Structure of PDB 2gv7 Chain A

Receptor sequence
>2gv7A (length=241) Species: 9606 (Homo sapiens) [Search protein sequence]
VVGGTDADEGEWPWQVSLHALGQGHICGASLISPNWLVSAAHCYIDDRGF
RYSDPTQWTAFLGLHDQSQRSAPGVQERRLKRIISHPFFNDFTFDYDIAL
LELEKPAEYSSMVRPICLPDASHVFPAGKAIWVTGWGHTQYGGTGALILQ
KGEIRVINQTTCENLLPQQITPRMMCVGFLSGGVDSCQGDSGGPLSSVEA
DGRIFQAGVVSWGDGCAQRNKPGVYTRLPLFRDWIKENTGV
3D structure
PDB2gv7 Secondary Amides of Sulfonylated 3-Amidinophenylalanine. New Potent and Selective Inhibitors of Matriptase.
ChainA
Resolution2.2 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) H57 D102 Q192 G193 D194 S195 G196
Catalytic site (residue number reindexed from 1) H42 D97 Q188 G189 D190 S191 G192
Enzyme Commision number 3.4.21.109: matriptase.
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 672 A H57 I60 Y60G F99 D189 S190 C191 Q192 S195 V213 S214 W215 G216 G219 C220 H42 I45 Y52 F94 D185 S186 C187 Q188 S191 V210 S211 W212 G213 G215 C216 MOAD: Ki=0.014uM
PDBbind-CN: -logKd/Ki=7.85,Ki=14nM
BindingDB: Ki=14nM
Gene Ontology
Molecular Function
GO:0004252 serine-type endopeptidase activity
Biological Process
GO:0006508 proteolysis

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Molecular Function
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Biological Process
External links
PDB RCSB:2gv7, PDBe:2gv7, PDBj:2gv7
PDBsum2gv7
PubMed16821772
UniProtQ9Y5Y6|ST14_HUMAN Suppressor of tumorigenicity 14 protein (Gene Name=ST14)

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