Structure of PDB 1cgl Chain B Binding Site BS05

Receptor Information
>1cgl Chain B (length=157) Species: 9606 (Homo sapiens) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
NPRWEQTHLRYRIENYTPDLPRADVDHAIEKAFQLWSDVTPLTFTKVQAD
IMISFVRGDHRDNSPFDGPGGNLAHAFDPGPGIGGDAHFDEDERWTNNFR
EYNLHRVAAHELGHSLGLSHSTDIGALMYPSYTFSGDVQLAQDDIDGIQA
IYGRSQN
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
Global viewLocal viewStructure summary

[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
PDB1cgl Structure of the catalytic domain of fibroblast collagenase complexed with an inhibitor.
Resolution2.4 Å
Binding residue
(original residue number in PDB)		S172 G179 N180 L181 A182 H183 F185 H218 E219 H228 P238 S239 Y240
Binding residue
(residue number reindexed from 1)		S64 G71 N72 L73 A74 H75 F77 H110 E111 H120 P130 S131 Y132
Annotation score1
Binding affinityMOAD: Ki=135nM
Enzymatic activity
Catalytic site (original residue number in PDB) H218 E219 H222 H228
Catalytic site (residue number reindexed from 1) H110 E111 H114 H120
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

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

[Back to BioLiP]