Structure of PDB 4r0i Chain A

Receptor sequence
>4r0iA (length=241) Species: 9606 (Homo sapiens) [Search protein sequence]
VVGGTDADEGEWPWQVSLHALGQGHICGASLISPNWLVSAAHCYIDDRGF
RYSDPTQWTAFLGLHDQSQRSAPGVQERRLKRIISHPFFNDFTFDYDIAL
LELEKPAEYSSMVRPICLPDASHVFPAGKAIWVTGWGHTQYGGTGALILQ
KGEIRVINQTTCENLLPQQITPRMMCVGFLSGGVDSCQGDSGGPLSSVEA
DGRIFQAGVVSWGDGCAQRNKPGVYTRLPLFRDWIKENTGV
3D structure
PDB4r0i Discovery of O-(3-carbamimidoylphenyl)-l-serine amides as matriptase inhibitors using a fragment-linking approach
ChainA
Resolution1.9 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 W29 R119 P120 I121 C122 R206 I207 W14 R114 P115 I116 C117 R203 I204
BS02 3KM A D189 S190 C191 Q192 S195 V213 W215 G216 D217 G219 C220 D185 S186 C187 Q188 S191 V210 W212 G213 D214 G215 C216 MOAD: Ki=0.3uM
PDBbind-CN: -logKd/Ki=6.52,Ki=0.3uM
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:4r0i, PDBe:4r0i, PDBj:4r0i
PDBsum4r0i
PubMed25556099
UniProtQ9Y5Y6|ST14_HUMAN Suppressor of tumorigenicity 14 protein (Gene Name=ST14)

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