Structure of PDB 2y6d Chain A

Receptor sequence
>2y6dA (length=159) Species: 9606 (Homo sapiens) [Search protein sequence]
GYSLFPNSPKWTSKVVTYRIVSYTRDLPHITVDRLVSKALNMWGKEIPLH
FRKVVWGTADIMIGFARGAHGDSYPFDGPGNTLAHAFAPGTGLGGDAHFD
EDERWTDGSSLGINFLYAATHELGHSLGMGHSSDPNAVMYPTYFKLSQDD
IKGIQKLYG
3D structure
PDB2y6d The Discovery of Mmp7 Inhibitors Exploiting a Novel Selectivity Trigger.
ChainA
Resolution1.6 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) H219 E220 H223 H229
Catalytic site (residue number reindexed from 1) H121 E122 H125 H131
Enzyme Commision number 3.4.24.23: matrilysin.
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 CA A D175 G176 G178 T180 D198 E201 D77 G78 G80 T82 D100 E103
BS02 CA A D158 G190 G192 D194 D60 G92 G94 D96
BS03 ZN A H168 D170 H183 H196 H70 D72 H85 H98
BS04 ZN A H219 H223 H229 H121 H125 H131
BS05 TQJ A Y172 L181 A182 H183 Y215 H219 E220 H223 H229 V236 P239 T240 Y241 Y74 L83 A84 H85 Y117 H121 E122 H125 H131 V138 P141 T142 Y143 PDBbind-CN: -logKd/Ki=7.10,IC50=79nM
BindingDB: Ki=79nM
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:2y6d, PDBe:2y6d, PDBj:2y6d
PDBsum2y6d
PubMed21520417
UniProtP09237|MMP7_HUMAN Matrilysin (Gene Name=MMP7)

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