Structure of PDB 2oxz Chain A

Receptor sequence

>2oxzA (length=158) Species: 9606 (Homo sapiens)

GPVWRKHYITYRINNYTPDMNREDVDYAIRKAFQVWSNVTPLKFSKINTG
MADILVVFARGAHGDDHAFDGKGGILAHAFGPGSGIGGDAHFDEDEFWTT
HSGGTNLFLTAVHEIGHSLGLGHSSDPKAVMFPTYKYVDINTFRLSADDI
RGIQSLYG

3D structure

• PDB: 2oxz Snapshots of the reaction mechanism of matrix metalloproteinases.
• Chain: A
• Resolution: 1.9 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): H218 E219 H222 H228
• Catalytic site (residue number reindexed from 1): H113 E114 H117 H123
• Enzyme Commision number: 3.4.24.65: macrophage elastase.

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	A184 H222 H228	A79 H117 H123
BS02	peptide	A	G179 L181 H218 E219 P238 T239 Y240	G74 L76 H113 E114 P133 T134 Y135
BS03	ZN	A	H218 H222 H228	H113 H117 H123
BS04	ZN	A	H168 D170 H183 H196	H63 D65 H78 H91
BS05	CA	A	D158 G190 G192 D194	D53 G85 G87 D89
BS06	CA	A	D124 E199 E201	D19 E94 E96
BS07	CA	A	D175 G176 G178 I180 D198 E201	D70 G71 G73 I75 D93 E96

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:2oxz, PDBe:2oxz, PDBj:2oxz
• PDBsum: 2oxz
• PubMed: 17096442
• UniProt: P39900|MMP12_HUMAN Macrophage metalloelastase (Gene Name=MMP12)