Structure of PDB 4o97 Chain A

Receptor sequence
>4o97A (length=241) Species: 9606 (Homo sapiens) [Search protein sequence]
VVGGTDADEGEWPWQVSLHALGQGHICGASLISPNWLVSAAHCYIDDRGF
RYSDPTQWTAFLGLHDQSQRSAPGVQERRLKRIISHPFFNDFTFDYDIAL
LELEKPAEYSSMVRPICLPDASHVFPAGKAIWVTGWGHTQYGGTGALILQ
KGEIRVINQTTCENLLPQQITPRMMCVGFLSGGVDSCQGDSGGPLSSVEA
DGRIFQAGVVSWGDGCAQRNKPGVYTRLPLFRDWIKENTGV
3D structure
PDB4o97 Structure-guided discovery of 1,3,5 tri-substituted benzenes as potent and selective matriptase inhibitors exhibiting in vivo antitumor efficacy.
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 peptide A E26 W29 R119 P120 C122 R206 I207 E11 W14 R114 P115 C117 R203 I204
BS02 NTX A T98 F99 Q175 D189 S190 C191 Q192 S195 V213 W215 G216 T93 F94 Q169 D185 S186 C187 Q188 S191 V210 W212 G213 MOAD: Ki=3nM
PDBbind-CN: -logKd/Ki=8.52,Ki=3nM
BindingDB: Ki=3.0nM
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:4o97, PDBe:4o97, PDBj:4o97
PDBsum4o97
PubMed24794746
UniProtQ9Y5Y6|ST14_HUMAN Suppressor of tumorigenicity 14 protein (Gene Name=ST14)

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