Structure of PDB 2wo9 Chain B

Receptor sequence

>2wo9B (length=162) Species: 9606 (Homo sapiens) [Search protein sequence]

MGPVWRKHYITYRINNYTPDMNREDVDYAIRKAFQVWSNVTPLKFSKINT
GMADILVVFARGAHGDFHAFDGKGGILAHAFGPGSGIGGDAHFDEDEFWT
THSGGTNLFLTAVHEIGHSLGLGHSSDPKAVMFPTYKYVDINTFRLSADD
IRGIQSLYGDPK

3D structure

PDB

2wo9 The Identification of Beta-Hydroxy Carboxylic Acids as Selective Mmp-12 Inhibitors.

Chain

Resolution

1.7 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)	H218 E219 H222 H228
Catalytic site (residue number reindexed from 1)	H114 E115 H118 H124
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)
BS01	023	B	G179 I180 L181 L214 T215 H218 E219 H222 H228 P238 T239 Y240 K241	G75 I76 L77 L110 T111 H114 E115 H118 H124 P134 T135 Y136 K137
BS02	ZN	B	H218 H222 H228	H114 H118 H124
BS03	ZN	B	H168 D170 H183 H196	H64 D66 H79 H92
BS04	CA	B	D175 G176 G178 I180 D198 E201	D71 G72 G74 I76 D94 E97
BS05	CA	B	D158 G190 I191 G192 D194	D54 G86 I87 G88 D90
BS06	CA	B	D124 E199 E201	D20 E95 E97

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:2wo9, PDBe:2wo9, PDBj:2wo9
PDBsum	2wo9
PubMed	19703773
UniProt	P39900\|MMP12_HUMAN Macrophage metalloelastase (Gene Name=MMP12)

[Back to BioLiP]