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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
4
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Target
Neutrophil collagenase
(Homo sapiens (Human))
TBA
Curated by
ChEMBL
Ligand
BDBM50284757
((R)-3-[(S)-1-Hexylcarbamoyl-2-(1H-indol-3-yl)-ethy...)
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Affinity Data
Ki: 163nM
Assay Description:
Inhibition of human Matrix metalloproteinase-8
More data for this Ligand-Target Pair
Target Info
PDB
MMDB
Reactome pathway
KEGG
UniProtKB/SwissProt
B.MOAD
DrugBank
antibodypedia
GoogleScholar
Ligand Info
CHEMBL
PC cid
PC sid
Similars
In Depth
Details
Article
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Target
Interstitial collagenase
(Homo sapiens (Human))
TBA
Curated by
ChEMBL
Ligand
BDBM50284757
((R)-3-[(S)-1-Hexylcarbamoyl-2-(1H-indol-3-yl)-ethy...)
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Affinity Data
Ki: 171nM
Assay Description:
Inhibition of human fibroblast collagenase, matrix metalloproteinase-1
More data for this Ligand-Target Pair
Target Info
PDB
MMDB
Reactome pathway
KEGG
UniProtKB/SwissProt
B.MOAD
DrugBank
antibodypedia
GoogleScholar
Ligand Info
CHEMBL
PC cid
PC sid
Similars
In Depth
Details
Article
Copy BDB DOI
Target
72 kDa type IV collagenase
(Homo sapiens (Human))
TBA
Curated by
ChEMBL
Ligand
BDBM50284757
((R)-3-[(S)-1-Hexylcarbamoyl-2-(1H-indol-3-yl)-ethy...)
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Affinity Data
Ki: 472nM
Assay Description:
Inhibition of human neutrophil gelatinase, matrix metalloproteinase-2
More data for this Ligand-Target Pair
Target Info
PDB
MMDB
Reactome pathway
KEGG
UniProtKB/SwissProt
B.MOAD
DrugBank
antibodypedia
GoogleScholar
Ligand Info
CHEMBL
PC cid
PC sid
Similars
In Depth
Details
Article
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Target
Matrilysin
(Homo sapiens (Human))
TBA
Curated by
ChEMBL
Ligand
BDBM50284757
((R)-3-[(S)-1-Hexylcarbamoyl-2-(1H-indol-3-yl)-ethy...)
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Copy InChI
Affinity Data
Ki: >620nM
Assay Description:
Inhibition of Matrix metalloproteinase-7
More data for this Ligand-Target Pair
Target Info
PDB
MMDB
Reactome pathway
KEGG
UniProtKB/SwissProt
B.MOAD
DrugBank
antibodypedia
GoogleScholar
Ligand Info
CHEMBL
PC cid
PC sid
Similars
In Depth
Details
Article
Copy BDB DOI