Structure of PDB 2woa Chain C

Receptor sequence

>2woaC (length=163) Species: 9606 (Homo sapiens)

MGPVWRKHYITYRINNYTPDMNREDVDYAIRKAFQVWSNVTPLKFSKINT
GMADILVVFARGAHGDFHAFDGKGGILAHAFGPGSGIGGDAHFDEDEFWT
THSGGTNLFLTAVHEIGHSLGLGHSSDPKAVMFPTYKYVDINTFRLSADD
IRGIQSLYGDPKE

3D structure

• PDB: 2woa The Identification of Beta-Hydroxy Carboxylic Acids as Selective Mmp-12 Inhibitors.
• Chain: C
• Resolution: 2.3 Å

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)	Binding affinity
BS01	ZN	C	H218 H222 H228	H114 H118 H124
BS02	ZN	C	H168 D170 H183 H196	H64 D66 H79 H92
BS03	CA	C	D175 G176 G178 I180 D198 E201	D71 G72 G74 I76 D94 E97
BS04	CA	C	D158 G190 I191 G192 D194	D54 G86 I87 G88 D90
BS05	CA	C	D124 E199 E201	D20 E95 E97
BS06	576	C	A182 L214 H218 E219 H222 H228 V235 F237 P238 T239 Y240	A78 L110 H114 E115 H118 H124 V131 F133 P134 T135 Y136	MOAD: ic50=1.15uM

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