Structure of PDB 2stb Chain E

Receptor sequence
>2stbE (length=222) Species: 8030 (Salmo salar) [Search protein sequence]
IVGGYECKPYSQPHQVSLNSGYHFCGGSLVNENWVVSAAHCYKSRVEVRL
GEHNIKVTEGSEQFISSSRVIRHPNYSSYNIDNDIMLIKLSKPATLNTYV
QPVALPTSCAPAGTMCTVSGWGNTMSSTADSNKLQCLNIPILSYSDCNNS
YPGMITNAMFCAGYLEGGKDSCQGDSGGPVVCNGELQGVVSWGYGCAEPG
NPGVYAKVCIFNDWLTSTMASY
3D structure
PDB2stb High-resolution structures of three new trypsin-squash-inhibitor complexes: a detailed comparison with other trypsins and their complexes.
ChainE
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) D102 G193 S195 G196
Catalytic site (residue number reindexed from 1) D84 G174 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 E Y39 F41 C42 H57 S190 C191 Q192 G193 S195 S214 W215 G216 Y217 Y22 F24 C25 H40 S171 C172 Q173 G174 S176 S191 W192 G193 Y194
BS02 CA E E70 N72 V75 E77 E80 E52 N54 V57 E59 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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Biological Process
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Cellular Component
External links
PDB RCSB:2stb, PDBe:2stb, PDBj:2stb
PDBsum2stb
PubMed10089404
UniProtP35031|TRY1_SALSA Trypsin-1

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