Structure of PDB 1mmq Chain A Binding Site BS01

Receptor Information
>1mmq Chain A (length=166) Species: 9606 (Homo sapiens) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
YSLFPNSPKWTSKVVTYRIVSYTRDLPHITVDRLVSKALNMWGKEIPLHF
RKVVWGTADIMIGFARGAHGDSYPFDGPGNTLAHAFAPGTGLGGDAHFDE
DERWTDGSSLGINFLYAATHELGHSLGMGHSSDPNAVMYPTYGNGDPQNF
KLSQDDIKGIQKLYGK
Ligand information
Ligand IDZN
InChIInChI=1S/Zn/q+2
InChIKeyPTFCDOFLOPIGGS-UHFFFAOYSA-N
SMILES
SoftwareSMILES
CACTVS 3.341[Zn++]
ACDLabs 10.04
OpenEye OEToolkits 1.5.0
[Zn+2]
FormulaZn
NameZINC ION
ChEMBLCHEMBL1236970
DrugBankDB14532
ZINC
PDB chain1mmq Chain A 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]
PDB1mmq Matrilysin-inhibitor complexes: common themes among metalloproteases.
Resolution1.9 Å
Binding residue
(original residue number in PDB)
H218 H222 H228
Binding residue
(residue number reindexed from 1)
H120 H124 H130
Annotation score4
Enzymatic activity
Catalytic site (original residue number in PDB) H218 E219 H222 H228
Catalytic site (residue number reindexed from 1) H120 E121 H124 H130
Enzyme Commision number 3.4.24.23: matrilysin.
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:1mmq, PDBe:1mmq, PDBj:1mmq
PDBsum1mmq
PubMed7756291
UniProtP09237|MMP7_HUMAN Matrilysin (Gene Name=MMP7)

[Back to BioLiP]