Structure of PDB 1sln Chain A Binding Site BS06

Receptor Information
>1sln 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]
FRTFPGIPKWRKTHLTYRIVNYTPDLPKDAVDSAVEKALKVWEEVTPLTF
SRLYEGEADIMISFAVREHGDFYPFDGPGNVLAHAYAPGPGINGDAHFDD
DEQWTKDTTGTNLFLVAAHEIGHSLGLFHSANTEALMYPLYHSLTDLTRF
RLSQDDINGIQSLYGPPP
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 chain1sln 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]
PDB1sln Stromelysin-1: three-dimensional structure of the inhibited catalytic domain and of the C-truncated proenzyme.
Resolution2.27 Å
Binding residue
(original residue number in PDB)		N162 L164 A165 L197 V198 H201 E202 H205 H211 L222 Y223
Binding residue
(residue number reindexed from 1)		N80 L82 A83 L115 V116 H119 E120 H123 H129 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:1sln, PDBe:1sln, PDBj:1sln
PDBsum1sln
PubMed8535233
UniProtP08254|MMP3_HUMAN Stromelysin-1 (Gene Name=MMP3)

[Back to BioLiP]