Structure of PDB 2srt Chain A Binding Site BS03

Receptor Information
>2srt Chain A (length=173) Species: 9606 (Homo sapiens) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
FRTFPGIPKWRKTHLTYRIVNYTPDLPKDAVDSAVEKALKVWEEVTPLTF
SRLYEGEADIMISFAVREHGDFYPFDGPGNVLAHAYAPGPGINGDAHFDD
DEQWTKDTTGTNLFLVAAHEIGHSLGLFHSANTEALMYPLYHSLTDLTRF
RLSQDDINGIQSLYGPPPDSPET
Ligand information
Ligand ID8MI
InChIInChI=1S/C25H34N6O4/c1-17(24(34)35)29-21(15-14-18-9-4-2-5-10-18)23(33)31-20(13-8-16-28-25(26)27)22(32)30-19-11-6-3-7-12-19/h2-7,9-12,17,20-21,29H,8,13-16H2,1H3,(H,30,32)(H,31,33)(H,34,35)(H4,26,27,28)/p+1/t17-,20+,21+/m1/s1
InChIKeyHDGWGGCPTVXRNA-QMMLZNLJSA-O
SMILES
SoftwareSMILES
OpenEye OEToolkits 2.0.7C[C@H](C(=O)O)N[C@@H](CCc1ccccc1)C(=O)N[C@@H](CCCNC(=[NH2+])N)C(=O)Nc2ccccc2
CACTVS 3.385C[CH](N[CH](CCc1ccccc1)C(=O)N[CH](CCCNC(N)=[NH2+])C(=O)Nc2ccccc2)C(O)=O
OpenEye OEToolkits 2.0.7CC(C(=O)O)NC(CCc1ccccc1)C(=O)NC(CCCNC(=[NH2+])N)C(=O)Nc2ccccc2
CACTVS 3.385C[C@@H](N[C@@H](CCc1ccccc1)C(=O)N[C@@H](CCCNC(N)=[NH2+])C(=O)Nc2ccccc2)C(O)=O
ACDLabs 12.01O=C(Nc1ccccc1)C(CCCNC(=[NH2+])N)NC(=O)C(CCc1ccccc1)NC(C)C(=O)O
FormulaC25 H35 N6 O4
NameN-(R-CARBOXY-ETHYL)-ALPHA-(S)-(2-PHENYLETHYL)GLYCYL-L-ARGININE-N-PHENYLAMIDE
ChEMBL
DrugBankDB02747
ZINC
PDB chain2srt Chain A Residue 256 [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]
PDB2srt The NMR structure of the inhibited catalytic domain of human stromelysin-1.
ResolutionN/A
Binding residue
(original residue number in PDB)		N162 V163 L164 A165 L197 H201 H211 L218 L222 Y223
Binding residue
(residue number reindexed from 1)		N80 V81 L82 A83 L115 H119 H129 L136 L140 Y141
Annotation score1
Enzymatic activity
Catalytic site (original residue number in PDB) H201 E202 H205 H211
Catalytic site (residue number reindexed from 1) H119 E120 H123 H129
Enzyme Commision number 3.4.24.17: stromelysin 1.
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:2srt, PDBe:2srt, PDBj:2srt
PDBsum2srt
PubMed7656014
UniProtP08254|MMP3_HUMAN Stromelysin-1 (Gene Name=MMP3)

[Back to BioLiP]