Structure of PDB 2sta Chain E Binding Site BS01

Receptor Information
>2sta Chain E (length=222) Species: 8030 (Salmo salar) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
IVGGYECKPYSQPHQVSLNSGYHFCGGSLVNENWVVSAAHCYKSRVEVRL
GEHNIKVTEGSEQFISSSRVIRHPNYSSYNIDNDIMLIKLSKPATLNTYV
QPVALPTSCAPAGTMCTVSGWGNTMSSTADSNKLQCLNIPILSYSDCNNS
YPGMITNAMFCAGYLEGGKDSCQGDSGGPVVCNGELQGVVSWGYGCAEPG
NPGVYAKVCIFNDWLTSTMASY
Ligand information
>2sta Chain I (length=29) Species: 3661 (Cucurbita maxima) [Search peptide sequence] [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
RVCPRILMECKKDSDCLAECVCLEHGYCG
Receptor-Ligand Complex Structure
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PDB2sta High-resolution structures of three new trypsin-squash-inhibitor complexes: a detailed comparison with other trypsins and their complexes.
Resolution1.8 Å
Binding residue
(original residue number in PDB)		F41 C42 H57 D189 S190 C191 Q192 G193 S195 S214 W215 G216 Y217
Binding residue
(residue number reindexed from 1)		F24 C25 H40 D170 S171 C172 Q173 G174 S176 S191 W192 G193 Y194
Enzymatic activity
Catalytic site (original residue number in PDB) D102 G193 S195 G196
Catalytic site (residue number reindexed from 1) D84 G174 S176 G177
Enzyme Commision number 3.4.21.4: trypsin.
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:2sta, PDBe:2sta, PDBj:2sta
PDBsum2sta
PubMed10089404
UniProtP35031|TRY1_SALSA Trypsin-1

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