Home
About
Info
Download
WebServices
Contact
Compile Data Set for Download or QSAR
maximum 50k data
Activity Spreadsheet -- Enzyme Inhibition Constant Data from BindingDB
(change energy unit to
kcal/mol
)
Found
3
hits in this display
Target
NAD-dependent protein deacetylase sirtuin-2
(Homo sapiens (Human))
Albert-Ludwigs-University Of Freiburg
Curated by
ChEMBL
Ligand
BDBM50148782
(CHEMBL3770049)
Copy SMILES
Copy InChI
Affinity Data
IC50: 180nM
Assay Description:
Inhibition of N-terminal his6-tagged human SIRT2 (25 to 389 amino acids) using ZMAL as substrate after 4 hrs by fluorescence-based microplate reader ...
More data for this Ligand-Target Pair
Target Info
PDB
MMDB
NCI pathway
Reactome pathway
KEGG
UniProtKB/SwissProt
B.MOAD
antibodypedia
GoogleScholar
Ligand Info
CHEMBL
PC cid
PC sid
In Depth
Details
Article
PubMed
Copy BDB DOI
Target
NAD-dependent protein deacetylase sirtuin-2
(Homo sapiens (Human))
Albert-Ludwigs-University Of Freiburg
Curated by
ChEMBL
Ligand
BDBM50148782
(CHEMBL3770049)
Copy SMILES
Copy InChI
Affinity Data
IC50: 180nM
Assay Description:
Inhibition of recombinant human His10-tagged Sirt2 (56 to 356 residues) expressed in Escherichia coli BL21(DE3) using Z-(Ac)Lys-AMC as substrate meas...
More data for this Ligand-Target Pair
Target Info
PDB
MMDB
NCI pathway
Reactome pathway
KEGG
UniProtKB/SwissProt
B.MOAD
antibodypedia
GoogleScholar
Ligand Info
CHEMBL
PC cid
PC sid
In Depth
Details
Article
PubMed
Copy BDB DOI
Target
NAD-dependent protein deacetylase sirtuin-1
(Homo sapiens (Human))
University Of Freiburg
Curated by
ChEMBL
Ligand
BDBM50148782
(CHEMBL3770049)
Copy SMILES
Copy InChI
Affinity Data
IC50: >1.00E+5nM
Assay Description:
Inhibition of recombinant human GST-tagged Sirt1 (133 to 747 residues) using Z-(Ac)Lys-AMC as substrate measured after 4 hrs by high-throughput fluor...
More data for this Ligand-Target Pair
Target Info
PDB
NCI pathway
Reactome pathway
KEGG
UniProtKB/SwissProt
B.MOAD
antibodypedia
GoogleScholar
Ligand Info
CHEMBL
PC cid
PC sid
In Depth
Details
Article
PubMed
Copy BDB DOI