Structure of PDB 2w0d Chain B

Receptor sequence
>2w0dB (length=158) Species: 9606 (Homo sapiens) [Search protein sequence]
GPVWRKHYITYRINNYTPDMNREDVDYAIRKAFQVWSNVTPLKFSKINTG
MADILVVFARGAHGDFHAFDGKGGILAHAFGPGSGIGGDAHFDEDEFWTT
HSGGTNLFLTAVHAIGHSLGLGHSSDPKAVMFPTYKYVDINTFRLSADDI
RGIQSLYG
3D structure
PDB2w0d Does a Fast Nuclear Magnetic Resonance Spectroscopy- and X-Ray Crystallography Hybrid Approach Provide Reliable Structural Information of Ligand-Protein Complexes? a Case Study of Metalloproteinases.
ChainB
Resolution2.0 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 A219 H222 H228
Catalytic site (residue number reindexed from 1) H113 A114 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 B H218 H222 H228 H113 H117 H123
BS02 ZN B H168 D170 H183 H196 H63 D65 H78 H91
BS03 CA B D175 G176 G178 I180 D198 E201 D70 G71 G73 I75 D93 E96
BS04 CA B D124 E199 E201 D19 E94 E96
BS05 CA B D158 G190 G192 D194 D53 G85 G87 D89
BS06 CGS B I180 L181 A182 H218 H222 H228 P238 I75 L76 A77 H113 H117 H123 P133 MOAD: ic50~2nM
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:2w0d, PDBe:2w0d, PDBj:2w0d
PDBsum2w0d
PubMed19239231
UniProtP39900|MMP12_HUMAN Macrophage metalloelastase (Gene Name=MMP12)

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