Structure of PDB 2poj Chain A

Receptor sequence
>2pojA (length=164) Species: 9606 (Homo sapiens) [Search protein sequence]
FREMPGGPVWRKHYITYRINNYTPDMNREDVDYAIRKAFQVWSNVTPLKF
SKINTGMADILVVFARGAHGDFHAFDGKGGILAHAFGPGSGIGGDAHFDE
DEFWTTHSGGTNLFLTAVHAIGHSLGLGHSSDPKAVMFPTYKYVDINTFR
LSADDIRGIQSLYG
3D structure
PDB2poj Solution Structure of Inhibitor-Free Human Metalloelastase (MMP-12) Indicates an Internal Conformational Adjustment.
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 A219 H222 H228
Catalytic site (residue number reindexed from 1) H119 A120 H123 H129
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 H119 H123 H129
BS02 ZN A H168 D170 H183 H196 H69 D71 H84 H97
BS03 CA A D175 G176 G178 G179 I180 L181 D198 E201 D76 G77 G79 G80 I81 L82 D99 E102
BS04 CA A A157 D158 G190 I191 G192 D194 A58 D59 G91 I92 G93 D95
BS05 CA A D124 E199 D200 E201 D25 E100 D101 E102
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:2poj, PDBe:2poj, PDBj:2poj
PDBsum2poj
PubMed17997411
UniProtP39900|MMP12_HUMAN Macrophage metalloelastase (Gene Name=MMP12)

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