c37-31-29-25-19-35(27-12-6-4-10-23(25)27)15-14-21(18-33-42(39,40)22-8-2-1-3-9-22)41-17-16-36-20-26(30(29)32(38)34-31)24-11-5-7-13-28(24)36/h1-13,19-21,33H,14-18H2,(H,34,37,38) ADVDNJCNXOTAHZ-UHFFFAOYSA-N 50052036 3,5-dioxo-17-phenylsulfonamidomethyl-(17S)-18-oxa-4,14,21-triazahexacyclo[19.6.1.17,14.02,6.08,13.022,27]nonacosa-1(28),2(6),7(29),8(13),9,11,22(27),23,25-nonaene::CHEMBL315389 Proto-oncogene tyrosine-protein kinase Src Homo sapiens >100000 ChEMBL 10.1021/jm950588y 10.7270/Q25H7FBV 8709095 Jirousek, MR; Gillig, JR; Gonzalez, CM; Heath, WF; McDonald, JH; Neel, DA; Rito, CJ; Singh, U; Stramm, LE; Melikian-Badalian, A; Baevsky, M; Ballas, LM; Hall, SE; Winneroski, LL; Faul, MM 9/10/1996 11/10/2009 Eli Lilly http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50052036 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=13&target=Proto-oncogene+tyrosine-protein+kinase+Src&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50052036&enzyme=Proto-oncogene+tyrosine-protein+kinase+Src&column=ki&startPg=0&Increment=50&submit=Search 10650891 103948961 CHEMBL315389 1 MGSNKSKPKDASQRRRSLEPAENVHGAGGGAFPASQTPSKPASADGHRGPSAAFAPAAAEPKLFGGFNSSDTVTSPQRAGPLAGGVTTFVALYDYESRTETDLSFKKGERLQIVNNTEGDWWLAHSLSTGQTGYIPSNYVAPSDSIQAEEWYFGKITRRESERLLLNAENPRGTFLVRESETTKGAYCLSVSDFDNAKGLNVKHYKIRKLDSGGFYITSRTQFNSLQQLVAYYSKHADGLCHRLTTVCPTSKPQTQGLAKDAWEIPRESLRLEVKLGQGCFGEVWMGTWNGTTRVAIKTLKPGTMSPEAFLQEAQVMKKLRHEKLVQLYAVVSEEPIYIVTEYMSKGSLLDFLKGETGKYLRLPQLVDMAAQIASGMAYVERMNYVHRDLRAANILVGENLVCKVADFGLARLIEDNEYTARQGAKFPIKWTAPEAALYGRFTIKSDVWSFGILLTELTTKGRVPYPGMVNREVLDQVERGYRMPCPPECPESLHDLMCQCWRKEPEERPTFEYLQAFLEDYFTSTEPQYQPGENL 8JN9,8JN8,2H8H,2SRC,1Y57,1FMK,2PTK,9NS0,8JF3,6ATE,4MXO,4MXX,2BDJ,2BDF,8HAQ,6E6E,1YI6 Proto-oncogene tyrosine-protein kinase Src SRC_HUMAN P12931 E1P5V4 Q76P87 Q86VB9 Q9H5A8 50085290 CNC[C@@H]1CCn2cc(C3=C(C(=O)NC3=O)c3cn(CCO1)c1ccccc31)c1ccccc21 |t:9| InChI=1S/C27H26N4O3/c1-28-14-17-10-11-30-15-20(18-6-2-4-8-22(18)30)24-25(27(33)29-26(24)32)21-16-31(12-13-34-17)23-9-5-3-7-19(21)23/h2-9,15-17,28H,10-14H2,1H3,(H,29,32,33) ZEYTZKVCOZMUKL-UHFFFAOYSA-N 50052034 18-methylaminomethyl-(18S)-17-oxa-4,14,21-triazahexacyclo[19.6.1.17,14.02,6.08,13.022,27]nonacosa-1(28),2(6),7(29),8(13),9,11,22(27),23,25-nonaene-3,5-dione::CHEMBL311543 Protein kinase C gamma type Homo sapiens 270 ChEMBL 10.1021/jm950588y 10.7270/Q25H7FBV 8709095 Jirousek, MR; Gillig, JR; Gonzalez, CM; Heath, WF; McDonald, JH; Neel, DA; Rito, CJ; Singh, U; Stramm, LE; Melikian-Badalian, A; Baevsky, M; Ballas, LM; Hall, SE; Winneroski, LL; Faul, MM 9/10/1996 11/10/2009 Eli Lilly http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50052034 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=602&target=Protein+kinase+C+gamma+type&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50052034&enzyme=Protein+kinase+C+gamma+type&column=ki&startPg=0&Increment=50&submit=Search 10671412 103948959 CHEMBL311543 1 MAGLGPGVGDSEGGPRPLFCRKGALRQKVVHEVKSHKFTARFFKQPTFCSHCTDFIWGIGKQGLQCQVCSFVVHRRCHEFVTFECPGAGKGPQTDDPRNKHKFRLHSYSSPTFCDHCGSLLYGLVHQGMKCSCCEMNVHRRCVRSVPSLCGVDHTERRGRLQLEIRAPTADEIHVTVGEARNLIPMDPNGLSDPYVKLKLIPDPRNLTKQKTRTVKATLNPVWNETFVFNLKPGDVERRLSVEVWDWDRTSRNDFMGAMSFGVSELLKAPVDGWYKLLNQEEGEYYNVPVADADNCSLLQKFEACNYPLELYERVRMGPSSSPIPSPSPSPTDPKRCFFGASPGRLHISDFSFLMVLGKGSFGKVMLAERRGSDELYAIKILKKDVIVQDDDVDCTLVEKRVLALGGRGPGGRPHFLTQLHSTFQTPDRLYFVMEYVTGGDLMYHIQQLGKFKEPHAAFYAAEIAIGLFFLHNQGIIYRDLKLDNVMLDAEGHIKITDFGMCKENVFPGTTTRTFCGTPDYIAPEIIAYQPYGKSVDWWSFGVLLYEMLAGQPPFDGEDEEELFQAIMEQTVTYPKSLSREAVAICKGFLTKHPGKRLGSGPDGEPTIRAHGFFRWIDWERLERLEIPPPFRPRPCGRSGENFDKFFTRAAPALTPPDRLVLASIDQADFQGFTYVNPDFVHPDARSPTSPVPVPVM 2UZP Protein kinase C gamma type KPCG_HUMAN P05129 B7Z8Q0 50085292 CN1CCN(C[C@@H]2CCn3cc(C4=C(C(=O)NC4=O)c4cn(CCO2)c2ccccc42)c2ccccc32)CC1 |t:12| InChI=1S/C31H33N5O3/c1-33-12-14-34(15-13-33)18-21-10-11-35-19-24(22-6-2-4-8-26(22)35)28-29(31(38)32-30(28)37)25-20-36(16-17-39-21)27-9-5-3-7-23(25)27/h2-9,19-21H,10-18H2,1H3,(H,32,37,38) QKXPAKQCFJVAFI-UHFFFAOYSA-N 50052041 18-(4-methylhexahydro-1-pyrazinylmethyl)-(18S)-17-oxa-4,14,21-triazahexacyclo[19.6.1.17,14.02,6.08,13.022,27]nonacosa-1(28),2(6),7(29),8(13),9,11,22(27),23,25-nonaene-3,5-dione::CHEMBL91959 Protein kinase C epsilon type Homo sapiens >5000 ChEMBL 10.1021/jm950588y 10.7270/Q25H7FBV 8709095 Jirousek, MR; Gillig, JR; Gonzalez, CM; Heath, WF; McDonald, JH; Neel, DA; Rito, CJ; Singh, U; Stramm, LE; Melikian-Badalian, A; Baevsky, M; Ballas, LM; Hall, SE; Winneroski, LL; Faul, MM 9/10/1996 11/10/2009 Eli Lilly http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50052041 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=604&target=Protein+kinase+C+epsilon+type&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50052041&enzyme=Protein+kinase+C+epsilon+type&column=ki&startPg=0&Increment=50&submit=Search 10768377 103948966 CHEMBL91959 1 MVVFNGLLKIKICEAVSLKPTAWSLRHAVGPRPQTFLLDPYIALNVDDSRIGQTATKQKTNSPAWHDEFVTDVCNGRKIELAVFHDAPIGYDDFVANCTIQFEELLQNGSRHFEDWIDLEPEGRVYVIIDLSGSSGEAPKDNEERVFRERMRPRKRQGAVRRRVHQVNGHKFMATYLRQPTYCSHCRDFIWGVIGKQGYQCQVCTCVVHKRCHELIITKCAGLKKQETPDQVGSQRFSVNMPHKFGIHNYKVPTFCDHCGSLLWGLLRQGLQCKVCKMNVHRRCETNVAPNCGVDARGIAKVLADLGVTPDKITNSGQRRKKLIAGAESPQPASGSSPSEEDRSKSAPTSPCDQEIKELENNIRKALSFDNRGEEHRAASSPDGQLMSPGENGEVRQGQAKRLGLDEFNFIKVLGKGSFGKVMLAELKGKDEVYAVKVLKKDVILQDDDVDCTMTEKRILALARKHPYLTQLYCCFQTKDRLFFVMEYVNGGDLMFQIQRSRKFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILLDAEGHCKLADFGMCKEGILNGVTTTTFCGTPDYIAPEILQELEYGPSVDWWALGVLMYEMMAGQPPFEADNEDDLFESILHDDVLYPVWLSKEAVSILKAFMTKNPHKRLGCVASQNGEDAIKQHPFFKEIDWVLLEQKKIKPPFKPRIKTKRDVNNFDQDFTREEPVLTLVDEAIVKQINQEEFKGFSYFGEDLMP Protein kinase C epsilon type KPCE_HUMAN Q02156 B0LPH7 Q32MQ3 Q53SL4 Q53SM5 Q9UE81 50085296 O=C1NC(=O)C2=C1c1cn(CCO[C@H](CN3CCCC3)CCn3cc2c2ccccc32)c2ccccc12 |c:5| InChI=1S/C30H30N4O3/c35-29-27-23-18-33(25-9-3-1-7-21(23)25)14-11-20(17-32-12-5-6-13-32)37-16-15-34-19-24(28(27)30(36)31-29)22-8-2-4-10-26(22)34/h1-4,7-10,18-20H,5-6,11-17H2,(H,31,35,36) WORLFHNBHSSAJQ-UHFFFAOYSA-N 50052038 18-tetrahydro-1H-1-pyrrolylmethyl-(18S)-17-oxa-4,14,21-triazahexacyclo[19.6.1.17,14.02,6.08,13.022,27]nonacosa-1(28),2(6),7(29),8(13),9,11,22(27),23,25-nonaene-3,5-dione::CHEMBL419866 Protein kinase C gamma type Homo sapiens 2200 ChEMBL 10.1021/jm950588y 10.7270/Q25H7FBV 8709095 Jirousek, MR; Gillig, JR; Gonzalez, CM; Heath, WF; McDonald, JH; Neel, DA; Rito, CJ; Singh, U; Stramm, LE; Melikian-Badalian, A; Baevsky, M; Ballas, LM; Hall, SE; Winneroski, LL; Faul, MM 9/10/1996 11/10/2009 Eli Lilly http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50052038 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=602&target=Protein+kinase+C+gamma+type&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50052038&enzyme=Protein+kinase+C+gamma+type&column=ki&startPg=0&Increment=50&submit=Search 11799388 103948963 CHEMBL419866 1 MAGLGPGVGDSEGGPRPLFCRKGALRQKVVHEVKSHKFTARFFKQPTFCSHCTDFIWGIGKQGLQCQVCSFVVHRRCHEFVTFECPGAGKGPQTDDPRNKHKFRLHSYSSPTFCDHCGSLLYGLVHQGMKCSCCEMNVHRRCVRSVPSLCGVDHTERRGRLQLEIRAPTADEIHVTVGEARNLIPMDPNGLSDPYVKLKLIPDPRNLTKQKTRTVKATLNPVWNETFVFNLKPGDVERRLSVEVWDWDRTSRNDFMGAMSFGVSELLKAPVDGWYKLLNQEEGEYYNVPVADADNCSLLQKFEACNYPLELYERVRMGPSSSPIPSPSPSPTDPKRCFFGASPGRLHISDFSFLMVLGKGSFGKVMLAERRGSDELYAIKILKKDVIVQDDDVDCTLVEKRVLALGGRGPGGRPHFLTQLHSTFQTPDRLYFVMEYVTGGDLMYHIQQLGKFKEPHAAFYAAEIAIGLFFLHNQGIIYRDLKLDNVMLDAEGHIKITDFGMCKENVFPGTTTRTFCGTPDYIAPEIIAYQPYGKSVDWWSFGVLLYEMLAGQPPFDGEDEEELFQAIMEQTVTYPKSLSREAVAICKGFLTKHPGKRLGSGPDGEPTIRAHGFFRWIDWERLERLEIPPPFRPRPCGRSGENFDKFFTRAAPALTPPDRLVLASIDQADFQGFTYVNPDFVHPDARSPTSPVPVPVM 2UZP Protein kinase C gamma type KPCG_HUMAN P05129 B7Z8Q0 50085297 O=C1NC(=O)C2=C1c1cn(CCO[C@H](CNS(=O)(=O)c3ccccc3)CCn3cc2c2ccccc32)c2ccccc12 |c:5| InChI=1S/C32H28N4O5S/c37-31-29-25-19-35(27-12-6-4-10-23(25)27)15-14-21(18-33-42(39,40)22-8-2-1-3-9-22)41-17-16-36-20-26(30(29)32(38)34-31)24-11-5-7-13-28(24)36/h1-13,19-21,33H,14-18H2,(H,34,37,38) ADVDNJCNXOTAHZ-UHFFFAOYSA-N 50052036 3,5-dioxo-17-phenylsulfonamidomethyl-(17S)-18-oxa-4,14,21-triazahexacyclo[19.6.1.17,14.02,6.08,13.022,27]nonacosa-1(28),2(6),7(29),8(13),9,11,22(27),23,25-nonaene::CHEMBL315389 Protein kinase C zeta type Homo sapiens >5000 ChEMBL 10.1021/jm950588y 10.7270/Q25H7FBV 8709095 Jirousek, MR; Gillig, JR; Gonzalez, CM; Heath, WF; McDonald, JH; Neel, DA; Rito, CJ; Singh, U; Stramm, LE; Melikian-Badalian, A; Baevsky, M; Ballas, LM; Hall, SE; Winneroski, LL; Faul, MM 9/10/1996 11/10/2009 Eli Lilly http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50052036 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=606&target=Protein+kinase+C+zeta+type&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50052036&enzyme=Protein+kinase+C+zeta+type&column=ki&startPg=0&Increment=50&submit=Search 10650891 103948961 CHEMBL315389 1 MPSRTGPKMEGSGGRVRLKAHYGGDIFITSVDAATTFEELCEEVRDMCRLHQQHPLTLKWVDSEGDPCTVSSQMELEEAFRLARQCRDEGLIIHVFPSTPEQPGLPCPGEDKSIYRRGARRWRKLYRANGHLFQAKRFNRRAYCGQCSERIWGLARQGYRCINCKLLVHKRCHGLVPLTCRKHMDSVMPSQEPPVDDKNEDADLPSEETDGIAYISSSRKHDSIKDDSEDLKPVIDGMDGIKISQGLGLQDFDLIRVIGRGSYAKVLLVRLKKNDQIYAMKVVKKELVHDDEDIDWVQTEKHVFEQASSNPFLVGLHSCFQTTSRLFLVIEYVNGGDLMFHMQRQRKLPEEHARFYAAEICIALNFLHERGIIYRDLKLDNVLLDADGHIKLTDYGMCKEGLGPGDTTSTFCGTPNYIAPEILRGEEYGFSVDWWALGVLMFEMMAGRSPFDIITDNPDMNTEDYLFQVILEKPIRIPRFLSVKASHVLKGFLNKDPKERLGCRPQTGFSDIKSHAFFRSIDWDLLEKKQALPPFQPQITDDYGLDNFDTQFTSEPVQLTPDDEDAIKRIDQSEFEGFEYINPLLLSTEESV Protein kinase C zeta type KPCZ_HUMAN Q05513 A8K4N0 A8MU64 B7Z2J7 E9PCW2 Q15207 Q5SYT5 Q969S4 50085299 O=C1NC(=O)C2=C1c1cn(CCO[C@H](CN3CCOCC3)CCn3cc2c2ccccc32)c2ccccc12 |c:5| InChI=1S/C30H30N4O4/c35-29-27-23-18-33(25-7-3-1-5-21(23)25)10-9-20(17-32-11-14-37-15-12-32)38-16-13-34-19-24(28(27)30(36)31-29)22-6-2-4-8-26(22)34/h1-8,18-20H,9-17H2,(H,31,35,36) CLHMTFQYMLYQME-UHFFFAOYSA-N 50052035 18-(1,4-oxazinan-4-ylmethyl)-(18S)-17-oxa-4,14,21-triazahexacyclo[19.6.1.17,14.02,6.08,13.022,27]nonacosa-1(28),2(6),7(29),8(13),9,11,22(27),23,25-nonaene-3,5-dione::CHEMBL315357 Protein kinase C delta type Homo sapiens 2000 ChEMBL 10.1021/jm950588y 10.7270/Q25H7FBV 8709095 Jirousek, MR; Gillig, JR; Gonzalez, CM; Heath, WF; McDonald, JH; Neel, DA; Rito, CJ; Singh, U; Stramm, LE; Melikian-Badalian, A; Baevsky, M; Ballas, LM; Hall, SE; Winneroski, LL; Faul, MM 9/10/1996 11/10/2009 Eli Lilly http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50052035 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=603&target=Protein+kinase+C+delta+type&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50052035&enzyme=Protein+kinase+C+delta+type&column=ki&startPg=0&Increment=50&submit=Search 10673286 103948960 CHEMBL315357 1 MAPFLRIAFNSYELGSLQAEDEANQPFCAVKMKEALSTERGKTLVQKKPTMYPEWKSTFDAHIYEGRVIQIVLMRAAEEPVSEVTVGVSVLAERCKKNNGKAEFWLDLQPQAKVLMSVQYFLEDVDCKQSMRSEDEAKFPTMNRRGAIKQAKIHYIKNHEFIATFFGQPTFCSVCKDFVWGLNKQGYKCRQCNAAIHKKCIDKIIGRCTGTAANSRDTIFQKERFNIDMPHRFKVHNYMSPTFCDHCGSLLWGLVKQGLKCEDCGMNVHHKCREKVANLCGINQKLLAEALNQVTQRASRRSDSASSEPVGIYQGFEKKTGVAGEDMQDNSGTYGKIWEGSSKCNINNFIFHKVLGKGSFGKVLLGELKGRGEYFAIKALKKDVVLIDDDVECTMVEKRVLTLAAENPFLTHLICTFQTKDHLFFVMEFLNGGDLMYHIQDKGRFELYRATFYAAEIMCGLQFLHSKGIIYRDLKLDNVLLDRDGHIKIADFGMCKENIFGESRASTFCGTPDYIAPEILQGLKYTFSVDWWSFGVLLYEMLIGQSPFHGDDEDELFESIRVDTPHYPRWITKESKDILEKLFEREPTKRLGVTGNIKIHPFFKTINWTLLEKRRLEPPFRPKVKSPRDYSNFDQEFLNEKARLSYSDKNLIDSMDQSAFAGFSFVNPKFEHLLED 1YRK Protein kinase C delta type KPCD_HUMAN Q05655 B0KZ81 B2R834 Q15144 Q86XJ6 50085302 O=C1NC(=O)C2=C1c1cn(CCO[C@H](CNS(=O)(=O)c3ccccc3)CCn3cc2c2ccccc32)c2ccccc12 |c:5| InChI=1S/C32H28N4O5S/c37-31-29-25-19-35(27-12-6-4-10-23(25)27)15-14-21(18-33-42(39,40)22-8-2-1-3-9-22)41-17-16-36-20-26(30(29)32(38)34-31)24-11-5-7-13-28(24)36/h1-13,19-21,33H,14-18H2,(H,34,37,38) ADVDNJCNXOTAHZ-UHFFFAOYSA-N 50052036 3,5-dioxo-17-phenylsulfonamidomethyl-(17S)-18-oxa-4,14,21-triazahexacyclo[19.6.1.17,14.02,6.08,13.022,27]nonacosa-1(28),2(6),7(29),8(13),9,11,22(27),23,25-nonaene::CHEMBL315389 Protein kinase C delta type Homo sapiens 880.0 ChEMBL 10.1021/jm950588y 10.7270/Q25H7FBV 8709095 Jirousek, MR; Gillig, JR; Gonzalez, CM; Heath, WF; McDonald, JH; Neel, DA; Rito, CJ; Singh, U; Stramm, LE; Melikian-Badalian, A; Baevsky, M; Ballas, LM; Hall, SE; Winneroski, LL; Faul, MM 9/10/1996 11/10/2009 Eli Lilly http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50052036 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=603&target=Protein+kinase+C+delta+type&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50052036&enzyme=Protein+kinase+C+delta+type&column=ki&startPg=0&Increment=50&submit=Search 10650891 103948961 CHEMBL315389 1 MAPFLRIAFNSYELGSLQAEDEANQPFCAVKMKEALSTERGKTLVQKKPTMYPEWKSTFDAHIYEGRVIQIVLMRAAEEPVSEVTVGVSVLAERCKKNNGKAEFWLDLQPQAKVLMSVQYFLEDVDCKQSMRSEDEAKFPTMNRRGAIKQAKIHYIKNHEFIATFFGQPTFCSVCKDFVWGLNKQGYKCRQCNAAIHKKCIDKIIGRCTGTAANSRDTIFQKERFNIDMPHRFKVHNYMSPTFCDHCGSLLWGLVKQGLKCEDCGMNVHHKCREKVANLCGINQKLLAEALNQVTQRASRRSDSASSEPVGIYQGFEKKTGVAGEDMQDNSGTYGKIWEGSSKCNINNFIFHKVLGKGSFGKVLLGELKGRGEYFAIKALKKDVVLIDDDVECTMVEKRVLTLAAENPFLTHLICTFQTKDHLFFVMEFLNGGDLMYHIQDKGRFELYRATFYAAEIMCGLQFLHSKGIIYRDLKLDNVLLDRDGHIKIADFGMCKENIFGESRASTFCGTPDYIAPEILQGLKYTFSVDWWSFGVLLYEMLIGQSPFHGDDEDELFESIRVDTPHYPRWITKESKDILEKLFEREPTKRLGVTGNIKIHPFFKTINWTLLEKRRLEPPFRPKVKSPRDYSNFDQEFLNEKARLSYSDKNLIDSMDQSAFAGFSFVNPKFEHLLED 1YRK Protein kinase C delta type KPCD_HUMAN Q05655 B0KZ81 B2R834 Q15144 Q86XJ6 50085304 O=C1NC(=O)C2=C1c1cn(CCO[C@H](CNS(=O)(=O)c3ccccc3)CCn3cc2c2ccccc32)c2ccccc12 |c:5| InChI=1S/C32H28N4O5S/c37-31-29-25-19-35(27-12-6-4-10-23(25)27)15-14-21(18-33-42(39,40)22-8-2-1-3-9-22)41-17-16-36-20-26(30(29)32(38)34-31)24-11-5-7-13-28(24)36/h1-13,19-21,33H,14-18H2,(H,34,37,38) ADVDNJCNXOTAHZ-UHFFFAOYSA-N 50052036 3,5-dioxo-17-phenylsulfonamidomethyl-(17S)-18-oxa-4,14,21-triazahexacyclo[19.6.1.17,14.02,6.08,13.022,27]nonacosa-1(28),2(6),7(29),8(13),9,11,22(27),23,25-nonaene::CHEMBL315389 Protein kinase C epsilon type Homo sapiens >5000 ChEMBL 10.1021/jm950588y 10.7270/Q25H7FBV 8709095 Jirousek, MR; Gillig, JR; Gonzalez, CM; Heath, WF; McDonald, JH; Neel, DA; Rito, CJ; Singh, U; Stramm, LE; Melikian-Badalian, A; Baevsky, M; Ballas, LM; Hall, SE; Winneroski, LL; Faul, MM 9/10/1996 11/10/2009 Eli Lilly http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50052036 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=604&target=Protein+kinase+C+epsilon+type&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50052036&enzyme=Protein+kinase+C+epsilon+type&column=ki&startPg=0&Increment=50&submit=Search 10650891 103948961 CHEMBL315389 1 MVVFNGLLKIKICEAVSLKPTAWSLRHAVGPRPQTFLLDPYIALNVDDSRIGQTATKQKTNSPAWHDEFVTDVCNGRKIELAVFHDAPIGYDDFVANCTIQFEELLQNGSRHFEDWIDLEPEGRVYVIIDLSGSSGEAPKDNEERVFRERMRPRKRQGAVRRRVHQVNGHKFMATYLRQPTYCSHCRDFIWGVIGKQGYQCQVCTCVVHKRCHELIITKCAGLKKQETPDQVGSQRFSVNMPHKFGIHNYKVPTFCDHCGSLLWGLLRQGLQCKVCKMNVHRRCETNVAPNCGVDARGIAKVLADLGVTPDKITNSGQRRKKLIAGAESPQPASGSSPSEEDRSKSAPTSPCDQEIKELENNIRKALSFDNRGEEHRAASSPDGQLMSPGENGEVRQGQAKRLGLDEFNFIKVLGKGSFGKVMLAELKGKDEVYAVKVLKKDVILQDDDVDCTMTEKRILALARKHPYLTQLYCCFQTKDRLFFVMEYVNGGDLMFQIQRSRKFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILLDAEGHCKLADFGMCKEGILNGVTTTTFCGTPDYIAPEILQELEYGPSVDWWALGVLMYEMMAGQPPFEADNEDDLFESILHDDVLYPVWLSKEAVSILKAFMTKNPHKRLGCVASQNGEDAIKQHPFFKEIDWVLLEQKKIKPPFKPRIKTKRDVNNFDQDFTREEPVLTLVDEAIVKQINQEEFKGFSYFGEDLMP Protein kinase C epsilon type KPCE_HUMAN Q02156 B0LPH7 Q32MQ3 Q53SL4 Q53SM5 Q9UE81 50085305 O=C1NC(=O)C2=C1c1cn(CCO[C@H](CNCc3ccccc3)CCn3cc2c2ccccc32)c2ccccc12 |c:5| InChI=1S/C33H30N4O3/c38-32-30-26-20-36(28-12-6-4-10-24(26)28)15-14-23(19-34-18-22-8-2-1-3-9-22)40-17-16-37-21-27(31(30)33(39)35-32)25-11-5-7-13-29(25)37/h1-13,20-21,23,34H,14-19H2,(H,35,38,39) RIXHNSFDUIBDSB-UHFFFAOYSA-N 50052040 18-benzylaminomethyl-(18S)-17-oxa-4,14,21-triazahexacyclo[19.6.1.17,14.02,6.08,13.022,27]nonacosa-1(28),2(6),7(29),8(13),9,11,22(27),23,25-nonaene-3,5-dione::CHEMBL328229 Protein kinase C beta type Homo sapiens 330 ChEMBL 10.1021/jm950588y 10.7270/Q25H7FBV 8709095 Jirousek, MR; Gillig, JR; Gonzalez, CM; Heath, WF; McDonald, JH; Neel, DA; Rito, CJ; Singh, U; Stramm, LE; Melikian-Badalian, A; Baevsky, M; Ballas, LM; Hall, SE; Winneroski, LL; Faul, MM 9/10/1996 11/10/2009 Eli Lilly http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50052040 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=600&target=Protein+kinase+C+beta+type&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50052040&enzyme=Protein+kinase+C+beta+type&column=ki&startPg=0&Increment=50&submit=Search 10768554 103948965 CHEMBL328229 1 MADPAAGPPPSEGEESTVRFARKGALRQKNVHEVKNHKFTARFFKQPTFCSHCTDFIWGFGKQGFQCQVCCFVVHKRCHEFVTFSCPGADKGPASDDPRSKHKFKIHTYSSPTFCDHCGSLLYGLIHQGMKCDTCMMNVHKRCVMNVPSLCGTDHTERRGRIYIQAHIDRDVLIVLVRDAKNLVPMDPNGLSDPYVKLKLIPDPKSESKQKTKTIKCSLNPEWNETFRFQLKESDKDRRLSVEIWDWDLTSRNDFMGSLSFGISELQKASVDGWFKLLSQEEGEYFNVPVPPEGSEANEELRQKFERAKISQGTKVPEEKTTNTVSKFDNNGNRDRMKLTDFNFLMVLGKGSFGKVMLSERKGTDELYAVKILKKDVVIQDDDVECTMVEKRVLALPGKPPFLTQLHSCFQTMDRLYFVMEYVNGGDLMYHIQQVGRFKEPHAVFYAAEIAIGLFFLQSKGIIYRDLKLDNVMLDSEGHIKIADFGMCKENIWDGVTTKTFCGTPDYIAPEIIAYQPYGKSVDWWAFGVLLYEMLAGQAPFEGEDEDELFQSIMEHNVAYPKSMSKEAVAICKGLMTKHPGKRLGCGPEGERDIKEHAFFRYIDWEKLERKEIQPPYKPKARDKRDTSNFDKEFTRQPVELTPTDKLFIMNLDQNEFAGFSYTNPEFVINV 8SE4,8SE3,8SE2,3PFQ,9C5F,1A25 Protein kinase C beta type KPCB_HUMAN P05771 C5IFJ8 D3DWF5 O43744 P05127 Q15138 Q93060 Q9UE49 Q9UE50 Q9UEH8 Q9UJ30 Q9UJ33 50085311 CN(C)C[C@@H]1CCn2cc(C3=C(C(=O)NC3=O)c3cn(CCO1)c1ccccc31)c1ccccc21 |r,t:10| InChI=1S/C28H28N4O3/c1-30(2)15-18-11-12-31-16-21(19-7-3-5-9-23(19)31)25-26(28(34)29-27(25)33)22-17-32(13-14-35-18)24-10-6-4-8-20(22)24/h3-10,16-18H,11-15H2,1-2H3,(H,29,33,34) ZCBUQCWBWNUWSU-UHFFFAOYSA-N 17055 (9S)-9-[(dimethylamino)methyl]-6,7,10,11-tetrahydro-9H,18H-5,21:12,17-di(metheno)dibenzo[e,k]pyrrolo[3,4-h][1,4,13]oxadiazacyclohexadecine-18,20(19H)-dione::(18S)-18-[(dimethylamino)methyl]-17-oxa-4,14,21-triazahexacyclo[19.6.1.1^{7,14}.0^{2,6}.0^{8,13}.0^{22,27}]nonacosa-1(28),2(6),7(29),8(13),9,11,22(27),23,25-nonaene-3,5-dione::K00587a::Ruboxistaurin::LY-333531::cid_153999::LY 333531::LY333531 Protein kinase C beta type Homo sapiens 4.7 ChEMBL 10.1021/jm950588y 10.7270/Q25H7FBV 8709095 Jirousek, MR; Gillig, JR; Gonzalez, CM; Heath, WF; McDonald, JH; Neel, DA; Rito, CJ; Singh, U; Stramm, LE; Melikian-Badalian, A; Baevsky, M; Ballas, LM; Hall, SE; Winneroski, LL; Faul, MM 9/10/1996 11/10/2009 Eli Lilly http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=17055 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=600&target=Protein+kinase+C+beta+type&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=17055&enzyme=Protein+kinase+C+beta+type&column=ki&startPg=0&Increment=50&submit=Search 153999 46517285 1 MADPAAGPPPSEGEESTVRFARKGALRQKNVHEVKNHKFTARFFKQPTFCSHCTDFIWGFGKQGFQCQVCCFVVHKRCHEFVTFSCPGADKGPASDDPRSKHKFKIHTYSSPTFCDHCGSLLYGLIHQGMKCDTCMMNVHKRCVMNVPSLCGTDHTERRGRIYIQAHIDRDVLIVLVRDAKNLVPMDPNGLSDPYVKLKLIPDPKSESKQKTKTIKCSLNPEWNETFRFQLKESDKDRRLSVEIWDWDLTSRNDFMGSLSFGISELQKASVDGWFKLLSQEEGEYFNVPVPPEGSEANEELRQKFERAKISQGTKVPEEKTTNTVSKFDNNGNRDRMKLTDFNFLMVLGKGSFGKVMLSERKGTDELYAVKILKKDVVIQDDDVECTMVEKRVLALPGKPPFLTQLHSCFQTMDRLYFVMEYVNGGDLMYHIQQVGRFKEPHAVFYAAEIAIGLFFLQSKGIIYRDLKLDNVMLDSEGHIKIADFGMCKENIWDGVTTKTFCGTPDYIAPEIIAYQPYGKSVDWWAFGVLLYEMLAGQAPFEGEDEDELFQSIMEHNVAYPKSMSKEAVAICKGLMTKHPGKRLGCGPEGERDIKEHAFFRYIDWEKLERKEIQPPYKPKARDKRDTSNFDKEFTRQPVELTPTDKLFIMNLDQNEFAGFSYTNPEFVINV 8SE4,8SE3,8SE2,3PFQ,9C5F,1A25 Protein kinase C beta type KPCB_HUMAN P05771 C5IFJ8 D3DWF5 O43744 P05127 Q15138 Q93060 Q9UE49 Q9UE50 Q9UEH8 Q9UJ30 Q9UJ33 50085315 CN(C)C[C@@H]1CCn2cc(C3=C(C(=O)NC3=O)c3cn(CCO1)c1ccccc31)c1ccccc21 |r,t:10| InChI=1S/C28H28N4O3/c1-30(2)15-18-11-12-31-16-21(19-7-3-5-9-23(19)31)25-26(28(34)29-27(25)33)22-17-32(13-14-35-18)24-10-6-4-8-20(22)24/h3-10,16-18H,11-15H2,1-2H3,(H,29,33,34) ZCBUQCWBWNUWSU-UHFFFAOYSA-N 17055 (9S)-9-[(dimethylamino)methyl]-6,7,10,11-tetrahydro-9H,18H-5,21:12,17-di(metheno)dibenzo[e,k]pyrrolo[3,4-h][1,4,13]oxadiazacyclohexadecine-18,20(19H)-dione::(18S)-18-[(dimethylamino)methyl]-17-oxa-4,14,21-triazahexacyclo[19.6.1.1^{7,14}.0^{2,6}.0^{8,13}.0^{22,27}]nonacosa-1(28),2(6),7(29),8(13),9,11,22(27),23,25-nonaene-3,5-dione::K00587a::Ruboxistaurin::LY-333531::cid_153999::LY 333531::LY333531 Protein kinase C epsilon type Homo sapiens 600 ChEMBL 10.1021/jm950588y 10.7270/Q25H7FBV 8709095 Jirousek, MR; Gillig, JR; Gonzalez, CM; Heath, WF; McDonald, JH; Neel, DA; Rito, CJ; Singh, U; Stramm, LE; Melikian-Badalian, A; Baevsky, M; Ballas, LM; Hall, SE; Winneroski, LL; Faul, MM 9/10/1996 11/10/2009 Eli Lilly http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=17055 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=604&target=Protein+kinase+C+epsilon+type&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=17055&enzyme=Protein+kinase+C+epsilon+type&column=ki&startPg=0&Increment=50&submit=Search 153999 46517285 1 MVVFNGLLKIKICEAVSLKPTAWSLRHAVGPRPQTFLLDPYIALNVDDSRIGQTATKQKTNSPAWHDEFVTDVCNGRKIELAVFHDAPIGYDDFVANCTIQFEELLQNGSRHFEDWIDLEPEGRVYVIIDLSGSSGEAPKDNEERVFRERMRPRKRQGAVRRRVHQVNGHKFMATYLRQPTYCSHCRDFIWGVIGKQGYQCQVCTCVVHKRCHELIITKCAGLKKQETPDQVGSQRFSVNMPHKFGIHNYKVPTFCDHCGSLLWGLLRQGLQCKVCKMNVHRRCETNVAPNCGVDARGIAKVLADLGVTPDKITNSGQRRKKLIAGAESPQPASGSSPSEEDRSKSAPTSPCDQEIKELENNIRKALSFDNRGEEHRAASSPDGQLMSPGENGEVRQGQAKRLGLDEFNFIKVLGKGSFGKVMLAELKGKDEVYAVKVLKKDVILQDDDVDCTMTEKRILALARKHPYLTQLYCCFQTKDRLFFVMEYVNGGDLMFQIQRSRKFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILLDAEGHCKLADFGMCKEGILNGVTTTTFCGTPDYIAPEILQELEYGPSVDWWALGVLMYEMMAGQPPFEADNEDDLFESILHDDVLYPVWLSKEAVSILKAFMTKNPHKRLGCVASQNGEDAIKQHPFFKEIDWVLLEQKKIKPPFKPRIKTKRDVNNFDQDFTREEPVLTLVDEAIVKQINQEEFKGFSYFGEDLMP Protein kinase C epsilon type KPCE_HUMAN Q02156 B0LPH7 Q32MQ3 Q53SL4 Q53SM5 Q9UE81 50085316 O=C1NC(=O)C2=C1c1cn(CCO[C@H](CN3CCCC3)CCn3cc2c2ccccc32)c2ccccc12 |c:5| InChI=1S/C30H30N4O3/c35-29-27-23-18-33(25-9-3-1-7-21(23)25)14-11-20(17-32-12-5-6-13-32)37-16-15-34-19-24(28(27)30(36)31-29)22-8-2-4-10-26(22)34/h1-4,7-10,18-20H,5-6,11-17H2,(H,31,35,36) WORLFHNBHSSAJQ-UHFFFAOYSA-N 50052038 18-tetrahydro-1H-1-pyrrolylmethyl-(18S)-17-oxa-4,14,21-triazahexacyclo[19.6.1.17,14.02,6.08,13.022,27]nonacosa-1(28),2(6),7(29),8(13),9,11,22(27),23,25-nonaene-3,5-dione::CHEMBL419866 Protein kinase C zeta type Homo sapiens 55000 ChEMBL 10.1021/jm950588y 10.7270/Q25H7FBV 8709095 Jirousek, MR; Gillig, JR; Gonzalez, CM; Heath, WF; McDonald, JH; Neel, DA; Rito, CJ; Singh, U; Stramm, LE; Melikian-Badalian, A; Baevsky, M; Ballas, LM; Hall, SE; Winneroski, LL; Faul, MM 9/10/1996 11/10/2009 Eli Lilly http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50052038 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=606&target=Protein+kinase+C+zeta+type&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50052038&enzyme=Protein+kinase+C+zeta+type&column=ki&startPg=0&Increment=50&submit=Search 11799388 103948963 CHEMBL419866 1 MPSRTGPKMEGSGGRVRLKAHYGGDIFITSVDAATTFEELCEEVRDMCRLHQQHPLTLKWVDSEGDPCTVSSQMELEEAFRLARQCRDEGLIIHVFPSTPEQPGLPCPGEDKSIYRRGARRWRKLYRANGHLFQAKRFNRRAYCGQCSERIWGLARQGYRCINCKLLVHKRCHGLVPLTCRKHMDSVMPSQEPPVDDKNEDADLPSEETDGIAYISSSRKHDSIKDDSEDLKPVIDGMDGIKISQGLGLQDFDLIRVIGRGSYAKVLLVRLKKNDQIYAMKVVKKELVHDDEDIDWVQTEKHVFEQASSNPFLVGLHSCFQTTSRLFLVIEYVNGGDLMFHMQRQRKLPEEHARFYAAEICIALNFLHERGIIYRDLKLDNVLLDADGHIKLTDYGMCKEGLGPGDTTSTFCGTPNYIAPEILRGEEYGFSVDWWALGVLMFEMMAGRSPFDIITDNPDMNTEDYLFQVILEKPIRIPRFLSVKASHVLKGFLNKDPKERLGCRPQTGFSDIKSHAFFRSIDWDLLEKKQALPPFQPQITDDYGLDNFDTQFTSEPVQLTPDDEDAIKRIDQSEFEGFEYINPLLLSTEESV Protein kinase C zeta type KPCZ_HUMAN Q05513 A8K4N0 A8MU64 B7Z2J7 E9PCW2 Q15207 Q5SYT5 Q969S4 50085319 OC[C@@H]1CCn2cc(C3=C(C(=O)NC3=O)c3cn(CCO1)c1ccccc31)c1ccccc21 |t:8| InChI=1S/C26H23N3O4/c30-15-16-9-10-28-13-19(17-5-1-3-7-21(17)28)23-24(26(32)27-25(23)31)20-14-29(11-12-33-16)22-8-4-2-6-18(20)22/h1-8,13-14,16,30H,9-12,15H2,(H,27,31,32) BGVKOUSMQGMSDY-UHFFFAOYSA-N 50052039 18-hydroxymethyl-(18S)-17-oxa-4,14,21-triazahexacyclo[19.6.1.17,14.02,6.08,13.022,27]nonacosa-1(28),2(6),7(29),8(13),9,11,22(27),23,25-nonaene-3,5-dione::LY-326449::CHEMBL292495 Protein kinase C beta type Homo sapiens 73.0 ChEMBL 10.1021/jm950588y 10.7270/Q25H7FBV 8709095 Jirousek, MR; Gillig, JR; Gonzalez, CM; Heath, WF; McDonald, JH; Neel, DA; Rito, CJ; Singh, U; Stramm, LE; Melikian-Badalian, A; Baevsky, M; Ballas, LM; Hall, SE; Winneroski, LL; Faul, MM 9/10/1996 11/10/2009 Eli Lilly http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50052039 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=600&target=Protein+kinase+C+beta+type&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50052039&enzyme=Protein+kinase+C+beta+type&column=ki&startPg=0&Increment=50&submit=Search 10455969 103948964 CHEMBL292495 1 MADPAAGPPPSEGEESTVRFARKGALRQKNVHEVKNHKFTARFFKQPTFCSHCTDFIWGFGKQGFQCQVCCFVVHKRCHEFVTFSCPGADKGPASDDPRSKHKFKIHTYSSPTFCDHCGSLLYGLIHQGMKCDTCMMNVHKRCVMNVPSLCGTDHTERRGRIYIQAHIDRDVLIVLVRDAKNLVPMDPNGLSDPYVKLKLIPDPKSESKQKTKTIKCSLNPEWNETFRFQLKESDKDRRLSVEIWDWDLTSRNDFMGSLSFGISELQKASVDGWFKLLSQEEGEYFNVPVPPEGSEANEELRQKFERAKISQGTKVPEEKTTNTVSKFDNNGNRDRMKLTDFNFLMVLGKGSFGKVMLSERKGTDELYAVKILKKDVVIQDDDVECTMVEKRVLALPGKPPFLTQLHSCFQTMDRLYFVMEYVNGGDLMYHIQQVGRFKEPHAVFYAAEIAIGLFFLQSKGIIYRDLKLDNVMLDSEGHIKIADFGMCKENIWDGVTTKTFCGTPDYIAPEIIAYQPYGKSVDWWAFGVLLYEMLAGQAPFEGEDEDELFQSIMEHNVAYPKSMSKEAVAICKGLMTKHPGKRLGCGPEGERDIKEHAFFRYIDWEKLERKEIQPPYKPKARDKRDTSNFDKEFTRQPVELTPTDKLFIMNLDQNEFAGFSYTNPEFVINV 8SE4,8SE3,8SE2,3PFQ,9C5F,1A25 Protein kinase C beta type KPCB_HUMAN P05771 C5IFJ8 D3DWF5 O43744 P05127 Q15138 Q93060 Q9UE49 Q9UE50 Q9UEH8 Q9UJ30 Q9UJ33 50085320 O=C1NC(=O)C2=C1c1cn(CCO[C@H](CNCc3ccccc3)CCn3cc2c2ccccc32)c2ccccc12 |c:5| InChI=1S/C33H30N4O3/c38-32-30-26-20-36(28-12-6-4-10-24(26)28)15-14-23(19-34-18-22-8-2-1-3-9-22)40-17-16-37-21-27(31(30)33(39)35-32)25-11-5-7-13-29(25)37/h1-13,20-21,23,34H,14-19H2,(H,35,38,39) RIXHNSFDUIBDSB-UHFFFAOYSA-N 50052040 18-benzylaminomethyl-(18S)-17-oxa-4,14,21-triazahexacyclo[19.6.1.17,14.02,6.08,13.022,27]nonacosa-1(28),2(6),7(29),8(13),9,11,22(27),23,25-nonaene-3,5-dione::CHEMBL328229 Protein kinase C delta type Homo sapiens 7800 ChEMBL 10.1021/jm950588y 10.7270/Q25H7FBV 8709095 Jirousek, MR; Gillig, JR; Gonzalez, CM; Heath, WF; McDonald, JH; Neel, DA; Rito, CJ; Singh, U; Stramm, LE; Melikian-Badalian, A; Baevsky, M; Ballas, LM; Hall, SE; Winneroski, LL; Faul, MM 9/10/1996 11/10/2009 Eli Lilly http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50052040 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=603&target=Protein+kinase+C+delta+type&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50052040&enzyme=Protein+kinase+C+delta+type&column=ki&startPg=0&Increment=50&submit=Search 10768554 103948965 CHEMBL328229 1 MAPFLRIAFNSYELGSLQAEDEANQPFCAVKMKEALSTERGKTLVQKKPTMYPEWKSTFDAHIYEGRVIQIVLMRAAEEPVSEVTVGVSVLAERCKKNNGKAEFWLDLQPQAKVLMSVQYFLEDVDCKQSMRSEDEAKFPTMNRRGAIKQAKIHYIKNHEFIATFFGQPTFCSVCKDFVWGLNKQGYKCRQCNAAIHKKCIDKIIGRCTGTAANSRDTIFQKERFNIDMPHRFKVHNYMSPTFCDHCGSLLWGLVKQGLKCEDCGMNVHHKCREKVANLCGINQKLLAEALNQVTQRASRRSDSASSEPVGIYQGFEKKTGVAGEDMQDNSGTYGKIWEGSSKCNINNFIFHKVLGKGSFGKVLLGELKGRGEYFAIKALKKDVVLIDDDVECTMVEKRVLTLAAENPFLTHLICTFQTKDHLFFVMEFLNGGDLMYHIQDKGRFELYRATFYAAEIMCGLQFLHSKGIIYRDLKLDNVLLDRDGHIKIADFGMCKENIFGESRASTFCGTPDYIAPEILQGLKYTFSVDWWSFGVLLYEMLIGQSPFHGDDEDELFESIRVDTPHYPRWITKESKDILEKLFEREPTKRLGVTGNIKIHPFFKTINWTLLEKRRLEPPFRPKVKSPRDYSNFDQEFLNEKARLSYSDKNLIDSMDQSAFAGFSFVNPKFEHLLED 1YRK Protein kinase C delta type KPCD_HUMAN Q05655 B0KZ81 B2R834 Q15144 Q86XJ6 50085321 CN(C)C[C@@H]1CCn2cc(C3=C(C(=O)NC3=O)c3cn(CCO1)c1ccccc31)c1ccccc21 |r,t:10| InChI=1S/C28H28N4O3/c1-30(2)15-18-11-12-31-16-21(19-7-3-5-9-23(19)31)25-26(28(34)29-27(25)33)22-17-32(13-14-35-18)24-10-6-4-8-20(22)24/h3-10,16-18H,11-15H2,1-2H3,(H,29,33,34) ZCBUQCWBWNUWSU-UHFFFAOYSA-N 17055 (9S)-9-[(dimethylamino)methyl]-6,7,10,11-tetrahydro-9H,18H-5,21:12,17-di(metheno)dibenzo[e,k]pyrrolo[3,4-h][1,4,13]oxadiazacyclohexadecine-18,20(19H)-dione::(18S)-18-[(dimethylamino)methyl]-17-oxa-4,14,21-triazahexacyclo[19.6.1.1^{7,14}.0^{2,6}.0^{8,13}.0^{22,27}]nonacosa-1(28),2(6),7(29),8(13),9,11,22(27),23,25-nonaene-3,5-dione::K00587a::Ruboxistaurin::LY-333531::cid_153999::LY 333531::LY333531 Protein kinase C gamma type Homo sapiens 300 ChEMBL 10.1021/jm950588y 10.7270/Q25H7FBV 8709095 Jirousek, MR; Gillig, JR; Gonzalez, CM; Heath, WF; McDonald, JH; Neel, DA; Rito, CJ; Singh, U; Stramm, LE; Melikian-Badalian, A; Baevsky, M; Ballas, LM; Hall, SE; Winneroski, LL; Faul, MM 9/10/1996 11/10/2009 Eli Lilly http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=17055 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=602&target=Protein+kinase+C+gamma+type&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=17055&enzyme=Protein+kinase+C+gamma+type&column=ki&startPg=0&Increment=50&submit=Search 153999 46517285 1 MAGLGPGVGDSEGGPRPLFCRKGALRQKVVHEVKSHKFTARFFKQPTFCSHCTDFIWGIGKQGLQCQVCSFVVHRRCHEFVTFECPGAGKGPQTDDPRNKHKFRLHSYSSPTFCDHCGSLLYGLVHQGMKCSCCEMNVHRRCVRSVPSLCGVDHTERRGRLQLEIRAPTADEIHVTVGEARNLIPMDPNGLSDPYVKLKLIPDPRNLTKQKTRTVKATLNPVWNETFVFNLKPGDVERRLSVEVWDWDRTSRNDFMGAMSFGVSELLKAPVDGWYKLLNQEEGEYYNVPVADADNCSLLQKFEACNYPLELYERVRMGPSSSPIPSPSPSPTDPKRCFFGASPGRLHISDFSFLMVLGKGSFGKVMLAERRGSDELYAIKILKKDVIVQDDDVDCTLVEKRVLALGGRGPGGRPHFLTQLHSTFQTPDRLYFVMEYVTGGDLMYHIQQLGKFKEPHAAFYAAEIAIGLFFLHNQGIIYRDLKLDNVMLDAEGHIKITDFGMCKENVFPGTTTRTFCGTPDYIAPEIIAYQPYGKSVDWWSFGVLLYEMLAGQPPFDGEDEEELFQAIMEQTVTYPKSLSREAVAICKGFLTKHPGKRLGSGPDGEPTIRAHGFFRWIDWERLERLEIPPPFRPRPCGRSGENFDKFFTRAAPALTPPDRLVLASIDQADFQGFTYVNPDFVHPDARSPTSPVPVPVM 2UZP Protein kinase C gamma type KPCG_HUMAN P05129 B7Z8Q0 50085322 O=C1NC(=O)C2=C1c1cn(CCO[C@H](CN3CCOCC3)CCn3cc2c2ccccc32)c2ccccc12 |c:5| InChI=1S/C30H30N4O4/c35-29-27-23-18-33(25-7-3-1-5-21(23)25)10-9-20(17-32-11-14-37-15-12-32)38-16-13-34-19-24(28(27)30(36)31-29)22-6-2-4-8-26(22)34/h1-8,18-20H,9-17H2,(H,31,35,36) CLHMTFQYMLYQME-UHFFFAOYSA-N 50052035 18-(1,4-oxazinan-4-ylmethyl)-(18S)-17-oxa-4,14,21-triazahexacyclo[19.6.1.17,14.02,6.08,13.022,27]nonacosa-1(28),2(6),7(29),8(13),9,11,22(27),23,25-nonaene-3,5-dione::CHEMBL315357 Protein kinase C gamma type Homo sapiens 2500 ChEMBL 10.1021/jm950588y 10.7270/Q25H7FBV 8709095 Jirousek, MR; Gillig, JR; Gonzalez, CM; Heath, WF; McDonald, JH; Neel, DA; Rito, CJ; Singh, U; Stramm, LE; Melikian-Badalian, A; Baevsky, M; Ballas, LM; Hall, SE; Winneroski, LL; Faul, MM 9/10/1996 11/10/2009 Eli Lilly http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50052035 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=602&target=Protein+kinase+C+gamma+type&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50052035&enzyme=Protein+kinase+C+gamma+type&column=ki&startPg=0&Increment=50&submit=Search 10673286 103948960 CHEMBL315357 1 MAGLGPGVGDSEGGPRPLFCRKGALRQKVVHEVKSHKFTARFFKQPTFCSHCTDFIWGIGKQGLQCQVCSFVVHRRCHEFVTFECPGAGKGPQTDDPRNKHKFRLHSYSSPTFCDHCGSLLYGLVHQGMKCSCCEMNVHRRCVRSVPSLCGVDHTERRGRLQLEIRAPTADEIHVTVGEARNLIPMDPNGLSDPYVKLKLIPDPRNLTKQKTRTVKATLNPVWNETFVFNLKPGDVERRLSVEVWDWDRTSRNDFMGAMSFGVSELLKAPVDGWYKLLNQEEGEYYNVPVADADNCSLLQKFEACNYPLELYERVRMGPSSSPIPSPSPSPTDPKRCFFGASPGRLHISDFSFLMVLGKGSFGKVMLAERRGSDELYAIKILKKDVIVQDDDVDCTLVEKRVLALGGRGPGGRPHFLTQLHSTFQTPDRLYFVMEYVTGGDLMYHIQQLGKFKEPHAAFYAAEIAIGLFFLHNQGIIYRDLKLDNVMLDAEGHIKITDFGMCKENVFPGTTTRTFCGTPDYIAPEIIAYQPYGKSVDWWSFGVLLYEMLAGQPPFDGEDEEELFQAIMEQTVTYPKSLSREAVAICKGFLTKHPGKRLGSGPDGEPTIRAHGFFRWIDWERLERLEIPPPFRPRPCGRSGENFDKFFTRAAPALTPPDRLVLASIDQADFQGFTYVNPDFVHPDARSPTSPVPVPVM 2UZP Protein kinase C gamma type KPCG_HUMAN P05129 B7Z8Q0 50085327 CN1CCN(C[C@@H]2CCn3cc(C4=C(C(=O)NC4=O)c4cn(CCO2)c2ccccc42)c2ccccc32)CC1 |t:12| InChI=1S/C31H33N5O3/c1-33-12-14-34(15-13-33)18-21-10-11-35-19-24(22-6-2-4-8-26(22)35)28-29(31(38)32-30(28)37)25-20-36(16-17-39-21)27-9-5-3-7-23(25)27/h2-9,19-21H,10-18H2,1H3,(H,32,37,38) QKXPAKQCFJVAFI-UHFFFAOYSA-N 50052041 18-(4-methylhexahydro-1-pyrazinylmethyl)-(18S)-17-oxa-4,14,21-triazahexacyclo[19.6.1.17,14.02,6.08,13.022,27]nonacosa-1(28),2(6),7(29),8(13),9,11,22(27),23,25-nonaene-3,5-dione::CHEMBL91959 Protein kinase C beta type Homo sapiens 24 ChEMBL 10.1021/jm950588y 10.7270/Q25H7FBV 8709095 Jirousek, MR; Gillig, JR; Gonzalez, CM; Heath, WF; McDonald, JH; Neel, DA; Rito, CJ; Singh, U; Stramm, LE; Melikian-Badalian, A; Baevsky, M; Ballas, LM; Hall, SE; Winneroski, LL; Faul, MM 9/10/1996 11/10/2009 Eli Lilly http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50052041 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=600&target=Protein+kinase+C+beta+type&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50052041&enzyme=Protein+kinase+C+beta+type&column=ki&startPg=0&Increment=50&submit=Search 10768377 103948966 CHEMBL91959 1 MADPAAGPPPSEGEESTVRFARKGALRQKNVHEVKNHKFTARFFKQPTFCSHCTDFIWGFGKQGFQCQVCCFVVHKRCHEFVTFSCPGADKGPASDDPRSKHKFKIHTYSSPTFCDHCGSLLYGLIHQGMKCDTCMMNVHKRCVMNVPSLCGTDHTERRGRIYIQAHIDRDVLIVLVRDAKNLVPMDPNGLSDPYVKLKLIPDPKSESKQKTKTIKCSLNPEWNETFRFQLKESDKDRRLSVEIWDWDLTSRNDFMGSLSFGISELQKASVDGWFKLLSQEEGEYFNVPVPPEGSEANEELRQKFERAKISQGTKVPEEKTTNTVSKFDNNGNRDRMKLTDFNFLMVLGKGSFGKVMLSERKGTDELYAVKILKKDVVIQDDDVECTMVEKRVLALPGKPPFLTQLHSCFQTMDRLYFVMEYVNGGDLMYHIQQVGRFKEPHAVFYAAEIAIGLFFLQSKGIIYRDLKLDNVMLDSEGHIKIADFGMCKENIWDGVTTKTFCGTPDYIAPEIIAYQPYGKSVDWWAFGVLLYEMLAGQAPFEGEDEDELFQSIMEHNVAYPKSMSKEAVAICKGLMTKHPGKRLGCGPEGERDIKEHAFFRYIDWEKLERKEIQPPYKPKARDKRDTSNFDKEFTRQPVELTPTDKLFIMNLDQNEFAGFSYTNPEFVINV 8SE4,8SE3,8SE2,3PFQ,9C5F,1A25 Protein kinase C beta type KPCB_HUMAN P05771 C5IFJ8 D3DWF5 O43744 P05127 Q15138 Q93060 Q9UE49 Q9UE50 Q9UEH8 Q9UJ30 Q9UJ33 50085330 O=C1NC(=O)C2=C1c1cn(CCO[C@H](CN3CCCC3)CCn3cc2c2ccccc32)c2ccccc12 |c:5| InChI=1S/C30H30N4O3/c35-29-27-23-18-33(25-9-3-1-7-21(23)25)14-11-20(17-32-12-5-6-13-32)37-16-15-34-19-24(28(27)30(36)31-29)22-8-2-4-10-26(22)34/h1-4,7-10,18-20H,5-6,11-17H2,(H,31,35,36) WORLFHNBHSSAJQ-UHFFFAOYSA-N 50052038 18-tetrahydro-1H-1-pyrrolylmethyl-(18S)-17-oxa-4,14,21-triazahexacyclo[19.6.1.17,14.02,6.08,13.022,27]nonacosa-1(28),2(6),7(29),8(13),9,11,22(27),23,25-nonaene-3,5-dione::CHEMBL419866 Proto-oncogene tyrosine-protein kinase Src Homo sapiens 11000 ChEMBL 10.1021/jm950588y 10.7270/Q25H7FBV 8709095 Jirousek, MR; Gillig, JR; Gonzalez, CM; Heath, WF; McDonald, JH; Neel, DA; Rito, CJ; Singh, U; Stramm, LE; Melikian-Badalian, A; Baevsky, M; Ballas, LM; Hall, SE; Winneroski, LL; Faul, MM 9/10/1996 11/10/2009 Eli Lilly http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50052038 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=13&target=Proto-oncogene+tyrosine-protein+kinase+Src&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50052038&enzyme=Proto-oncogene+tyrosine-protein+kinase+Src&column=ki&startPg=0&Increment=50&submit=Search 11799388 103948963 CHEMBL419866 1 MGSNKSKPKDASQRRRSLEPAENVHGAGGGAFPASQTPSKPASADGHRGPSAAFAPAAAEPKLFGGFNSSDTVTSPQRAGPLAGGVTTFVALYDYESRTETDLSFKKGERLQIVNNTEGDWWLAHSLSTGQTGYIPSNYVAPSDSIQAEEWYFGKITRRESERLLLNAENPRGTFLVRESETTKGAYCLSVSDFDNAKGLNVKHYKIRKLDSGGFYITSRTQFNSLQQLVAYYSKHADGLCHRLTTVCPTSKPQTQGLAKDAWEIPRESLRLEVKLGQGCFGEVWMGTWNGTTRVAIKTLKPGTMSPEAFLQEAQVMKKLRHEKLVQLYAVVSEEPIYIVTEYMSKGSLLDFLKGETGKYLRLPQLVDMAAQIASGMAYVERMNYVHRDLRAANILVGENLVCKVADFGLARLIEDNEYTARQGAKFPIKWTAPEAALYGRFTIKSDVWSFGILLTELTTKGRVPYPGMVNREVLDQVERGYRMPCPPECPESLHDLMCQCWRKEPEERPTFEYLQAFLEDYFTSTEPQYQPGENL 8JN9,8JN8,2H8H,2SRC,1Y57,1FMK,2PTK,9NS0,8JF3,6ATE,4MXO,4MXX,2BDJ,2BDF,8HAQ,6E6E,1YI6 Proto-oncogene tyrosine-protein kinase Src SRC_HUMAN P12931 E1P5V4 Q76P87 Q86VB9 Q9H5A8 50085331 CNC[C@@H]1CCn2cc(C3=C(C(=O)NC3=O)c3cn(CCO1)c1ccccc31)c1ccccc21 |t:9| InChI=1S/C27H26N4O3/c1-28-14-17-10-11-30-15-20(18-6-2-4-8-22(18)30)24-25(27(33)29-26(24)32)21-16-31(12-13-34-17)23-9-5-3-7-19(21)23/h2-9,15-17,28H,10-14H2,1H3,(H,29,32,33) ZEYTZKVCOZMUKL-UHFFFAOYSA-N 50052034 18-methylaminomethyl-(18S)-17-oxa-4,14,21-triazahexacyclo[19.6.1.17,14.02,6.08,13.022,27]nonacosa-1(28),2(6),7(29),8(13),9,11,22(27),23,25-nonaene-3,5-dione::CHEMBL311543 Protein kinase C delta type Homo sapiens 170 ChEMBL 10.1021/jm950588y 10.7270/Q25H7FBV 8709095 Jirousek, MR; Gillig, JR; Gonzalez, CM; Heath, WF; McDonald, JH; Neel, DA; Rito, CJ; Singh, U; Stramm, LE; Melikian-Badalian, A; Baevsky, M; Ballas, LM; Hall, SE; Winneroski, LL; Faul, MM 9/10/1996 11/10/2009 Eli Lilly http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50052034 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=603&target=Protein+kinase+C+delta+type&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50052034&enzyme=Protein+kinase+C+delta+type&column=ki&startPg=0&Increment=50&submit=Search 10671412 103948959 CHEMBL311543 1 MAPFLRIAFNSYELGSLQAEDEANQPFCAVKMKEALSTERGKTLVQKKPTMYPEWKSTFDAHIYEGRVIQIVLMRAAEEPVSEVTVGVSVLAERCKKNNGKAEFWLDLQPQAKVLMSVQYFLEDVDCKQSMRSEDEAKFPTMNRRGAIKQAKIHYIKNHEFIATFFGQPTFCSVCKDFVWGLNKQGYKCRQCNAAIHKKCIDKIIGRCTGTAANSRDTIFQKERFNIDMPHRFKVHNYMSPTFCDHCGSLLWGLVKQGLKCEDCGMNVHHKCREKVANLCGINQKLLAEALNQVTQRASRRSDSASSEPVGIYQGFEKKTGVAGEDMQDNSGTYGKIWEGSSKCNINNFIFHKVLGKGSFGKVLLGELKGRGEYFAIKALKKDVVLIDDDVECTMVEKRVLTLAAENPFLTHLICTFQTKDHLFFVMEFLNGGDLMYHIQDKGRFELYRATFYAAEIMCGLQFLHSKGIIYRDLKLDNVLLDRDGHIKIADFGMCKENIFGESRASTFCGTPDYIAPEILQGLKYTFSVDWWSFGVLLYEMLIGQSPFHGDDEDELFESIRVDTPHYPRWITKESKDILEKLFEREPTKRLGVTGNIKIHPFFKTINWTLLEKRRLEPPFRPKVKSPRDYSNFDQEFLNEKARLSYSDKNLIDSMDQSAFAGFSFVNPKFEHLLED 1YRK Protein kinase C delta type KPCD_HUMAN Q05655 B0KZ81 B2R834 Q15144 Q86XJ6 50085332 O=C1NC(=O)C2=C1c1cn(CCO[C@H](CNCc3ccccc3)CCn3cc2c2ccccc32)c2ccccc12 |c:5| InChI=1S/C33H30N4O3/c38-32-30-26-20-36(28-12-6-4-10-24(26)28)15-14-23(19-34-18-22-8-2-1-3-9-22)40-17-16-37-21-27(31(30)33(39)35-32)25-11-5-7-13-29(25)37/h1-13,20-21,23,34H,14-19H2,(H,35,38,39) RIXHNSFDUIBDSB-UHFFFAOYSA-N 50052040 18-benzylaminomethyl-(18S)-17-oxa-4,14,21-triazahexacyclo[19.6.1.17,14.02,6.08,13.022,27]nonacosa-1(28),2(6),7(29),8(13),9,11,22(27),23,25-nonaene-3,5-dione::CHEMBL328229 Protein kinase C epsilon type Homo sapiens 57000 ChEMBL 10.1021/jm950588y 10.7270/Q25H7FBV 8709095 Jirousek, MR; Gillig, JR; Gonzalez, CM; Heath, WF; McDonald, JH; Neel, DA; Rito, CJ; Singh, U; Stramm, LE; Melikian-Badalian, A; Baevsky, M; Ballas, LM; Hall, SE; Winneroski, LL; Faul, MM 9/10/1996 11/10/2009 Eli Lilly http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50052040 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=604&target=Protein+kinase+C+epsilon+type&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50052040&enzyme=Protein+kinase+C+epsilon+type&column=ki&startPg=0&Increment=50&submit=Search 10768554 103948965 CHEMBL328229 1 MVVFNGLLKIKICEAVSLKPTAWSLRHAVGPRPQTFLLDPYIALNVDDSRIGQTATKQKTNSPAWHDEFVTDVCNGRKIELAVFHDAPIGYDDFVANCTIQFEELLQNGSRHFEDWIDLEPEGRVYVIIDLSGSSGEAPKDNEERVFRERMRPRKRQGAVRRRVHQVNGHKFMATYLRQPTYCSHCRDFIWGVIGKQGYQCQVCTCVVHKRCHELIITKCAGLKKQETPDQVGSQRFSVNMPHKFGIHNYKVPTFCDHCGSLLWGLLRQGLQCKVCKMNVHRRCETNVAPNCGVDARGIAKVLADLGVTPDKITNSGQRRKKLIAGAESPQPASGSSPSEEDRSKSAPTSPCDQEIKELENNIRKALSFDNRGEEHRAASSPDGQLMSPGENGEVRQGQAKRLGLDEFNFIKVLGKGSFGKVMLAELKGKDEVYAVKVLKKDVILQDDDVDCTMTEKRILALARKHPYLTQLYCCFQTKDRLFFVMEYVNGGDLMFQIQRSRKFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILLDAEGHCKLADFGMCKEGILNGVTTTTFCGTPDYIAPEILQELEYGPSVDWWALGVLMYEMMAGQPPFEADNEDDLFESILHDDVLYPVWLSKEAVSILKAFMTKNPHKRLGCVASQNGEDAIKQHPFFKEIDWVLLEQKKIKPPFKPRIKTKRDVNNFDQDFTREEPVLTLVDEAIVKQINQEEFKGFSYFGEDLMP Protein kinase C epsilon type KPCE_HUMAN Q02156 B0LPH7 Q32MQ3 Q53SL4 Q53SM5 Q9UE81 50085335 NC[C@@H]1CCn2cc(C3=C(C(=O)NC3=O)c3cn(CCO1)c1ccccc31)c1ccccc21 |t:8| InChI=1S/C26H24N4O3/c27-13-16-9-10-29-14-19(17-5-1-3-7-21(17)29)23-24(26(32)28-25(23)31)20-15-30(11-12-33-16)22-8-4-2-6-18(20)22/h1-8,14-16H,9-13,27H2,(H,28,31,32) JPLUPRIZLHXUPQ-UHFFFAOYSA-N 50052037 18-aminomethyl-(18S)-17-oxa-4,14,21-triazahexacyclo[19.6.1.17,14.02,6.08,13.022,27]nonacosa-1(28),2(6),7(29),8(13),9,11,22(27),23,25-nonaene-3,5-dione::CHEMBL316239 Protein kinase C epsilon type Homo sapiens >5000 ChEMBL 10.1021/jm950588y 10.7270/Q25H7FBV 8709095 Jirousek, MR; Gillig, JR; Gonzalez, CM; Heath, WF; McDonald, JH; Neel, DA; Rito, CJ; Singh, U; Stramm, LE; Melikian-Badalian, A; Baevsky, M; Ballas, LM; Hall, SE; Winneroski, LL; Faul, MM 9/10/1996 11/10/2009 Eli Lilly http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50052037 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=604&target=Protein+kinase+C+epsilon+type&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50052037&enzyme=Protein+kinase+C+epsilon+type&column=ki&startPg=0&Increment=50&submit=Search 10527068 103948962 CHEMBL316239 1 MVVFNGLLKIKICEAVSLKPTAWSLRHAVGPRPQTFLLDPYIALNVDDSRIGQTATKQKTNSPAWHDEFVTDVCNGRKIELAVFHDAPIGYDDFVANCTIQFEELLQNGSRHFEDWIDLEPEGRVYVIIDLSGSSGEAPKDNEERVFRERMRPRKRQGAVRRRVHQVNGHKFMATYLRQPTYCSHCRDFIWGVIGKQGYQCQVCTCVVHKRCHELIITKCAGLKKQETPDQVGSQRFSVNMPHKFGIHNYKVPTFCDHCGSLLWGLLRQGLQCKVCKMNVHRRCETNVAPNCGVDARGIAKVLADLGVTPDKITNSGQRRKKLIAGAESPQPASGSSPSEEDRSKSAPTSPCDQEIKELENNIRKALSFDNRGEEHRAASSPDGQLMSPGENGEVRQGQAKRLGLDEFNFIKVLGKGSFGKVMLAELKGKDEVYAVKVLKKDVILQDDDVDCTMTEKRILALARKHPYLTQLYCCFQTKDRLFFVMEYVNGGDLMFQIQRSRKFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILLDAEGHCKLADFGMCKEGILNGVTTTTFCGTPDYIAPEILQELEYGPSVDWWALGVLMYEMMAGQPPFEADNEDDLFESILHDDVLYPVWLSKEAVSILKAFMTKNPHKRLGCVASQNGEDAIKQHPFFKEIDWVLLEQKKIKPPFKPRIKTKRDVNNFDQDFTREEPVLTLVDEAIVKQINQEEFKGFSYFGEDLMP Protein kinase C epsilon type KPCE_HUMAN Q02156 B0LPH7 Q32MQ3 Q53SL4 Q53SM5 Q9UE81 50085336 O=C1NC(=O)C2=C1c1cn(CCO[C@H](CN3CCCC3)CCn3cc2c2ccccc32)c2ccccc12 |c:5| InChI=1S/C30H30N4O3/c35-29-27-23-18-33(25-9-3-1-7-21(23)25)14-11-20(17-32-12-5-6-13-32)37-16-15-34-19-24(28(27)30(36)31-29)22-8-2-4-10-26(22)34/h1-4,7-10,18-20H,5-6,11-17H2,(H,31,35,36) WORLFHNBHSSAJQ-UHFFFAOYSA-N 50052038 18-tetrahydro-1H-1-pyrrolylmethyl-(18S)-17-oxa-4,14,21-triazahexacyclo[19.6.1.17,14.02,6.08,13.022,27]nonacosa-1(28),2(6),7(29),8(13),9,11,22(27),23,25-nonaene-3,5-dione::CHEMBL419866 Protein kinase C epsilon type Homo sapiens 3800 ChEMBL 10.1021/jm950588y 10.7270/Q25H7FBV 8709095 Jirousek, MR; Gillig, JR; Gonzalez, CM; Heath, WF; McDonald, JH; Neel, DA; Rito, CJ; Singh, U; Stramm, LE; Melikian-Badalian, A; Baevsky, M; Ballas, LM; Hall, SE; Winneroski, LL; Faul, MM 9/10/1996 11/10/2009 Eli Lilly http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50052038 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=604&target=Protein+kinase+C+epsilon+type&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50052038&enzyme=Protein+kinase+C+epsilon+type&column=ki&startPg=0&Increment=50&submit=Search 11799388 103948963 CHEMBL419866 1 MVVFNGLLKIKICEAVSLKPTAWSLRHAVGPRPQTFLLDPYIALNVDDSRIGQTATKQKTNSPAWHDEFVTDVCNGRKIELAVFHDAPIGYDDFVANCTIQFEELLQNGSRHFEDWIDLEPEGRVYVIIDLSGSSGEAPKDNEERVFRERMRPRKRQGAVRRRVHQVNGHKFMATYLRQPTYCSHCRDFIWGVIGKQGYQCQVCTCVVHKRCHELIITKCAGLKKQETPDQVGSQRFSVNMPHKFGIHNYKVPTFCDHCGSLLWGLLRQGLQCKVCKMNVHRRCETNVAPNCGVDARGIAKVLADLGVTPDKITNSGQRRKKLIAGAESPQPASGSSPSEEDRSKSAPTSPCDQEIKELENNIRKALSFDNRGEEHRAASSPDGQLMSPGENGEVRQGQAKRLGLDEFNFIKVLGKGSFGKVMLAELKGKDEVYAVKVLKKDVILQDDDVDCTMTEKRILALARKHPYLTQLYCCFQTKDRLFFVMEYVNGGDLMFQIQRSRKFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILLDAEGHCKLADFGMCKEGILNGVTTTTFCGTPDYIAPEILQELEYGPSVDWWALGVLMYEMMAGQPPFEADNEDDLFESILHDDVLYPVWLSKEAVSILKAFMTKNPHKRLGCVASQNGEDAIKQHPFFKEIDWVLLEQKKIKPPFKPRIKTKRDVNNFDQDFTREEPVLTLVDEAIVKQINQEEFKGFSYFGEDLMP Protein kinase C epsilon type KPCE_HUMAN Q02156 B0LPH7 Q32MQ3 Q53SL4 Q53SM5 Q9UE81 50085339 CN(C)C[C@@H]1CCn2cc(C3=C(C(=O)NC3=O)c3cn(CCO1)c1ccccc31)c1ccccc21 |r,t:10| InChI=1S/C28H28N4O3/c1-30(2)15-18-11-12-31-16-21(19-7-3-5-9-23(19)31)25-26(28(34)29-27(25)33)22-17-32(13-14-35-18)24-10-6-4-8-20(22)24/h3-10,16-18H,11-15H2,1-2H3,(H,29,33,34) ZCBUQCWBWNUWSU-UHFFFAOYSA-N 17055 (9S)-9-[(dimethylamino)methyl]-6,7,10,11-tetrahydro-9H,18H-5,21:12,17-di(metheno)dibenzo[e,k]pyrrolo[3,4-h][1,4,13]oxadiazacyclohexadecine-18,20(19H)-dione::(18S)-18-[(dimethylamino)methyl]-17-oxa-4,14,21-triazahexacyclo[19.6.1.1^{7,14}.0^{2,6}.0^{8,13}.0^{22,27}]nonacosa-1(28),2(6),7(29),8(13),9,11,22(27),23,25-nonaene-3,5-dione::K00587a::Ruboxistaurin::LY-333531::cid_153999::LY 333531::LY333531 Proto-oncogene tyrosine-protein kinase Src Homo sapiens >100000 ChEMBL 10.1021/jm950588y 10.7270/Q25H7FBV 8709095 Jirousek, MR; Gillig, JR; Gonzalez, CM; Heath, WF; McDonald, JH; Neel, DA; Rito, CJ; Singh, U; Stramm, LE; Melikian-Badalian, A; Baevsky, M; Ballas, LM; Hall, SE; Winneroski, LL; Faul, MM 9/10/1996 11/10/2009 Eli Lilly http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=17055 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=13&target=Proto-oncogene+tyrosine-protein+kinase+Src&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=17055&enzyme=Proto-oncogene+tyrosine-protein+kinase+Src&column=ki&startPg=0&Increment=50&submit=Search 153999 46517285 1 MGSNKSKPKDASQRRRSLEPAENVHGAGGGAFPASQTPSKPASADGHRGPSAAFAPAAAEPKLFGGFNSSDTVTSPQRAGPLAGGVTTFVALYDYESRTETDLSFKKGERLQIVNNTEGDWWLAHSLSTGQTGYIPSNYVAPSDSIQAEEWYFGKITRRESERLLLNAENPRGTFLVRESETTKGAYCLSVSDFDNAKGLNVKHYKIRKLDSGGFYITSRTQFNSLQQLVAYYSKHADGLCHRLTTVCPTSKPQTQGLAKDAWEIPRESLRLEVKLGQGCFGEVWMGTWNGTTRVAIKTLKPGTMSPEAFLQEAQVMKKLRHEKLVQLYAVVSEEPIYIVTEYMSKGSLLDFLKGETGKYLRLPQLVDMAAQIASGMAYVERMNYVHRDLRAANILVGENLVCKVADFGLARLIEDNEYTARQGAKFPIKWTAPEAALYGRFTIKSDVWSFGILLTELTTKGRVPYPGMVNREVLDQVERGYRMPCPPECPESLHDLMCQCWRKEPEERPTFEYLQAFLEDYFTSTEPQYQPGENL 8JN9,8JN8,2H8H,2SRC,1Y57,1FMK,2PTK,9NS0,8JF3,6ATE,4MXO,4MXX,2BDJ,2BDF,8HAQ,6E6E,1YI6 Proto-oncogene tyrosine-protein kinase Src SRC_HUMAN P12931 E1P5V4 Q76P87 Q86VB9 Q9H5A8 50085340 O=C1NC(=O)C2=C1c1cn(CCO[C@H](CNCc3ccccc3)CCn3cc2c2ccccc32)c2ccccc12 |c:5| InChI=1S/C33H30N4O3/c38-32-30-26-20-36(28-12-6-4-10-24(26)28)15-14-23(19-34-18-22-8-2-1-3-9-22)40-17-16-37-21-27(31(30)33(39)35-32)25-11-5-7-13-29(25)37/h1-13,20-21,23,34H,14-19H2,(H,35,38,39) RIXHNSFDUIBDSB-UHFFFAOYSA-N 50052040 18-benzylaminomethyl-(18S)-17-oxa-4,14,21-triazahexacyclo[19.6.1.17,14.02,6.08,13.022,27]nonacosa-1(28),2(6),7(29),8(13),9,11,22(27),23,25-nonaene-3,5-dione::CHEMBL328229 Protein kinase C zeta type Homo sapiens 54000 ChEMBL 10.1021/jm950588y 10.7270/Q25H7FBV 8709095 Jirousek, MR; Gillig, JR; Gonzalez, CM; Heath, WF; McDonald, JH; Neel, DA; Rito, CJ; Singh, U; Stramm, LE; Melikian-Badalian, A; Baevsky, M; Ballas, LM; Hall, SE; Winneroski, LL; Faul, MM 9/10/1996 11/10/2009 Eli Lilly http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50052040 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=606&target=Protein+kinase+C+zeta+type&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50052040&enzyme=Protein+kinase+C+zeta+type&column=ki&startPg=0&Increment=50&submit=Search 10768554 103948965 CHEMBL328229 1 MPSRTGPKMEGSGGRVRLKAHYGGDIFITSVDAATTFEELCEEVRDMCRLHQQHPLTLKWVDSEGDPCTVSSQMELEEAFRLARQCRDEGLIIHVFPSTPEQPGLPCPGEDKSIYRRGARRWRKLYRANGHLFQAKRFNRRAYCGQCSERIWGLARQGYRCINCKLLVHKRCHGLVPLTCRKHMDSVMPSQEPPVDDKNEDADLPSEETDGIAYISSSRKHDSIKDDSEDLKPVIDGMDGIKISQGLGLQDFDLIRVIGRGSYAKVLLVRLKKNDQIYAMKVVKKELVHDDEDIDWVQTEKHVFEQASSNPFLVGLHSCFQTTSRLFLVIEYVNGGDLMFHMQRQRKLPEEHARFYAAEICIALNFLHERGIIYRDLKLDNVLLDADGHIKLTDYGMCKEGLGPGDTTSTFCGTPNYIAPEILRGEEYGFSVDWWALGVLMFEMMAGRSPFDIITDNPDMNTEDYLFQVILEKPIRIPRFLSVKASHVLKGFLNKDPKERLGCRPQTGFSDIKSHAFFRSIDWDLLEKKQALPPFQPQITDDYGLDNFDTQFTSEPVQLTPDDEDAIKRIDQSEFEGFEYINPLLLSTEESV Protein kinase C zeta type KPCZ_HUMAN Q05513 A8K4N0 A8MU64 B7Z2J7 E9PCW2 Q15207 Q5SYT5 Q969S4 50085344 CNC[C@@H]1CCn2cc(C3=C(C(=O)NC3=O)c3cn(CCO1)c1ccccc31)c1ccccc21 |t:9| InChI=1S/C27H26N4O3/c1-28-14-17-10-11-30-15-20(18-6-2-4-8-22(18)30)24-25(27(33)29-26(24)32)21-16-31(12-13-34-17)23-9-5-3-7-19(21)23/h2-9,15-17,28H,10-14H2,1H3,(H,29,32,33) ZEYTZKVCOZMUKL-UHFFFAOYSA-N 50052034 18-methylaminomethyl-(18S)-17-oxa-4,14,21-triazahexacyclo[19.6.1.17,14.02,6.08,13.022,27]nonacosa-1(28),2(6),7(29),8(13),9,11,22(27),23,25-nonaene-3,5-dione::CHEMBL311543 Protein kinase C beta type Homo sapiens 5 ChEMBL 10.1021/jm950588y 10.7270/Q25H7FBV 8709095 Jirousek, MR; Gillig, JR; Gonzalez, CM; Heath, WF; McDonald, JH; Neel, DA; Rito, CJ; Singh, U; Stramm, LE; Melikian-Badalian, A; Baevsky, M; Ballas, LM; Hall, SE; Winneroski, LL; Faul, MM 9/10/1996 11/10/2009 Eli Lilly http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50052034 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=600&target=Protein+kinase+C+beta+type&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50052034&enzyme=Protein+kinase+C+beta+type&column=ki&startPg=0&Increment=50&submit=Search 10671412 103948959 CHEMBL311543 1 MADPAAGPPPSEGEESTVRFARKGALRQKNVHEVKNHKFTARFFKQPTFCSHCTDFIWGFGKQGFQCQVCCFVVHKRCHEFVTFSCPGADKGPASDDPRSKHKFKIHTYSSPTFCDHCGSLLYGLIHQGMKCDTCMMNVHKRCVMNVPSLCGTDHTERRGRIYIQAHIDRDVLIVLVRDAKNLVPMDPNGLSDPYVKLKLIPDPKSESKQKTKTIKCSLNPEWNETFRFQLKESDKDRRLSVEIWDWDLTSRNDFMGSLSFGISELQKASVDGWFKLLSQEEGEYFNVPVPPEGSEANEELRQKFERAKISQGTKVPEEKTTNTVSKFDNNGNRDRMKLTDFNFLMVLGKGSFGKVMLSERKGTDELYAVKILKKDVVIQDDDVECTMVEKRVLALPGKPPFLTQLHSCFQTMDRLYFVMEYVNGGDLMYHIQQVGRFKEPHAVFYAAEIAIGLFFLQSKGIIYRDLKLDNVMLDSEGHIKIADFGMCKENIWDGVTTKTFCGTPDYIAPEIIAYQPYGKSVDWWAFGVLLYEMLAGQAPFEGEDEDELFQSIMEHNVAYPKSMSKEAVAICKGLMTKHPGKRLGCGPEGERDIKEHAFFRYIDWEKLERKEIQPPYKPKARDKRDTSNFDKEFTRQPVELTPTDKLFIMNLDQNEFAGFSYTNPEFVINV 8SE4,8SE3,8SE2,3PFQ,9C5F,1A25 Protein kinase C beta type KPCB_HUMAN P05771 C5IFJ8 D3DWF5 O43744 P05127 Q15138 Q93060 Q9UE49 Q9UE50 Q9UEH8 Q9UJ30 Q9UJ33 50085346 NC[C@@H]1CCn2cc(C3=C(C(=O)NC3=O)c3cn(CCO1)c1ccccc31)c1ccccc21 |t:8| InChI=1S/C26H24N4O3/c27-13-16-9-10-29-14-19(17-5-1-3-7-21(17)29)23-24(26(32)28-25(23)31)20-15-30(11-12-33-16)22-8-4-2-6-18(20)22/h1-8,14-16H,9-13,27H2,(H,28,31,32) JPLUPRIZLHXUPQ-UHFFFAOYSA-N 50052037 18-aminomethyl-(18S)-17-oxa-4,14,21-triazahexacyclo[19.6.1.17,14.02,6.08,13.022,27]nonacosa-1(28),2(6),7(29),8(13),9,11,22(27),23,25-nonaene-3,5-dione::CHEMBL316239 Protein kinase C beta type Homo sapiens 48 ChEMBL 10.1021/jm950588y 10.7270/Q25H7FBV 8709095 Jirousek, MR; Gillig, JR; Gonzalez, CM; Heath, WF; McDonald, JH; Neel, DA; Rito, CJ; Singh, U; Stramm, LE; Melikian-Badalian, A; Baevsky, M; Ballas, LM; Hall, SE; Winneroski, LL; Faul, MM 9/10/1996 11/10/2009 Eli Lilly http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50052037 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=600&target=Protein+kinase+C+beta+type&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50052037&enzyme=Protein+kinase+C+beta+type&column=ki&startPg=0&Increment=50&submit=Search 10527068 103948962 CHEMBL316239 1 MADPAAGPPPSEGEESTVRFARKGALRQKNVHEVKNHKFTARFFKQPTFCSHCTDFIWGFGKQGFQCQVCCFVVHKRCHEFVTFSCPGADKGPASDDPRSKHKFKIHTYSSPTFCDHCGSLLYGLIHQGMKCDTCMMNVHKRCVMNVPSLCGTDHTERRGRIYIQAHIDRDVLIVLVRDAKNLVPMDPNGLSDPYVKLKLIPDPKSESKQKTKTIKCSLNPEWNETFRFQLKESDKDRRLSVEIWDWDLTSRNDFMGSLSFGISELQKASVDGWFKLLSQEEGEYFNVPVPPEGSEANEELRQKFERAKISQGTKVPEEKTTNTVSKFDNNGNRDRMKLTDFNFLMVLGKGSFGKVMLSERKGTDELYAVKILKKDVVIQDDDVECTMVEKRVLALPGKPPFLTQLHSCFQTMDRLYFVMEYVNGGDLMYHIQQVGRFKEPHAVFYAAEIAIGLFFLQSKGIIYRDLKLDNVMLDSEGHIKIADFGMCKENIWDGVTTKTFCGTPDYIAPEIIAYQPYGKSVDWWAFGVLLYEMLAGQAPFEGEDEDELFQSIMEHNVAYPKSMSKEAVAICKGLMTKHPGKRLGCGPEGERDIKEHAFFRYIDWEKLERKEIQPPYKPKARDKRDTSNFDKEFTRQPVELTPTDKLFIMNLDQNEFAGFSYTNPEFVINV 8SE4,8SE3,8SE2,3PFQ,9C5F,1A25 Protein kinase C beta type KPCB_HUMAN P05771 C5IFJ8 D3DWF5 O43744 P05127 Q15138 Q93060 Q9UE49 Q9UE50 Q9UEH8 Q9UJ30 Q9UJ33 50085347 OC[C@@H]1CCn2cc(C3=C(C(=O)NC3=O)c3cn(CCO1)c1ccccc31)c1ccccc21 |t:8| InChI=1S/C26H23N3O4/c30-15-16-9-10-28-13-19(17-5-1-3-7-21(17)28)23-24(26(32)27-25(23)31)20-14-29(11-12-33-16)22-8-4-2-6-18(20)22/h1-8,13-14,16,30H,9-12,15H2,(H,27,31,32) BGVKOUSMQGMSDY-UHFFFAOYSA-N 50052039 18-hydroxymethyl-(18S)-17-oxa-4,14,21-triazahexacyclo[19.6.1.17,14.02,6.08,13.022,27]nonacosa-1(28),2(6),7(29),8(13),9,11,22(27),23,25-nonaene-3,5-dione::LY-326449::CHEMBL292495 Protein kinase C delta type Homo sapiens 690.0 ChEMBL 10.1021/jm950588y 10.7270/Q25H7FBV 8709095 Jirousek, MR; Gillig, JR; Gonzalez, CM; Heath, WF; McDonald, JH; Neel, DA; Rito, CJ; Singh, U; Stramm, LE; Melikian-Badalian, A; Baevsky, M; Ballas, LM; Hall, SE; Winneroski, LL; Faul, MM 9/10/1996 11/10/2009 Eli Lilly http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50052039 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=603&target=Protein+kinase+C+delta+type&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50052039&enzyme=Protein+kinase+C+delta+type&column=ki&startPg=0&Increment=50&submit=Search 10455969 103948964 CHEMBL292495 1 MAPFLRIAFNSYELGSLQAEDEANQPFCAVKMKEALSTERGKTLVQKKPTMYPEWKSTFDAHIYEGRVIQIVLMRAAEEPVSEVTVGVSVLAERCKKNNGKAEFWLDLQPQAKVLMSVQYFLEDVDCKQSMRSEDEAKFPTMNRRGAIKQAKIHYIKNHEFIATFFGQPTFCSVCKDFVWGLNKQGYKCRQCNAAIHKKCIDKIIGRCTGTAANSRDTIFQKERFNIDMPHRFKVHNYMSPTFCDHCGSLLWGLVKQGLKCEDCGMNVHHKCREKVANLCGINQKLLAEALNQVTQRASRRSDSASSEPVGIYQGFEKKTGVAGEDMQDNSGTYGKIWEGSSKCNINNFIFHKVLGKGSFGKVLLGELKGRGEYFAIKALKKDVVLIDDDVECTMVEKRVLTLAAENPFLTHLICTFQTKDHLFFVMEFLNGGDLMYHIQDKGRFELYRATFYAAEIMCGLQFLHSKGIIYRDLKLDNVLLDRDGHIKIADFGMCKENIFGESRASTFCGTPDYIAPEILQGLKYTFSVDWWSFGVLLYEMLIGQSPFHGDDEDELFESIRVDTPHYPRWITKESKDILEKLFEREPTKRLGVTGNIKIHPFFKTINWTLLEKRRLEPPFRPKVKSPRDYSNFDQEFLNEKARLSYSDKNLIDSMDQSAFAGFSFVNPKFEHLLED 1YRK Protein kinase C delta type KPCD_HUMAN Q05655 B0KZ81 B2R834 Q15144 Q86XJ6 50085348 CN1CCN(C[C@@H]2CCn3cc(C4=C(C(=O)NC4=O)c4cn(CCO2)c2ccccc42)c2ccccc32)CC1 |t:12| InChI=1S/C31H33N5O3/c1-33-12-14-34(15-13-33)18-21-10-11-35-19-24(22-6-2-4-8-26(22)35)28-29(31(38)32-30(28)37)25-20-36(16-17-39-21)27-9-5-3-7-23(25)27/h2-9,19-21H,10-18H2,1H3,(H,32,37,38) QKXPAKQCFJVAFI-UHFFFAOYSA-N 50052041 18-(4-methylhexahydro-1-pyrazinylmethyl)-(18S)-17-oxa-4,14,21-triazahexacyclo[19.6.1.17,14.02,6.08,13.022,27]nonacosa-1(28),2(6),7(29),8(13),9,11,22(27),23,25-nonaene-3,5-dione::CHEMBL91959 Protein kinase C gamma type Homo sapiens 3200 ChEMBL 10.1021/jm950588y 10.7270/Q25H7FBV 8709095 Jirousek, MR; Gillig, JR; Gonzalez, CM; Heath, WF; McDonald, JH; Neel, DA; Rito, CJ; Singh, U; Stramm, LE; Melikian-Badalian, A; Baevsky, M; Ballas, LM; Hall, SE; Winneroski, LL; Faul, MM 9/10/1996 11/10/2009 Eli Lilly http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50052041 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=602&target=Protein+kinase+C+gamma+type&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50052041&enzyme=Protein+kinase+C+gamma+type&column=ki&startPg=0&Increment=50&submit=Search 10768377 103948966 CHEMBL91959 1 MAGLGPGVGDSEGGPRPLFCRKGALRQKVVHEVKSHKFTARFFKQPTFCSHCTDFIWGIGKQGLQCQVCSFVVHRRCHEFVTFECPGAGKGPQTDDPRNKHKFRLHSYSSPTFCDHCGSLLYGLVHQGMKCSCCEMNVHRRCVRSVPSLCGVDHTERRGRLQLEIRAPTADEIHVTVGEARNLIPMDPNGLSDPYVKLKLIPDPRNLTKQKTRTVKATLNPVWNETFVFNLKPGDVERRLSVEVWDWDRTSRNDFMGAMSFGVSELLKAPVDGWYKLLNQEEGEYYNVPVADADNCSLLQKFEACNYPLELYERVRMGPSSSPIPSPSPSPTDPKRCFFGASPGRLHISDFSFLMVLGKGSFGKVMLAERRGSDELYAIKILKKDVIVQDDDVDCTLVEKRVLALGGRGPGGRPHFLTQLHSTFQTPDRLYFVMEYVTGGDLMYHIQQLGKFKEPHAAFYAAEIAIGLFFLHNQGIIYRDLKLDNVMLDAEGHIKITDFGMCKENVFPGTTTRTFCGTPDYIAPEIIAYQPYGKSVDWWSFGVLLYEMLAGQPPFDGEDEEELFQAIMEQTVTYPKSLSREAVAICKGFLTKHPGKRLGSGPDGEPTIRAHGFFRWIDWERLERLEIPPPFRPRPCGRSGENFDKFFTRAAPALTPPDRLVLASIDQADFQGFTYVNPDFVHPDARSPTSPVPVPVM 2UZP Protein kinase C gamma type KPCG_HUMAN P05129 B7Z8Q0 50085353 CNC[C@@H]1CCn2cc(C3=C(C(=O)NC3=O)c3cn(CCO1)c1ccccc31)c1ccccc21 |t:9| InChI=1S/C27H26N4O3/c1-28-14-17-10-11-30-15-20(18-6-2-4-8-22(18)30)24-25(27(33)29-26(24)32)21-16-31(12-13-34-17)23-9-5-3-7-19(21)23/h2-9,15-17,28H,10-14H2,1H3,(H,29,32,33) ZEYTZKVCOZMUKL-UHFFFAOYSA-N 50052034 18-methylaminomethyl-(18S)-17-oxa-4,14,21-triazahexacyclo[19.6.1.17,14.02,6.08,13.022,27]nonacosa-1(28),2(6),7(29),8(13),9,11,22(27),23,25-nonaene-3,5-dione::CHEMBL311543 Protein kinase C epsilon type Homo sapiens 1100 ChEMBL 10.1021/jm950588y 10.7270/Q25H7FBV 8709095 Jirousek, MR; Gillig, JR; Gonzalez, CM; Heath, WF; McDonald, JH; Neel, DA; Rito, CJ; Singh, U; Stramm, LE; Melikian-Badalian, A; Baevsky, M; Ballas, LM; Hall, SE; Winneroski, LL; Faul, MM 9/10/1996 11/10/2009 Eli Lilly http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50052034 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=604&target=Protein+kinase+C+epsilon+type&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50052034&enzyme=Protein+kinase+C+epsilon+type&column=ki&startPg=0&Increment=50&submit=Search 10671412 103948959 CHEMBL311543 1 MVVFNGLLKIKICEAVSLKPTAWSLRHAVGPRPQTFLLDPYIALNVDDSRIGQTATKQKTNSPAWHDEFVTDVCNGRKIELAVFHDAPIGYDDFVANCTIQFEELLQNGSRHFEDWIDLEPEGRVYVIIDLSGSSGEAPKDNEERVFRERMRPRKRQGAVRRRVHQVNGHKFMATYLRQPTYCSHCRDFIWGVIGKQGYQCQVCTCVVHKRCHELIITKCAGLKKQETPDQVGSQRFSVNMPHKFGIHNYKVPTFCDHCGSLLWGLLRQGLQCKVCKMNVHRRCETNVAPNCGVDARGIAKVLADLGVTPDKITNSGQRRKKLIAGAESPQPASGSSPSEEDRSKSAPTSPCDQEIKELENNIRKALSFDNRGEEHRAASSPDGQLMSPGENGEVRQGQAKRLGLDEFNFIKVLGKGSFGKVMLAELKGKDEVYAVKVLKKDVILQDDDVDCTMTEKRILALARKHPYLTQLYCCFQTKDRLFFVMEYVNGGDLMFQIQRSRKFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILLDAEGHCKLADFGMCKEGILNGVTTTTFCGTPDYIAPEILQELEYGPSVDWWALGVLMYEMMAGQPPFEADNEDDLFESILHDDVLYPVWLSKEAVSILKAFMTKNPHKRLGCVASQNGEDAIKQHPFFKEIDWVLLEQKKIKPPFKPRIKTKRDVNNFDQDFTREEPVLTLVDEAIVKQINQEEFKGFSYFGEDLMP Protein kinase C epsilon type KPCE_HUMAN Q02156 B0LPH7 Q32MQ3 Q53SL4 Q53SM5 Q9UE81 50085356 NC[C@@H]1CCn2cc(C3=C(C(=O)NC3=O)c3cn(CCO1)c1ccccc31)c1ccccc21 |t:8| InChI=1S/C26H24N4O3/c27-13-16-9-10-29-14-19(17-5-1-3-7-21(17)29)23-24(26(32)28-25(23)31)20-15-30(11-12-33-16)22-8-4-2-6-18(20)22/h1-8,14-16H,9-13,27H2,(H,28,31,32) JPLUPRIZLHXUPQ-UHFFFAOYSA-N 50052037 18-aminomethyl-(18S)-17-oxa-4,14,21-triazahexacyclo[19.6.1.17,14.02,6.08,13.022,27]nonacosa-1(28),2(6),7(29),8(13),9,11,22(27),23,25-nonaene-3,5-dione::CHEMBL316239 Protein kinase C delta type Homo sapiens 2600 ChEMBL 10.1021/jm950588y 10.7270/Q25H7FBV 8709095 Jirousek, MR; Gillig, JR; Gonzalez, CM; Heath, WF; McDonald, JH; Neel, DA; Rito, CJ; Singh, U; Stramm, LE; Melikian-Badalian, A; Baevsky, M; Ballas, LM; Hall, SE; Winneroski, LL; Faul, MM 9/10/1996 11/10/2009 Eli Lilly http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50052037 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=603&target=Protein+kinase+C+delta+type&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50052037&enzyme=Protein+kinase+C+delta+type&column=ki&startPg=0&Increment=50&submit=Search 10527068 103948962 CHEMBL316239 1 MAPFLRIAFNSYELGSLQAEDEANQPFCAVKMKEALSTERGKTLVQKKPTMYPEWKSTFDAHIYEGRVIQIVLMRAAEEPVSEVTVGVSVLAERCKKNNGKAEFWLDLQPQAKVLMSVQYFLEDVDCKQSMRSEDEAKFPTMNRRGAIKQAKIHYIKNHEFIATFFGQPTFCSVCKDFVWGLNKQGYKCRQCNAAIHKKCIDKIIGRCTGTAANSRDTIFQKERFNIDMPHRFKVHNYMSPTFCDHCGSLLWGLVKQGLKCEDCGMNVHHKCREKVANLCGINQKLLAEALNQVTQRASRRSDSASSEPVGIYQGFEKKTGVAGEDMQDNSGTYGKIWEGSSKCNINNFIFHKVLGKGSFGKVLLGELKGRGEYFAIKALKKDVVLIDDDVECTMVEKRVLTLAAENPFLTHLICTFQTKDHLFFVMEFLNGGDLMYHIQDKGRFELYRATFYAAEIMCGLQFLHSKGIIYRDLKLDNVLLDRDGHIKIADFGMCKENIFGESRASTFCGTPDYIAPEILQGLKYTFSVDWWSFGVLLYEMLIGQSPFHGDDEDELFESIRVDTPHYPRWITKESKDILEKLFEREPTKRLGVTGNIKIHPFFKTINWTLLEKRRLEPPFRPKVKSPRDYSNFDQEFLNEKARLSYSDKNLIDSMDQSAFAGFSFVNPKFEHLLED 1YRK Protein kinase C delta type KPCD_HUMAN Q05655 B0KZ81 B2R834 Q15144 Q86XJ6 50085358 O=C1NC(=O)C2=C1c1cn(CCO[C@H](CNCc3ccccc3)CCn3cc2c2ccccc32)c2ccccc12 |c:5| InChI=1S/C33H30N4O3/c38-32-30-26-20-36(28-12-6-4-10-24(26)28)15-14-23(19-34-18-22-8-2-1-3-9-22)40-17-16-37-21-27(31(30)33(39)35-32)25-11-5-7-13-29(25)37/h1-13,20-21,23,34H,14-19H2,(H,35,38,39) RIXHNSFDUIBDSB-UHFFFAOYSA-N 50052040 18-benzylaminomethyl-(18S)-17-oxa-4,14,21-triazahexacyclo[19.6.1.17,14.02,6.08,13.022,27]nonacosa-1(28),2(6),7(29),8(13),9,11,22(27),23,25-nonaene-3,5-dione::CHEMBL328229 Proto-oncogene tyrosine-protein kinase Src Homo sapiens >100000 ChEMBL 10.1021/jm950588y 10.7270/Q25H7FBV 8709095 Jirousek, MR; Gillig, JR; Gonzalez, CM; Heath, WF; McDonald, JH; Neel, DA; Rito, CJ; Singh, U; Stramm, LE; Melikian-Badalian, A; Baevsky, M; Ballas, LM; Hall, SE; Winneroski, LL; Faul, MM 9/10/1996 11/10/2009 Eli Lilly http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50052040 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=13&target=Proto-oncogene+tyrosine-protein+kinase+Src&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50052040&enzyme=Proto-oncogene+tyrosine-protein+kinase+Src&column=ki&startPg=0&Increment=50&submit=Search 10768554 103948965 CHEMBL328229 1 MGSNKSKPKDASQRRRSLEPAENVHGAGGGAFPASQTPSKPASADGHRGPSAAFAPAAAEPKLFGGFNSSDTVTSPQRAGPLAGGVTTFVALYDYESRTETDLSFKKGERLQIVNNTEGDWWLAHSLSTGQTGYIPSNYVAPSDSIQAEEWYFGKITRRESERLLLNAENPRGTFLVRESETTKGAYCLSVSDFDNAKGLNVKHYKIRKLDSGGFYITSRTQFNSLQQLVAYYSKHADGLCHRLTTVCPTSKPQTQGLAKDAWEIPRESLRLEVKLGQGCFGEVWMGTWNGTTRVAIKTLKPGTMSPEAFLQEAQVMKKLRHEKLVQLYAVVSEEPIYIVTEYMSKGSLLDFLKGETGKYLRLPQLVDMAAQIASGMAYVERMNYVHRDLRAANILVGENLVCKVADFGLARLIEDNEYTARQGAKFPIKWTAPEAALYGRFTIKSDVWSFGILLTELTTKGRVPYPGMVNREVLDQVERGYRMPCPPECPESLHDLMCQCWRKEPEERPTFEYLQAFLEDYFTSTEPQYQPGENL 8JN9,8JN8,2H8H,2SRC,1Y57,1FMK,2PTK,9NS0,8JF3,6ATE,4MXO,4MXX,2BDJ,2BDF,8HAQ,6E6E,1YI6 Proto-oncogene tyrosine-protein kinase Src SRC_HUMAN P12931 E1P5V4 Q76P87 Q86VB9 Q9H5A8 50085359 CN(C)C[C@@H]1CCn2cc(C3=C(C(=O)NC3=O)c3cn(CCO1)c1ccccc31)c1ccccc21 |r,t:10| InChI=1S/C28H28N4O3/c1-30(2)15-18-11-12-31-16-21(19-7-3-5-9-23(19)31)25-26(28(34)29-27(25)33)22-17-32(13-14-35-18)24-10-6-4-8-20(22)24/h3-10,16-18H,11-15H2,1-2H3,(H,29,33,34) ZCBUQCWBWNUWSU-UHFFFAOYSA-N 17055 (9S)-9-[(dimethylamino)methyl]-6,7,10,11-tetrahydro-9H,18H-5,21:12,17-di(metheno)dibenzo[e,k]pyrrolo[3,4-h][1,4,13]oxadiazacyclohexadecine-18,20(19H)-dione::(18S)-18-[(dimethylamino)methyl]-17-oxa-4,14,21-triazahexacyclo[19.6.1.1^{7,14}.0^{2,6}.0^{8,13}.0^{22,27}]nonacosa-1(28),2(6),7(29),8(13),9,11,22(27),23,25-nonaene-3,5-dione::K00587a::Ruboxistaurin::LY-333531::cid_153999::LY 333531::LY333531 Protein kinase C delta type Homo sapiens 250 ChEMBL 10.1021/jm950588y 10.7270/Q25H7FBV 8709095 Jirousek, MR; Gillig, JR; Gonzalez, CM; Heath, WF; McDonald, JH; Neel, DA; Rito, CJ; Singh, U; Stramm, LE; Melikian-Badalian, A; Baevsky, M; Ballas, LM; Hall, SE; Winneroski, LL; Faul, MM 9/10/1996 11/10/2009 Eli Lilly http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=17055 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=603&target=Protein+kinase+C+delta+type&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=17055&enzyme=Protein+kinase+C+delta+type&column=ki&startPg=0&Increment=50&submit=Search 153999 46517285 1 MAPFLRIAFNSYELGSLQAEDEANQPFCAVKMKEALSTERGKTLVQKKPTMYPEWKSTFDAHIYEGRVIQIVLMRAAEEPVSEVTVGVSVLAERCKKNNGKAEFWLDLQPQAKVLMSVQYFLEDVDCKQSMRSEDEAKFPTMNRRGAIKQAKIHYIKNHEFIATFFGQPTFCSVCKDFVWGLNKQGYKCRQCNAAIHKKCIDKIIGRCTGTAANSRDTIFQKERFNIDMPHRFKVHNYMSPTFCDHCGSLLWGLVKQGLKCEDCGMNVHHKCREKVANLCGINQKLLAEALNQVTQRASRRSDSASSEPVGIYQGFEKKTGVAGEDMQDNSGTYGKIWEGSSKCNINNFIFHKVLGKGSFGKVLLGELKGRGEYFAIKALKKDVVLIDDDVECTMVEKRVLTLAAENPFLTHLICTFQTKDHLFFVMEFLNGGDLMYHIQDKGRFELYRATFYAAEIMCGLQFLHSKGIIYRDLKLDNVLLDRDGHIKIADFGMCKENIFGESRASTFCGTPDYIAPEILQGLKYTFSVDWWSFGVLLYEMLIGQSPFHGDDEDELFESIRVDTPHYPRWITKESKDILEKLFEREPTKRLGVTGNIKIHPFFKTINWTLLEKRRLEPPFRPKVKSPRDYSNFDQEFLNEKARLSYSDKNLIDSMDQSAFAGFSFVNPKFEHLLED 1YRK Protein kinase C delta type KPCD_HUMAN Q05655 B0KZ81 B2R834 Q15144 Q86XJ6 50085361 OC[C@@H]1CCn2cc(C3=C(C(=O)NC3=O)c3cn(CCO1)c1ccccc31)c1ccccc21 |t:8| InChI=1S/C26H23N3O4/c30-15-16-9-10-28-13-19(17-5-1-3-7-21(17)28)23-24(26(32)27-25(23)31)20-14-29(11-12-33-16)22-8-4-2-6-18(20)22/h1-8,13-14,16,30H,9-12,15H2,(H,27,31,32) BGVKOUSMQGMSDY-UHFFFAOYSA-N 50052039 18-hydroxymethyl-(18S)-17-oxa-4,14,21-triazahexacyclo[19.6.1.17,14.02,6.08,13.022,27]nonacosa-1(28),2(6),7(29),8(13),9,11,22(27),23,25-nonaene-3,5-dione::LY-326449::CHEMBL292495 Protein kinase C epsilon type Homo sapiens 79000 ChEMBL 10.1021/jm950588y 10.7270/Q25H7FBV 8709095 Jirousek, MR; Gillig, JR; Gonzalez, CM; Heath, WF; McDonald, JH; Neel, DA; Rito, CJ; Singh, U; Stramm, LE; Melikian-Badalian, A; Baevsky, M; Ballas, LM; Hall, SE; Winneroski, LL; Faul, MM 9/10/1996 11/10/2009 Eli Lilly http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50052039 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=604&target=Protein+kinase+C+epsilon+type&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50052039&enzyme=Protein+kinase+C+epsilon+type&column=ki&startPg=0&Increment=50&submit=Search 10455969 103948964 CHEMBL292495 1 MVVFNGLLKIKICEAVSLKPTAWSLRHAVGPRPQTFLLDPYIALNVDDSRIGQTATKQKTNSPAWHDEFVTDVCNGRKIELAVFHDAPIGYDDFVANCTIQFEELLQNGSRHFEDWIDLEPEGRVYVIIDLSGSSGEAPKDNEERVFRERMRPRKRQGAVRRRVHQVNGHKFMATYLRQPTYCSHCRDFIWGVIGKQGYQCQVCTCVVHKRCHELIITKCAGLKKQETPDQVGSQRFSVNMPHKFGIHNYKVPTFCDHCGSLLWGLLRQGLQCKVCKMNVHRRCETNVAPNCGVDARGIAKVLADLGVTPDKITNSGQRRKKLIAGAESPQPASGSSPSEEDRSKSAPTSPCDQEIKELENNIRKALSFDNRGEEHRAASSPDGQLMSPGENGEVRQGQAKRLGLDEFNFIKVLGKGSFGKVMLAELKGKDEVYAVKVLKKDVILQDDDVDCTMTEKRILALARKHPYLTQLYCCFQTKDRLFFVMEYVNGGDLMFQIQRSRKFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILLDAEGHCKLADFGMCKEGILNGVTTTTFCGTPDYIAPEILQELEYGPSVDWWALGVLMYEMMAGQPPFEADNEDDLFESILHDDVLYPVWLSKEAVSILKAFMTKNPHKRLGCVASQNGEDAIKQHPFFKEIDWVLLEQKKIKPPFKPRIKTKRDVNNFDQDFTREEPVLTLVDEAIVKQINQEEFKGFSYFGEDLMP Protein kinase C epsilon type KPCE_HUMAN Q02156 B0LPH7 Q32MQ3 Q53SL4 Q53SM5 Q9UE81 50085362 CNC[C@@H]1CCn2cc(C3=C(C(=O)NC3=O)c3cn(CCO1)c1ccccc31)c1ccccc21 |t:9| InChI=1S/C27H26N4O3/c1-28-14-17-10-11-30-15-20(18-6-2-4-8-22(18)30)24-25(27(33)29-26(24)32)21-16-31(12-13-34-17)23-9-5-3-7-19(21)23/h2-9,15-17,28H,10-14H2,1H3,(H,29,32,33) ZEYTZKVCOZMUKL-UHFFFAOYSA-N 50052034 18-methylaminomethyl-(18S)-17-oxa-4,14,21-triazahexacyclo[19.6.1.17,14.02,6.08,13.022,27]nonacosa-1(28),2(6),7(29),8(13),9,11,22(27),23,25-nonaene-3,5-dione::CHEMBL311543 Protein kinase C zeta type Homo sapiens 22000 ChEMBL 10.1021/jm950588y 10.7270/Q25H7FBV 8709095 Jirousek, MR; Gillig, JR; Gonzalez, CM; Heath, WF; McDonald, JH; Neel, DA; Rito, CJ; Singh, U; Stramm, LE; Melikian-Badalian, A; Baevsky, M; Ballas, LM; Hall, SE; Winneroski, LL; Faul, MM 9/10/1996 11/10/2009 Eli Lilly http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50052034 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=606&target=Protein+kinase+C+zeta+type&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50052034&enzyme=Protein+kinase+C+zeta+type&column=ki&startPg=0&Increment=50&submit=Search 10671412 103948959 CHEMBL311543 1 MPSRTGPKMEGSGGRVRLKAHYGGDIFITSVDAATTFEELCEEVRDMCRLHQQHPLTLKWVDSEGDPCTVSSQMELEEAFRLARQCRDEGLIIHVFPSTPEQPGLPCPGEDKSIYRRGARRWRKLYRANGHLFQAKRFNRRAYCGQCSERIWGLARQGYRCINCKLLVHKRCHGLVPLTCRKHMDSVMPSQEPPVDDKNEDADLPSEETDGIAYISSSRKHDSIKDDSEDLKPVIDGMDGIKISQGLGLQDFDLIRVIGRGSYAKVLLVRLKKNDQIYAMKVVKKELVHDDEDIDWVQTEKHVFEQASSNPFLVGLHSCFQTTSRLFLVIEYVNGGDLMFHMQRQRKLPEEHARFYAAEICIALNFLHERGIIYRDLKLDNVLLDADGHIKLTDYGMCKEGLGPGDTTSTFCGTPNYIAPEILRGEEYGFSVDWWALGVLMFEMMAGRSPFDIITDNPDMNTEDYLFQVILEKPIRIPRFLSVKASHVLKGFLNKDPKERLGCRPQTGFSDIKSHAFFRSIDWDLLEKKQALPPFQPQITDDYGLDNFDTQFTSEPVQLTPDDEDAIKRIDQSEFEGFEYINPLLLSTEESV Protein kinase C zeta type KPCZ_HUMAN Q05513 A8K4N0 A8MU64 B7Z2J7 E9PCW2 Q15207 Q5SYT5 Q969S4 50085363 O=C1NC(=O)C2=C1c1cn(CCO[C@H](CN3CCOCC3)CCn3cc2c2ccccc32)c2ccccc12 |c:5| InChI=1S/C30H30N4O4/c35-29-27-23-18-33(25-7-3-1-5-21(23)25)10-9-20(17-32-11-14-37-15-12-32)38-16-13-34-19-24(28(27)30(36)31-29)22-6-2-4-8-26(22)34/h1-8,18-20H,9-17H2,(H,31,35,36) CLHMTFQYMLYQME-UHFFFAOYSA-N 50052035 18-(1,4-oxazinan-4-ylmethyl)-(18S)-17-oxa-4,14,21-triazahexacyclo[19.6.1.17,14.02,6.08,13.022,27]nonacosa-1(28),2(6),7(29),8(13),9,11,22(27),23,25-nonaene-3,5-dione::CHEMBL315357 Protein kinase C beta type Homo sapiens 38 ChEMBL 10.1021/jm950588y 10.7270/Q25H7FBV 8709095 Jirousek, MR; Gillig, JR; Gonzalez, CM; Heath, WF; McDonald, JH; Neel, DA; Rito, CJ; Singh, U; Stramm, LE; Melikian-Badalian, A; Baevsky, M; Ballas, LM; Hall, SE; Winneroski, LL; Faul, MM 9/10/1996 11/10/2009 Eli Lilly http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50052035 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=600&target=Protein+kinase+C+beta+type&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50052035&enzyme=Protein+kinase+C+beta+type&column=ki&startPg=0&Increment=50&submit=Search 10673286 103948960 CHEMBL315357 1 MADPAAGPPPSEGEESTVRFARKGALRQKNVHEVKNHKFTARFFKQPTFCSHCTDFIWGFGKQGFQCQVCCFVVHKRCHEFVTFSCPGADKGPASDDPRSKHKFKIHTYSSPTFCDHCGSLLYGLIHQGMKCDTCMMNVHKRCVMNVPSLCGTDHTERRGRIYIQAHIDRDVLIVLVRDAKNLVPMDPNGLSDPYVKLKLIPDPKSESKQKTKTIKCSLNPEWNETFRFQLKESDKDRRLSVEIWDWDLTSRNDFMGSLSFGISELQKASVDGWFKLLSQEEGEYFNVPVPPEGSEANEELRQKFERAKISQGTKVPEEKTTNTVSKFDNNGNRDRMKLTDFNFLMVLGKGSFGKVMLSERKGTDELYAVKILKKDVVIQDDDVECTMVEKRVLALPGKPPFLTQLHSCFQTMDRLYFVMEYVNGGDLMYHIQQVGRFKEPHAVFYAAEIAIGLFFLQSKGIIYRDLKLDNVMLDSEGHIKIADFGMCKENIWDGVTTKTFCGTPDYIAPEIIAYQPYGKSVDWWAFGVLLYEMLAGQAPFEGEDEDELFQSIMEHNVAYPKSMSKEAVAICKGLMTKHPGKRLGCGPEGERDIKEHAFFRYIDWEKLERKEIQPPYKPKARDKRDTSNFDKEFTRQPVELTPTDKLFIMNLDQNEFAGFSYTNPEFVINV 8SE4,8SE3,8SE2,3PFQ,9C5F,1A25 Protein kinase C beta type KPCB_HUMAN P05771 C5IFJ8 D3DWF5 O43744 P05127 Q15138 Q93060 Q9UE49 Q9UE50 Q9UEH8 Q9UJ30 Q9UJ33 50085364 O=C1NC(=O)C2=C1c1cn(CCO[C@H](CNCc3ccccc3)CCn3cc2c2ccccc32)c2ccccc12 |c:5| InChI=1S/C33H30N4O3/c38-32-30-26-20-36(28-12-6-4-10-24(26)28)15-14-23(19-34-18-22-8-2-1-3-9-22)40-17-16-37-21-27(31(30)33(39)35-32)25-11-5-7-13-29(25)37/h1-13,20-21,23,34H,14-19H2,(H,35,38,39) RIXHNSFDUIBDSB-UHFFFAOYSA-N 50052040 18-benzylaminomethyl-(18S)-17-oxa-4,14,21-triazahexacyclo[19.6.1.17,14.02,6.08,13.022,27]nonacosa-1(28),2(6),7(29),8(13),9,11,22(27),23,25-nonaene-3,5-dione::CHEMBL328229 Protein kinase C gamma type Homo sapiens 6500 ChEMBL 10.1021/jm950588y 10.7270/Q25H7FBV 8709095 Jirousek, MR; Gillig, JR; Gonzalez, CM; Heath, WF; McDonald, JH; Neel, DA; Rito, CJ; Singh, U; Stramm, LE; Melikian-Badalian, A; Baevsky, M; Ballas, LM; Hall, SE; Winneroski, LL; Faul, MM 9/10/1996 11/10/2009 Eli Lilly http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50052040 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=602&target=Protein+kinase+C+gamma+type&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50052040&enzyme=Protein+kinase+C+gamma+type&column=ki&startPg=0&Increment=50&submit=Search 10768554 103948965 CHEMBL328229 1 MAGLGPGVGDSEGGPRPLFCRKGALRQKVVHEVKSHKFTARFFKQPTFCSHCTDFIWGIGKQGLQCQVCSFVVHRRCHEFVTFECPGAGKGPQTDDPRNKHKFRLHSYSSPTFCDHCGSLLYGLVHQGMKCSCCEMNVHRRCVRSVPSLCGVDHTERRGRLQLEIRAPTADEIHVTVGEARNLIPMDPNGLSDPYVKLKLIPDPRNLTKQKTRTVKATLNPVWNETFVFNLKPGDVERRLSVEVWDWDRTSRNDFMGAMSFGVSELLKAPVDGWYKLLNQEEGEYYNVPVADADNCSLLQKFEACNYPLELYERVRMGPSSSPIPSPSPSPTDPKRCFFGASPGRLHISDFSFLMVLGKGSFGKVMLAERRGSDELYAIKILKKDVIVQDDDVDCTLVEKRVLALGGRGPGGRPHFLTQLHSTFQTPDRLYFVMEYVTGGDLMYHIQQLGKFKEPHAAFYAAEIAIGLFFLHNQGIIYRDLKLDNVMLDAEGHIKITDFGMCKENVFPGTTTRTFCGTPDYIAPEIIAYQPYGKSVDWWSFGVLLYEMLAGQPPFDGEDEEELFQAIMEQTVTYPKSLSREAVAICKGFLTKHPGKRLGSGPDGEPTIRAHGFFRWIDWERLERLEIPPPFRPRPCGRSGENFDKFFTRAAPALTPPDRLVLASIDQADFQGFTYVNPDFVHPDARSPTSPVPVPVM 2UZP Protein kinase C gamma type KPCG_HUMAN P05129 B7Z8Q0 50085365 O=C1NC(=O)C2=C1c1cn(CCO[C@H](CN3CCCC3)CCn3cc2c2ccccc32)c2ccccc12 |c:5| InChI=1S/C30H30N4O3/c35-29-27-23-18-33(25-9-3-1-7-21(23)25)14-11-20(17-32-12-5-6-13-32)37-16-15-34-19-24(28(27)30(36)31-29)22-8-2-4-10-26(22)34/h1-4,7-10,18-20H,5-6,11-17H2,(H,31,35,36) WORLFHNBHSSAJQ-UHFFFAOYSA-N 50052038 18-tetrahydro-1H-1-pyrrolylmethyl-(18S)-17-oxa-4,14,21-triazahexacyclo[19.6.1.17,14.02,6.08,13.022,27]nonacosa-1(28),2(6),7(29),8(13),9,11,22(27),23,25-nonaene-3,5-dione::CHEMBL419866 Protein kinase C delta type Homo sapiens 3300 ChEMBL 10.1021/jm950588y 10.7270/Q25H7FBV 8709095 Jirousek, MR; Gillig, JR; Gonzalez, CM; Heath, WF; McDonald, JH; Neel, DA; Rito, CJ; Singh, U; Stramm, LE; Melikian-Badalian, A; Baevsky, M; Ballas, LM; Hall, SE; Winneroski, LL; Faul, MM 9/10/1996 11/10/2009 Eli Lilly http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50052038 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=603&target=Protein+kinase+C+delta+type&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50052038&enzyme=Protein+kinase+C+delta+type&column=ki&startPg=0&Increment=50&submit=Search 11799388 103948963 CHEMBL419866 1 MAPFLRIAFNSYELGSLQAEDEANQPFCAVKMKEALSTERGKTLVQKKPTMYPEWKSTFDAHIYEGRVIQIVLMRAAEEPVSEVTVGVSVLAERCKKNNGKAEFWLDLQPQAKVLMSVQYFLEDVDCKQSMRSEDEAKFPTMNRRGAIKQAKIHYIKNHEFIATFFGQPTFCSVCKDFVWGLNKQGYKCRQCNAAIHKKCIDKIIGRCTGTAANSRDTIFQKERFNIDMPHRFKVHNYMSPTFCDHCGSLLWGLVKQGLKCEDCGMNVHHKCREKVANLCGINQKLLAEALNQVTQRASRRSDSASSEPVGIYQGFEKKTGVAGEDMQDNSGTYGKIWEGSSKCNINNFIFHKVLGKGSFGKVLLGELKGRGEYFAIKALKKDVVLIDDDVECTMVEKRVLTLAAENPFLTHLICTFQTKDHLFFVMEFLNGGDLMYHIQDKGRFELYRATFYAAEIMCGLQFLHSKGIIYRDLKLDNVLLDRDGHIKIADFGMCKENIFGESRASTFCGTPDYIAPEILQGLKYTFSVDWWSFGVLLYEMLIGQSPFHGDDEDELFESIRVDTPHYPRWITKESKDILEKLFEREPTKRLGVTGNIKIHPFFKTINWTLLEKRRLEPPFRPKVKSPRDYSNFDQEFLNEKARLSYSDKNLIDSMDQSAFAGFSFVNPKFEHLLED 1YRK Protein kinase C delta type KPCD_HUMAN Q05655 B0KZ81 B2R834 Q15144 Q86XJ6 50085375 CN1CCN(C[C@@H]2CCn3cc(C4=C(C(=O)NC4=O)c4cn(CCO2)c2ccccc42)c2ccccc32)CC1 |t:12| InChI=1S/C31H33N5O3/c1-33-12-14-34(15-13-33)18-21-10-11-35-19-24(22-6-2-4-8-26(22)35)28-29(31(38)32-30(28)37)25-20-36(16-17-39-21)27-9-5-3-7-23(25)27/h2-9,19-21H,10-18H2,1H3,(H,32,37,38) QKXPAKQCFJVAFI-UHFFFAOYSA-N 50052041 18-(4-methylhexahydro-1-pyrazinylmethyl)-(18S)-17-oxa-4,14,21-triazahexacyclo[19.6.1.17,14.02,6.08,13.022,27]nonacosa-1(28),2(6),7(29),8(13),9,11,22(27),23,25-nonaene-3,5-dione::CHEMBL91959 Protein kinase C zeta type Homo sapiens >5000 ChEMBL 10.1021/jm950588y 10.7270/Q25H7FBV 8709095 Jirousek, MR; Gillig, JR; Gonzalez, CM; Heath, WF; McDonald, JH; Neel, DA; Rito, CJ; Singh, U; Stramm, LE; Melikian-Badalian, A; Baevsky, M; Ballas, LM; Hall, SE; Winneroski, LL; Faul, MM 9/10/1996 11/10/2009 Eli Lilly http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50052041 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=606&target=Protein+kinase+C+zeta+type&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50052041&enzyme=Protein+kinase+C+zeta+type&column=ki&startPg=0&Increment=50&submit=Search 10768377 103948966 CHEMBL91959 1 MPSRTGPKMEGSGGRVRLKAHYGGDIFITSVDAATTFEELCEEVRDMCRLHQQHPLTLKWVDSEGDPCTVSSQMELEEAFRLARQCRDEGLIIHVFPSTPEQPGLPCPGEDKSIYRRGARRWRKLYRANGHLFQAKRFNRRAYCGQCSERIWGLARQGYRCINCKLLVHKRCHGLVPLTCRKHMDSVMPSQEPPVDDKNEDADLPSEETDGIAYISSSRKHDSIKDDSEDLKPVIDGMDGIKISQGLGLQDFDLIRVIGRGSYAKVLLVRLKKNDQIYAMKVVKKELVHDDEDIDWVQTEKHVFEQASSNPFLVGLHSCFQTTSRLFLVIEYVNGGDLMFHMQRQRKLPEEHARFYAAEICIALNFLHERGIIYRDLKLDNVLLDADGHIKLTDYGMCKEGLGPGDTTSTFCGTPNYIAPEILRGEEYGFSVDWWALGVLMFEMMAGRSPFDIITDNPDMNTEDYLFQVILEKPIRIPRFLSVKASHVLKGFLNKDPKERLGCRPQTGFSDIKSHAFFRSIDWDLLEKKQALPPFQPQITDDYGLDNFDTQFTSEPVQLTPDDEDAIKRIDQSEFEGFEYINPLLLSTEESV Protein kinase C zeta type KPCZ_HUMAN Q05513 A8K4N0 A8MU64 B7Z2J7 E9PCW2 Q15207 Q5SYT5 Q969S4 50085378 CN1CCN(C[C@@H]2CCn3cc(C4=C(C(=O)NC4=O)c4cn(CCO2)c2ccccc42)c2ccccc32)CC1 |t:12| InChI=1S/C31H33N5O3/c1-33-12-14-34(15-13-33)18-21-10-11-35-19-24(22-6-2-4-8-26(22)35)28-29(31(38)32-30(28)37)25-20-36(16-17-39-21)27-9-5-3-7-23(25)27/h2-9,19-21H,10-18H2,1H3,(H,32,37,38) QKXPAKQCFJVAFI-UHFFFAOYSA-N 50052041 18-(4-methylhexahydro-1-pyrazinylmethyl)-(18S)-17-oxa-4,14,21-triazahexacyclo[19.6.1.17,14.02,6.08,13.022,27]nonacosa-1(28),2(6),7(29),8(13),9,11,22(27),23,25-nonaene-3,5-dione::CHEMBL91959 Protein kinase C delta type Homo sapiens 2800 ChEMBL 10.1021/jm950588y 10.7270/Q25H7FBV 8709095 Jirousek, MR; Gillig, JR; Gonzalez, CM; Heath, WF; McDonald, JH; Neel, DA; Rito, CJ; Singh, U; Stramm, LE; Melikian-Badalian, A; Baevsky, M; Ballas, LM; Hall, SE; Winneroski, LL; Faul, MM 9/10/1996 11/10/2009 Eli Lilly http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50052041 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=603&target=Protein+kinase+C+delta+type&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50052041&enzyme=Protein+kinase+C+delta+type&column=ki&startPg=0&Increment=50&submit=Search 10768377 103948966 CHEMBL91959 1 MAPFLRIAFNSYELGSLQAEDEANQPFCAVKMKEALSTERGKTLVQKKPTMYPEWKSTFDAHIYEGRVIQIVLMRAAEEPVSEVTVGVSVLAERCKKNNGKAEFWLDLQPQAKVLMSVQYFLEDVDCKQSMRSEDEAKFPTMNRRGAIKQAKIHYIKNHEFIATFFGQPTFCSVCKDFVWGLNKQGYKCRQCNAAIHKKCIDKIIGRCTGTAANSRDTIFQKERFNIDMPHRFKVHNYMSPTFCDHCGSLLWGLVKQGLKCEDCGMNVHHKCREKVANLCGINQKLLAEALNQVTQRASRRSDSASSEPVGIYQGFEKKTGVAGEDMQDNSGTYGKIWEGSSKCNINNFIFHKVLGKGSFGKVLLGELKGRGEYFAIKALKKDVVLIDDDVECTMVEKRVLTLAAENPFLTHLICTFQTKDHLFFVMEFLNGGDLMYHIQDKGRFELYRATFYAAEIMCGLQFLHSKGIIYRDLKLDNVLLDRDGHIKIADFGMCKENIFGESRASTFCGTPDYIAPEILQGLKYTFSVDWWSFGVLLYEMLIGQSPFHGDDEDELFESIRVDTPHYPRWITKESKDILEKLFEREPTKRLGVTGNIKIHPFFKTINWTLLEKRRLEPPFRPKVKSPRDYSNFDQEFLNEKARLSYSDKNLIDSMDQSAFAGFSFVNPKFEHLLED 1YRK Protein kinase C delta type KPCD_HUMAN Q05655 B0KZ81 B2R834 Q15144 Q86XJ6 50085379 CN(C)C[C@@H]1CCn2cc(C3=C(C(=O)NC3=O)c3cn(CCO1)c1ccccc31)c1ccccc21 |r,t:10| InChI=1S/C28H28N4O3/c1-30(2)15-18-11-12-31-16-21(19-7-3-5-9-23(19)31)25-26(28(34)29-27(25)33)22-17-32(13-14-35-18)24-10-6-4-8-20(22)24/h3-10,16-18H,11-15H2,1-2H3,(H,29,33,34) ZCBUQCWBWNUWSU-UHFFFAOYSA-N 17055 (9S)-9-[(dimethylamino)methyl]-6,7,10,11-tetrahydro-9H,18H-5,21:12,17-di(metheno)dibenzo[e,k]pyrrolo[3,4-h][1,4,13]oxadiazacyclohexadecine-18,20(19H)-dione::(18S)-18-[(dimethylamino)methyl]-17-oxa-4,14,21-triazahexacyclo[19.6.1.1^{7,14}.0^{2,6}.0^{8,13}.0^{22,27}]nonacosa-1(28),2(6),7(29),8(13),9,11,22(27),23,25-nonaene-3,5-dione::K00587a::Ruboxistaurin::LY-333531::cid_153999::LY 333531::LY333531 Protein kinase C zeta type Homo sapiens >100000 ChEMBL 10.1021/jm950588y 10.7270/Q25H7FBV 8709095 Jirousek, MR; Gillig, JR; Gonzalez, CM; Heath, WF; McDonald, JH; Neel, DA; Rito, CJ; Singh, U; Stramm, LE; Melikian-Badalian, A; Baevsky, M; Ballas, LM; Hall, SE; Winneroski, LL; Faul, MM 9/10/1996 11/10/2009 Eli Lilly http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=17055 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=606&target=Protein+kinase+C+zeta+type&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=17055&enzyme=Protein+kinase+C+zeta+type&column=ki&startPg=0&Increment=50&submit=Search 153999 46517285 1 MPSRTGPKMEGSGGRVRLKAHYGGDIFITSVDAATTFEELCEEVRDMCRLHQQHPLTLKWVDSEGDPCTVSSQMELEEAFRLARQCRDEGLIIHVFPSTPEQPGLPCPGEDKSIYRRGARRWRKLYRANGHLFQAKRFNRRAYCGQCSERIWGLARQGYRCINCKLLVHKRCHGLVPLTCRKHMDSVMPSQEPPVDDKNEDADLPSEETDGIAYISSSRKHDSIKDDSEDLKPVIDGMDGIKISQGLGLQDFDLIRVIGRGSYAKVLLVRLKKNDQIYAMKVVKKELVHDDEDIDWVQTEKHVFEQASSNPFLVGLHSCFQTTSRLFLVIEYVNGGDLMFHMQRQRKLPEEHARFYAAEICIALNFLHERGIIYRDLKLDNVLLDADGHIKLTDYGMCKEGLGPGDTTSTFCGTPNYIAPEILRGEEYGFSVDWWALGVLMFEMMAGRSPFDIITDNPDMNTEDYLFQVILEKPIRIPRFLSVKASHVLKGFLNKDPKERLGCRPQTGFSDIKSHAFFRSIDWDLLEKKQALPPFQPQITDDYGLDNFDTQFTSEPVQLTPDDEDAIKRIDQSEFEGFEYINPLLLSTEESV Protein kinase C zeta type KPCZ_HUMAN Q05513 A8K4N0 A8MU64 B7Z2J7 E9PCW2 Q15207 Q5SYT5 Q969S4 50085380 OC[C@@H]1CCn2cc(C3=C(C(=O)NC3=O)c3cn(CCO1)c1ccccc31)c1ccccc21 |t:8| InChI=1S/C26H23N3O4/c30-15-16-9-10-28-13-19(17-5-1-3-7-21(17)28)23-24(26(32)27-25(23)31)20-14-29(11-12-33-16)22-8-4-2-6-18(20)22/h1-8,13-14,16,30H,9-12,15H2,(H,27,31,32) BGVKOUSMQGMSDY-UHFFFAOYSA-N 50052039 18-hydroxymethyl-(18S)-17-oxa-4,14,21-triazahexacyclo[19.6.1.17,14.02,6.08,13.022,27]nonacosa-1(28),2(6),7(29),8(13),9,11,22(27),23,25-nonaene-3,5-dione::LY-326449::CHEMBL292495 Protein kinase C zeta type Homo sapiens 8700.0 ChEMBL 10.1021/jm950588y 10.7270/Q25H7FBV 8709095 Jirousek, MR; Gillig, JR; Gonzalez, CM; Heath, WF; McDonald, JH; Neel, DA; Rito, CJ; Singh, U; Stramm, LE; Melikian-Badalian, A; Baevsky, M; Ballas, LM; Hall, SE; Winneroski, LL; Faul, MM 9/10/1996 11/10/2009 Eli Lilly http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50052039 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=606&target=Protein+kinase+C+zeta+type&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50052039&enzyme=Protein+kinase+C+zeta+type&column=ki&startPg=0&Increment=50&submit=Search 10455969 103948964 CHEMBL292495 1 MPSRTGPKMEGSGGRVRLKAHYGGDIFITSVDAATTFEELCEEVRDMCRLHQQHPLTLKWVDSEGDPCTVSSQMELEEAFRLARQCRDEGLIIHVFPSTPEQPGLPCPGEDKSIYRRGARRWRKLYRANGHLFQAKRFNRRAYCGQCSERIWGLARQGYRCINCKLLVHKRCHGLVPLTCRKHMDSVMPSQEPPVDDKNEDADLPSEETDGIAYISSSRKHDSIKDDSEDLKPVIDGMDGIKISQGLGLQDFDLIRVIGRGSYAKVLLVRLKKNDQIYAMKVVKKELVHDDEDIDWVQTEKHVFEQASSNPFLVGLHSCFQTTSRLFLVIEYVNGGDLMFHMQRQRKLPEEHARFYAAEICIALNFLHERGIIYRDLKLDNVLLDADGHIKLTDYGMCKEGLGPGDTTSTFCGTPNYIAPEILRGEEYGFSVDWWALGVLMFEMMAGRSPFDIITDNPDMNTEDYLFQVILEKPIRIPRFLSVKASHVLKGFLNKDPKERLGCRPQTGFSDIKSHAFFRSIDWDLLEKKQALPPFQPQITDDYGLDNFDTQFTSEPVQLTPDDEDAIKRIDQSEFEGFEYINPLLLSTEESV Protein kinase C zeta type KPCZ_HUMAN Q05513 A8K4N0 A8MU64 B7Z2J7 E9PCW2 Q15207 Q5SYT5 Q969S4 50085385 OC[C@@H]1CCn2cc(C3=C(C(=O)NC3=O)c3cn(CCO1)c1ccccc31)c1ccccc21 |t:8| InChI=1S/C26H23N3O4/c30-15-16-9-10-28-13-19(17-5-1-3-7-21(17)28)23-24(26(32)27-25(23)31)20-14-29(11-12-33-16)22-8-4-2-6-18(20)22/h1-8,13-14,16,30H,9-12,15H2,(H,27,31,32) BGVKOUSMQGMSDY-UHFFFAOYSA-N 50052039 18-hydroxymethyl-(18S)-17-oxa-4,14,21-triazahexacyclo[19.6.1.17,14.02,6.08,13.022,27]nonacosa-1(28),2(6),7(29),8(13),9,11,22(27),23,25-nonaene-3,5-dione::LY-326449::CHEMBL292495 Protein kinase C gamma type Homo sapiens 2000 ChEMBL 10.1021/jm950588y 10.7270/Q25H7FBV 8709095 Jirousek, MR; Gillig, JR; Gonzalez, CM; Heath, WF; McDonald, JH; Neel, DA; Rito, CJ; Singh, U; Stramm, LE; Melikian-Badalian, A; Baevsky, M; Ballas, LM; Hall, SE; Winneroski, LL; Faul, MM 9/10/1996 11/10/2009 Eli Lilly http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50052039 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=602&target=Protein+kinase+C+gamma+type&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50052039&enzyme=Protein+kinase+C+gamma+type&column=ki&startPg=0&Increment=50&submit=Search 10455969 103948964 CHEMBL292495 1 MAGLGPGVGDSEGGPRPLFCRKGALRQKVVHEVKSHKFTARFFKQPTFCSHCTDFIWGIGKQGLQCQVCSFVVHRRCHEFVTFECPGAGKGPQTDDPRNKHKFRLHSYSSPTFCDHCGSLLYGLVHQGMKCSCCEMNVHRRCVRSVPSLCGVDHTERRGRLQLEIRAPTADEIHVTVGEARNLIPMDPNGLSDPYVKLKLIPDPRNLTKQKTRTVKATLNPVWNETFVFNLKPGDVERRLSVEVWDWDRTSRNDFMGAMSFGVSELLKAPVDGWYKLLNQEEGEYYNVPVADADNCSLLQKFEACNYPLELYERVRMGPSSSPIPSPSPSPTDPKRCFFGASPGRLHISDFSFLMVLGKGSFGKVMLAERRGSDELYAIKILKKDVIVQDDDVDCTLVEKRVLALGGRGPGGRPHFLTQLHSTFQTPDRLYFVMEYVTGGDLMYHIQQLGKFKEPHAAFYAAEIAIGLFFLHNQGIIYRDLKLDNVMLDAEGHIKITDFGMCKENVFPGTTTRTFCGTPDYIAPEIIAYQPYGKSVDWWSFGVLLYEMLAGQPPFDGEDEEELFQAIMEQTVTYPKSLSREAVAICKGFLTKHPGKRLGSGPDGEPTIRAHGFFRWIDWERLERLEIPPPFRPRPCGRSGENFDKFFTRAAPALTPPDRLVLASIDQADFQGFTYVNPDFVHPDARSPTSPVPVPVM 2UZP Protein kinase C gamma type KPCG_HUMAN P05129 B7Z8Q0