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BioLiP

Structure of PDB 2oy2 Chain A Binding Site BS01

Receptor Information
>2oy2 Chain A (length=157) Species: 9606 (Homo sapiens) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
PKWERTNLTYRIRNYTPQLSEAEVERAIKDAFELWSVASPLIFTRISQGE
ADINIAFYQRDHGDNSPFDGPNGILAHAFQPGQGIGGDAHFDAEETWTNT
SANYNLFLVAAHEFGHSLGLAHSSDPGALMYPNYAFRETSNYSLPQDDID
GIQAIYG
Ligand information
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

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PDB2oy2 Snapshots of the reaction mechanism of matrix metalloproteinases.
Resolution1.5 Å
Binding residue
(original residue number in PDB)
G158 L160 H197 E198 P217 N218 Y219
Binding residue
(residue number reindexed from 1)
G73 L75 H112 E113 P132 N133 Y134
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.
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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Cellular Component
External links
PDB RCSB:2oy2, PDBe:2oy2, PDBj:2oy2
PDBsum2oy2
PubMed17096442
UniProtP22894|MMP8_HUMAN Neutrophil collagenase (Gene Name=MMP8)

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