Structure of PDB 2wo9 Chain A

Receptor sequence
>2wo9A (length=162) Species: 9606 (Homo sapiens) [Search protein sequence]
GPVWRKHYITYRINNYTPDMNREDVDYAIRKAFQVWSNVTPLKFSKINTG
MADILVVFARGAHGDFHAFDGKGGILAHAFGPGSGIGGDAHFDEDEFWTT
HSGGTNLFLTAVHEIGHSLGLGHSSDPKAVMFPTYKYVDINTFRLSADDI
RGIQSLYGDPKE
3D structure
PDB2wo9 The Identification of Beta-Hydroxy Carboxylic Acids as Selective Mmp-12 Inhibitors.
ChainA
Resolution1.7 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) 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 ZN A H218 H222 H228 H113 H117 H123
BS02 ZN A H168 D170 H183 H196 H63 D65 H78 H91
BS03 CA A D175 G176 G178 I180 D198 E201 D70 G71 G73 I75 D93 E96
BS04 068 A I180 L181 A182 H218 E219 H222 H228 V235 T239 Y240 F248 I75 L76 A77 H113 E114 H117 H123 V130 T134 Y135 F143 MOAD: ic50=0.062uM
PDBbind-CN: -logKd/Ki=7.21,IC50=62nM
BindingDB: IC50=62nM
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:2wo9, PDBe:2wo9, PDBj:2wo9
PDBsum2wo9
PubMed19703773
UniProtP39900|MMP12_HUMAN Macrophage metalloelastase (Gene Name=MMP12)

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