Structure of PDB 2oy4 Chain A

Receptor sequence
>2oy4A (length=157) Species: 9606 (Homo sapiens) [Search protein sequence]
PKWERTNLTYRIRNYTPQLSEAEVERAIKDAFELWSVASPLIFTRISQGE
ADINIAFYQRDHGDNSPFDGPNGILAHAFQPGQGIGGDAHFDAEETWTNT
SANYNLFLVAAHEFGHSLGLAHSSDPGALMYPNYAFRETSNYSLPQDDID
GIQAIYG
3D structure
PDB2oy4 Snapshots of the reaction mechanism of matrix metalloproteinases.
ChainA
Resolution1.7 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
Enzymatic activity
Catalytic site (original residue number in PDB) H197 E198 H201 H207
Catalytic site (residue number reindexed from 1) H112 E113 H116 H122
Enzyme Commision number 3.4.24.34: neutrophil collagenase.
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 CA A D137 G169 G171 D173 D52 G84 G86 D88
BS02 CA A D154 G155 N157 I159 D177 E180 D69 G70 N72 I74 D92 E95
BS03 ZN A H147 D149 H162 H175 H62 D64 H77 H90
BS04 ZN A H197 H201 H207 H112 H116 H122
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:2oy4, PDBe:2oy4, PDBj:2oy4
PDBsum2oy4
PubMed17096442
UniProtP22894|MMP8_HUMAN Neutrophil collagenase (Gene Name=MMP8)

[Back to BioLiP]