Structure of PDB 1cgl Chain A Binding Site BS05

Receptor Information
>1cgl Chain A (length=168) Species: 9606 (Homo sapiens) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
VLTEGNPRWEQTHLRYRIENYTPDLPRADVDHAIEKAFQLWSDVTPLTFT
KVSEGQADIMISFVRGDHRDNSPFDGPGGNLAHAFDPGPGIGGDAHFDED
ERWTNNFREYNLHRVAAHELGHSLGLSHSTDIGALMYPSYTFSGDVQLAQ
DDIDGIQAIYGRSQNPVQ
Ligand information
Ligand ID0ED
InChIInChI=1S/C33H47N5O7/c1-24(2)21-28(36-27(32(41)42)13-14-35-33(43)45-23-26-11-7-4-8-12-26)31(40)37-29(22-25-9-5-3-6-10-25)30(39)34-15-16-38-17-19-44-20-18-38/h3-12,24,27-29,36H,13-23H2,1-2H3,(H,34,39)(H,35,43)(H,37,40)(H,41,42)/t27-,28+,29+/m1/s1
InChIKeyXQSMAYNMHYYWCR-ULNSLHSMSA-N
SMILES
SoftwareSMILES
CACTVS 3.341CC(C)C[CH](N[CH](CCNC(=O)OCc1ccccc1)C(O)=O)C(=O)N[CH](Cc2ccccc2)C(=O)NCCN3CCOCC3
CACTVS 3.341CC(C)C[C@H](N[C@@H](CCNC(=O)OCc1ccccc1)C(O)=O)C(=O)N[C@@H](Cc2ccccc2)C(=O)NCCN3CCOCC3
ACDLabs 10.04O=C(O)C(NC(C(=O)NC(C(=O)NCCN1CCOCC1)Cc2ccccc2)CC(C)C)CCNC(=O)OCc3ccccc3
FormulaC33 H47 N5 O7
NameN-[(1S)-3-{[(benzyloxy)carbonyl]amino}-1-carboxypropyl]-L-leucyl-N-(2-morpholin-4-ylethyl)-L-phenylalaninamide
ChEMBL
DrugBank
ZINC
PDB chain1cgl Chain B Residue 1 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB1cgl Structure of the catalytic domain of fibroblast collagenase complexed with an inhibitor.
Resolution2.4 Å
Binding residue
(original residue number in PDB)		G179 T230 P238 S239
Binding residue
(residue number reindexed from 1)		G79 T130 P138 S139
Annotation score1
Binding affinityMOAD: Ki=135nM
PDBbind-CN: -logKd/Ki=6.87,Ki=0.135uM
Enzymatic activity
Catalytic site (original residue number in PDB) H218 E219 H222 H228
Catalytic site (residue number reindexed from 1) H118 E119 H122 H128
Enzyme Commision number 3.4.24.7: interstitial collagenase.
Gene Ontology
Molecular Function
GO:0004222 metalloendopeptidase activity
GO:0008237 metallopeptidase activity
GO:0008270 zinc ion binding
Biological Process
GO:0006508 proteolysis
Cellular Component
GO:0031012 extracellular matrix

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:1cgl, PDBe:1cgl, PDBj:1cgl
PDBsum1cgl
PubMed8278810
UniProtP03956|MMP1_HUMAN Interstitial collagenase (Gene Name=MMP1)

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