Structure of PDB 2k2g Chain A

Receptor sequence
>2k2gA (length=165) Species: 9606 (Homo sapiens) [Search protein sequence]
MFREMPGGPVWRKHYITYRINNYTPDMNREDVDYAIRKAFQVWSNVTPLK
FSKINTGMADILVVFARGAHGDFHAFDGKGGILAHAFGPGSGIGGDAHFD
EDEFWTTHSGGTNLFLTAVHEIGHSLGLGHSSDPKAVMFPTYKYVDINTF
RLSADDIRGIQSLYG
3D structure
PDB2k2g Solution structure of wild-type human matrix metalloproteinase 12 (MMP-12) in complex with a tight-binding inhibitor.
ChainA
ResolutionN/A
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) H120 E121 H124 H130
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 H120 H124 H130
BS02 ZN A H168 F171 H183 H196 H70 F73 H85 H98
BS03 DSV A L181 L214 T215 H218 H222 H228 V235 M236 L83 L116 T117 H120 H124 H130 V137 M138 PDBbind-CN: -logKd/Ki=8.12,Kd=7.5nM
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:2k2g, PDBe:2k2g, PDBj:2k2g
PDBsum2k2g
PubMed18425585
UniProtP39900|MMP12_HUMAN Macrophage metalloelastase (Gene Name=MMP12)

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