Structure of PDB 2woa Chain A

Receptor sequence
>2woaA (length=163) Species: 9606 (Homo sapiens) [Search protein sequence]
MGPVWRKHYITYRINNYTPDMNREDVDYAIRKAFQVWSNVTPLKFSKINT
GMADILVVFARGAHGDFHAFDGKGGILAHAFGPGSGIGGDAHFDEDEFWT
THSGGTNLFLTAVHEIGHSLGLGHSSDPKAVMFPTYKYVDINTFRLSADD
IRGIQSLYGDPKE
3D structure
PDB2woa The Identification of Beta-Hydroxy Carboxylic Acids as Selective Mmp-12 Inhibitors.
ChainA
Resolution2.3 Å
3D
structure
Catalytic site residues are labeled in the structure
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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 A H218 H222 H228 H114 H118 H124
BS02 ZN A H168 D170 H183 H196 H64 D66 H79 H92
BS03 CA A D175 G176 G178 I180 D198 E201 D71 G72 G74 I76 D94 E97
BS04 576 A L181 A182 L214 H218 E219 H228 V235 F237 T239 Y240 K241 L77 A78 L110 H114 E115 H124 V131 F133 T135 Y136 K137 MOAD: ic50=1.15uM
PDBbind-CN: -logKd/Ki=5.94,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

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:2woa, PDBe:2woa, PDBj:2woa
PDBsum2woa
PubMed19703773
UniProtP39900|MMP12_HUMAN Macrophage metalloelastase (Gene Name=MMP12)

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