Structure of PDB 6n4t Chain A

Receptor sequence
>6n4tA (length=241) Species: 9606 (Homo sapiens) [Search protein sequence]
VVGGTDADEGEWPWQVSLHALGQGHICGASLISPNWLVSAAHCYIDDRGF
RYSDPTQWTAFLGLHDQSQRSAPGVQERRLKRIISHPFFNDFTFDYDIAL
LELEKPAEYSSMVRPICLPDASHVFPAGKAIWVTGWGHTQYGGTGALILQ
KGEIRVINQTTCENLLPQQITPRMMCVGFLSGGVDSCQGDSGGPLSSVEA
DGRIFQAGVVSWGDGCAQRNKPGVYTRLPLFRDWIKENTGV
3D structure
PDB6n4t Discovery and Development of TMPRSS6 Inhibitors Modulating Hepcidin Levels in Human Hepatocytes.
ChainA
Resolution1.945 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 MG A E24 M117 E9 M112
BS02 GSH A W29 R119 P120 C122 R206 I207 W14 R114 P115 C117 R203 I204
BS03 KD7 A H57 F99 Y146 Q175 D189 S190 C191 Q192 G193 D194 S195 W215 G216 G219 H42 F94 Y141 Q169 D185 S186 C187 Q188 G189 D190 S191 W212 G213 G215 PDBbind-CN: -logKd/Ki=8.09,IC50=8.1nM
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:6n4t, PDBe:6n4t, PDBj:6n4t
PDBsum6n4t
PubMed31543462
UniProtQ9Y5Y6|ST14_HUMAN Suppressor of tumorigenicity 14 protein (Gene Name=ST14)

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