Structure of PDB 3ljg Chain A

Receptor sequence
>3ljgA (length=159) Species: 9606 (Homo sapiens) [Search protein sequence]
MGPVWRKHYITYRINNYTPDMNREDVDYAIRKAFQVWSNVTPLKFSKINT
GMADILVVFARGAHGDDHAFDGKGGILAHAFGPGSGIGGDAHFDEDEFWT
THSGGTNLFLTAVHEIGHSLGLGHSSDPKAVMFPTYKYVDINTFRLSADD
IRGIQSLYG
3D structure
PDB3ljg Insights from selective non-phosphinic inhibitors of MMP-12 tailored to fit with an S1' loop canonical conformation.
ChainA
Resolution1.313 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) H114 E115 H118 H124
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 H114 H118 H124
BS02 ZN A H168 D170 H183 H196 H64 D66 H79 H92
BS03 CA A D158 G190 G192 D194 D54 G86 G88 D90
BS04 CA A D124 E199 E201 D20 E95 E97
BS05 CA A D175 G176 G178 I180 D198 E201 D71 G72 G74 I76 D94 E97
BS06 EEF A G179 L181 T215 H218 V235 F237 P238 T239 Y240 G75 L77 T111 H114 V131 F133 P134 T135 Y136 MOAD: Ki=18.6nM
PDBbind-CN: -logKd/Ki=7.73,Ki=18.6nM
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:3ljg, PDBe:3ljg, PDBj:3ljg
PDBsum3ljg
PubMed20817735
UniProtP39900|MMP12_HUMAN Macrophage metalloelastase (Gene Name=MMP12)

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