Structure of PDB 1hv5 Chain B Binding Site BS02
Receptor Information
>1hv5 Chain B (length=164) Species:
10090
(Mus musculus) [
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MFVLSGGRWEKTDLTYRILRFPWQLVREQVRQTVAEALQVWSEVTPLTFT
EVHEGRADIMIDFARYWHGDNLPFDGPGGILAHAFFPKTHREGDVHFDYD
ETWTIGDNQGTDLLQVAAHEFGHVLGLQHTTAAKALMSPFYTFRYPLSLS
PDDRRGIQHLYGRP
Ligand information
Ligand ID
ZN
InChI
InChI=1S/Zn/q+2
InChIKey
PTFCDOFLOPIGGS-UHFFFAOYSA-N
SMILES
Software
SMILES
CACTVS 3.341
[Zn++]
ACDLabs 10.04
OpenEye OEToolkits 1.5.0
[Zn+2]
Formula
Zn
Name
ZINC ION
ChEMBL
CHEMBL1236970
DrugBank
DB14532
ZINC
PDB chain
1hv5 Chain B Residue 5505 [
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Receptor-Ligand Complex Structure
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PDB
1hv5
Crystal structure of the stromelysin-3 (MMP-11) catalytic domain complexed with a phosphinic inhibitor mimicking the transition-state.
Resolution
2.6 Å
Binding residue
(original residue number in PDB)
H219 H223 H229
Binding residue
(residue number reindexed from 1)
H119 H123 H129
Annotation score
4
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
PDBsum
1hv5
PubMed
11254383
UniProt
Q02853
|MMP11_MOUSE Stromelysin-3 (Gene Name=Mmp11)
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