Structure of PDB 2wo9 Chain D

Receptor sequence

>2wo9D (length=160) Species: 9606 (Homo sapiens)

GPVWRKHYITYRINNYTPDMNREDVDYAIRKAFQVWSNVTPLKFSKINTG
MADILVVFARGAHGDFHAFDGKGGILAHAFGPGSGIGGDAHFDEDEFWTT
HSGGTNLFLTAVHEIGHSLGLGHSSDPKAVMFPTYKYVDINTFRLSADDI
RGIQSLYGDP

3D structure

• PDB: 2wo9 The Identification of Beta-Hydroxy Carboxylic Acids as Selective Mmp-12 Inhibitors.
• Chain: D
• Resolution: 1.7 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	023	D	G179 I180 L181 L214 T215 H218 E219 H222 H228 P238 T239 Y240 K241	G74 I75 L76 L109 T110 H113 E114 H117 H123 P133 T134 Y135 K136
BS02	ZN	D	H218 H222 H228	H113 H117 H123
BS03	ZN	D	H168 D170 H183 H196	H63 D65 H78 H91
BS04	CA	D	D175 G176 G178 I180 D198 E201	D70 G71 G73 I75 D93 E96
BS05	CA	D	D124 E199 E201	D19 E94 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:2wo9, PDBe:2wo9, PDBj:2wo9
• PDBsum: 2wo9
• PubMed: 19703773
• UniProt: P39900|MMP12_HUMAN Macrophage metalloelastase (Gene Name=MMP12)