Structure of PDB 1jiz Chain B

Receptor sequence
>1jizB (length=166) Species: 9606 (Homo sapiens) [Search protein sequence]
GFREMPGGPVWRKHYITYRINNYTPDMNREDVDYAIRKAFQVWSNVTPLK
FSKINTGMADILVVFARGAHGDFHAFDGKGGILAHAFGPGSGIGGDAHFD
EDEFWTTHSGGTNLFLTAVHEIGHSLGLGHSSDPKAVMFPTYKYVDINTF
RLSADDIRGIQSLYGD
3D structure
PDB1jiz Crystal structure of human macrophage elastase (MMP-12) in complex with a hydroxamic acid inhibitor.
ChainB
Resolution2.6 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) H119 E120 H123 H129
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 B H119 H123 H129 H120 H124 H130
BS02 ZN B H69 D71 H84 H97 H70 D72 H85 H98
BS03 CA B D76 G77 G79 I81 D99 E102 D77 G78 G80 I82 D100 E103
BS04 CA B D59 G91 I92 G93 D95 D60 G92 I93 G94 D96
BS05 CA B D25 E100 E102 D26 E101 E103
BS06 CGS B I81 L82 T116 H119 E120 H123 H129 P139 I82 L83 T117 H120 E121 H124 H130 P140
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:1jiz, PDBe:1jiz, PDBj:1jiz
PDBsum1jiz
PubMed11575929
UniProtP39900|MMP12_HUMAN Macrophage metalloelastase (Gene Name=MMP12)

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