Structure of PDB 3ayu Chain A

Receptor sequence

>3ayuA (length=166) Species: 9606 (Homo sapiens)

YNFFPRKPKWDKNQITYRIIGYTPDLDPETVDDAFARAFQVWSDVTPLRF
SRIHDGEADIMINFGRWEHGDGYPFDGKDGLLAHAFAPGTGVGGDSHFDD
DELWTLGKGVGYSLFLVAAHAFGHAMGLEHSQDPGALMAPIYTYTKNFRL
SQDDIKGIQELYGASP

3D structure

• PDB: 3ayu Structural basis for matrix metalloproteinase-2 (MMP-2)-selective inhibitory action of {beta}-amyloid precursor protein-derived inhibitor
• Chain: A
• Resolution: 2.0 Å

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.

Interaction with ligand

Site #	Ligand	Ligand chain	Binding residues on receptor (original residue number in PDB)	Binding residues on receptor (residue number reindexed from 1)	Binding affinity
BS01	peptide	A	F4 Y73 H84 A85 F86 V92 G93 Y112 H120 H124 H130 P140 I141 Y142	F4 Y73 H84 A85 F86 V92 G93 Y112 H120 H124 H130 P140 I141 Y142
BS02	ZN	A	H120 H124 H130	H120 H124 H130
BS03	ZN	A	H69 D71 H84 H97	H69 D71 H84 H97
BS04	CA	A	D76 G77 D79 L81 D99 E102	D76 G77 D79 L81 D99 E102
BS05	CA	A	D59 G91 G93 D95	D59 G91 G93 D95
BS06	CA	A	D25 D100 E102	D25 D100 E102

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

External links

• PDB: RCSB:3ayu, PDBe:3ayu, PDBj:3ayu
• PDBsum: 3ayu
• PubMed: 21813640
• UniProt: P08253|MMP2_HUMAN 72 kDa type IV collagenase (Gene Name=MMP2)