Structure of PDB 1hv5 Chain B Binding Site BS04

Receptor Information
>1hv5 Chain B (length=164) Species: 10090 (Mus musculus) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
MFVLSGGRWEKTDLTYRILRFPWQLVREQVRQTVAEALQVWSEVTPLTFT
EVHEGRADIMIDFARYWHGDNLPFDGPGGILAHAFFPKTHREGDVHFDYD
ETWTIGDNQGTDLLQVAAHEFGHVLGLQHTTAAKALMSPFYTFRYPLSLS
PDDRRGIQHLYGRP
Ligand information
Ligand IDRXP
InChIInChI=1S/C39H43N4O6P/c40-37(44)35(24-32-25-41-34-22-11-10-21-33(32)34)42-38(45)31(20-12-19-28-13-4-1-5-14-28)27-50(47,48)36(23-29-15-6-2-7-16-29)43-39(46)49-26-30-17-8-3-9-18-30/h1-11,13-18,21-22,25,31,35-36,41H,12,19-20,23-24,26-27H2,(H2,40,44)(H,42,45)(H,43,46)(H,47,48)/t31-,35+,36+/m1/s1
InChIKeyYQEMFOGNUTYMTJ-JNBVYXHXSA-N
SMILES
SoftwareSMILES
OpenEye OEToolkits 1.5.0c1ccc(cc1)CCCC(CP(=O)(C(Cc2ccccc2)NC(=O)OCc3ccccc3)O)C(=O)NC(Cc4c[nH]c5c4cccc5)C(=O)N
OpenEye OEToolkits 1.5.0c1ccc(cc1)CCC[C@H](C[P@@](=O)([C@@H](Cc2ccccc2)NC(=O)OCc3ccccc3)O)C(=O)N[C@@H](Cc4c[nH]c5c4cccc5)C(=O)N
CACTVS 3.341NC(=O)[CH](Cc1c[nH]c2ccccc12)NC(=O)[CH](CCCc3ccccc3)C[P](O)(=O)[CH](Cc4ccccc4)NC(=O)OCc5ccccc5
ACDLabs 10.04O=C(OCc1ccccc1)NC(Cc2ccccc2)P(=O)(O)CC(C(=O)NC(C(=O)N)Cc4c3ccccc3nc4)CCCc5ccccc5
CACTVS 3.341NC(=O)[C@H](Cc1c[nH]c2ccccc12)NC(=O)[C@H](CCCc3ccccc3)C[P@@](O)(=O)[C@@H](Cc4ccccc4)NC(=O)OCc5ccccc5
FormulaC39 H43 N4 O6 P
Name1-BENZYLOXYCARBONYLAMINO-2-PHENYL-ETHYL)-{2-[1-CARBAMOYL-2-(1H-INDOL-3-YL)-ETHYLCARBAMOYL]-5-PHENYL-PENTYL}-PHOSPHINIC ACID
ChEMBL
DrugBankDB04318
ZINCZINC000026576087
PDB chain1hv5 Chain B Residue 6002 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

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PDB1hv5 Crystal structure of the stromelysin-3 (MMP-11) catalytic domain complexed with a phosphinic inhibitor mimicking the transition-state.
Resolution2.6 Å
Binding residue
(original residue number in PDB)		L172 G179 I180 L181 A182 A184 Q215 H219 E220 H223 F240 Y241
Binding residue
(residue number reindexed from 1)		L72 G79 I80 L81 A82 A84 Q115 H119 E120 H123 F140 Y141
Annotation score1
Binding affinityBindingDB: Ki=5nM
Enzymatic activity
Catalytic site (original residue number in PDB) H219 E220 H223 H229
Catalytic site (residue number reindexed from 1) H119 E120 H123 H129
Enzyme Commision number 3.4.24.-
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:1hv5, PDBe:1hv5, PDBj:1hv5
PDBsum1hv5
PubMed11254383
UniProtQ02853|MMP11_MOUSE Stromelysin-3 (Gene Name=Mmp11)

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