Structure of PDB 5xwj Chain B

Receptor sequence
>5xwjB (length=222) Species: 9823 (Sus scrofa) [Search protein sequence]
IVGGYTCAANSIPYQVSLNSGSHFCGGSLINSQWVVSAAHCYKSRIQVRL
GEHNIDVLEGNEQFINAAKIITHPNFNGNTLDNDIMLIKLSSPATLNSRV
ATVSLPRSCAAAGTECLISGWGNTKSGSSYPSLLQCLKAPVLSDSSCKSS
YPGQITGNMICVGFLEGGKDSCQGDSGGPVVCNGQLQGIVSWGYGCAQKN
KPGVYTKVCNYVNWIQQTIAAN
3D structure
PDB5xwj Tripeptides derived from reactive centre loop of potato type II protease inhibitors preferentially inhibit midgut proteases of Helicoverpa armigera.
ChainB
Resolution1.8 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) H48 D92 Q182 G183 D184 S185 G186
Catalytic site (residue number reindexed from 1) H40 D84 Q173 G174 D175 S176 G177
Enzyme Commision number 3.4.21.4: trypsin.
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 B H48 D179 S180 C181 Q182 G183 S185 S200 W201 G202 G204 H40 D170 S171 C172 Q173 G174 S176 S191 W192 G193 G195
BS02 CA B E60 N62 V65 E70 E52 N54 V57 E62
Gene Ontology
Molecular Function
GO:0004252 serine-type endopeptidase activity
GO:0008236 serine-type peptidase activity
GO:0046872 metal ion binding
Biological Process
GO:0006508 proteolysis
GO:0007586 digestion
Cellular Component
GO:0005576 extracellular region
GO:0005615 extracellular space

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:5xwj, PDBe:5xwj, PDBj:5xwj
PDBsum5xwj
PubMed29486250
UniProtP00761|TRYP_PIG Trypsin

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