Structure of PDB 1os2 Chain E

Receptor sequence
>1os2E (length=165) Species: 9606 (Homo sapiens) [Search protein sequence]
MMGPVWRKHYITYRINNYTPDMNREDVDYAIRKAFQVWSNVTPLKFSKIN
TGMADILVVFARGAHGDDHAFDGKGGILAHAFGPGSGIGGDAHFDEDEFW
TTHSGGTNLFLTAVHEIGHSLGLGHSSDPKAVMFPTYKYVDINTFRLSAD
DIRGIQSLYGDPKEN
3D structure
PDB1os2 X-ray Structures of Binary and Ternary Enzyme-Product-Inhibitor Complexes of Matrix Metalloproteinases
ChainE
Resolution2.15 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) H115 E116 H119 H125
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 E H218 H222 H228 H115 H119 H125
BS02 ZN E H168 D170 H183 H196 H65 D67 H80 H93
BS03 CA E D175 G176 G178 I180 D198 E201 D72 G73 G75 I77 D95 E98
BS04 CA E D158 G190 G192 D194 D55 G87 G89 D91
BS05 CA E D124 E199 E201 D21 E96 E98
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:1os2, PDBe:1os2, PDBj:1os2
PDBsum1os2
PubMed12813751
UniProtP39900|MMP12_HUMAN Macrophage metalloelastase (Gene Name=MMP12)

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