Structure of PDB 4ilw Chain D

Receptor sequence
>4ilwD (length=159) Species: 9606 (Homo sapiens) [Search protein sequence]
MPKWRKTHLTYRIVNYTPDLPRDAVDSAIEKALKVWEEVTPLTFSRLYEG
EADIMISFAVKEHGDFYSFDGPGHSLAHAYPPGPGLYGDIHFDDDEKWTE
DASGTNLFLVAAHELGHSLGLFHSANTEALMYPLYNSFTELAQFRLSQDD
VNGIQSLYG
3D structure
PDB4ilw Matrix Metalloproteinase-10/TIMP-2 Structure and Analyses Define Conserved Core Interactions and Diverse Exosite Interactions in MMP/TIMP Complexes.
ChainD
Resolution2.103 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) H217 E218 H221 H227
Catalytic site (residue number reindexed from 1) H113 E114 H117 H123
Enzyme Commision number 3.4.24.22: stromelysin 2.
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 D H217 H221 H227 H113 H117 H123
BS02 ZN D H167 D169 H182 H195 H63 D65 H78 H91
BS03 CA D D174 G175 G177 S179 D197 E200 D70 G71 G73 S75 D93 E96
BS04 CA D D157 G189 Y191 D193 D53 G85 Y87 D89
BS05 CA D D123 D198 E200 D19 D94 E96
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:4ilw, PDBe:4ilw, PDBj:4ilw
PDBsum4ilw
PubMed24073280
UniProtP09238|MMP10_HUMAN Stromelysin-2 (Gene Name=MMP10)

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