Structure of PDB 2n8r Chain A

Receptor sequence
>2n8rA (length=164) Species: 9606 (Homo sapiens) [Search protein sequence]
FREMPGGPVWRKHYITYRINNYTPDMNREDVDYAIRKAFQVWSNVTPLKF
SKINTGMADILVVFARGAHGDFHAFDGKGGILAHAFGPGSGIGGDAHFDE
DEFWTTHSGGTNLFLTAVHEIGHSLGLGHSSDPKAVMFPTYKYVDINTFR
LSADDIRGIQSLYG
3D structure
PDB2n8r Path to Collagenolysis: COLLAGEN V TRIPLE-HELIX MODEL BOUND PRODUCTIVELY AND IN ENCOUNTERS BY MATRIX METALLOPROTEINASE-12.
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) H119 E120 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 I180 D198 E201 D76 G77 G79 I81 D99 E102
BS04 CA A D158 G190 G192 D194 D59 G91 G93 D95
BS05 CA A D124 E199 E201 D25 E100 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:2n8r, PDBe:2n8r, PDBj:2n8r
PDBsum2n8r
PubMed26887942
UniProtP39900|MMP12_HUMAN Macrophage metalloelastase (Gene Name=MMP12)

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