Structure of PDB 3f15 Chain A

Receptor sequence
>3f15A (length=158) Species: 9606 (Homo sapiens) [Search protein sequence]
GPVWRKHYITYRINNYTPDMNREDVDYAIRKAFQVWSNVTPLKFSKINTG
MADILVVFARGAHGDDHAFDGKGGILAHAFGPGSGIGGDAHFDEDEFWTT
HSGGTNLFLTAVHEIGHSLGLGHSSDPKAVMFPTYKYVDINTFRLSADDI
RGIQSLYG
3D structure
PDB3f15 Exploring the subtleties of drug-receptor interactions: the case of matrix metalloproteinases.
ChainA
Resolution1.7 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) H113 E114 H117 H123
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 H113 H117 H123
BS02 ZN A H168 D170 H183 H196 H63 D65 H78 H91
BS03 CA A D158 G190 I191 G192 D194 D53 G85 I86 G87 D89
BS04 CA A D124 E199 E201 D19 E94 E96
BS05 CA A D175 G176 G178 I180 D198 E201 D70 G71 G73 I75 D93 E96
BS06 HS1 A I180 L181 A182 H218 E219 H222 H228 P238 Y240 I75 L76 A77 H113 E114 H117 H123 P133 Y135 MOAD: Kd=7.88nM
PDBbind-CN: -logKd/Ki=8.10,Kd=7.88nM
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:3f15, PDBe:3f15, PDBj:3f15
PDBsum3f15
PubMed17269766
UniProtP39900|MMP12_HUMAN Macrophage metalloelastase (Gene Name=MMP12)

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