Structure of PDB 3ayu Chain A Binding Site BS01

Receptor Information
>3ayu 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]
YNFFPRKPKWDKNQITYRIIGYTPDLDPETVDDAFARAFQVWSDVTPLRF
SRIHDGEADIMINFGRWEHGDGYPFDGKDGLLAHAFAPGTGVGGDSHFDD
DELWTLGKGVGYSLFLVAAHAFGHAMGLEHSQDPGALMAPIYTYTKNFRL
SQDDIKGIQELYGASP
Ligand information
Receptor-Ligand Complex Structure
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PDB3ayu Structural basis for matrix metalloproteinase-2 (MMP-2)-selective inhibitory action of {beta}-amyloid precursor protein-derived inhibitor
Resolution2.0 Å
Binding residue
(original residue number in PDB)		F4 Y73 H84 A85 F86 V92 G93 Y112 H120 H124 H130 P140 I141 Y142
Binding residue
(residue number reindexed from 1)		F4 Y73 H84 A85 F86 V92 G93 Y112 H120 H124 H130 P140 I141 Y142
Enzymatic activity
Catalytic site (original residue number in PDB) H120 A121 H124 H130
Catalytic site (residue number reindexed from 1) H120 A121 H124 H130
Enzyme Commision number 3.4.24.24: gelatinase A.
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:3ayu, PDBe:3ayu, PDBj:3ayu
PDBsum3ayu
PubMed21813640
UniProtP08253|MMP2_HUMAN 72 kDa type IV collagenase (Gene Name=MMP2)

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