Structure of PDB 2stb Chain E Binding Site BS01

Receptor Information

>2stb 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

>2stb Chain I (length=29) Species: 3663 (Cucurbita pepo) [Search peptide sequence] [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]

RVCPKILMECKKDSDCLAECICLEHGYCG

Receptor-Ligand Complex Structure

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Structure summary

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PDB	2stb High-resolution structures of three new trypsin-squash-inhibitor complexes: a detailed comparison with other trypsins and their complexes.
Resolution	1.8 Å
Binding residue (original residue number in PDB)	Y39 F41 C42 H57 S190 C191 Q192 G193 S195 S214 W215 G216 Y217
Binding residue (residue number reindexed from 1)	Y22 F24 C25 H40 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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Cellular Component

External links

PDB	RCSB:2stb, PDBe:2stb, PDBj:2stb
PDBsum	2stb
PubMed	10089404
UniProt	P35031\|TRY1_SALSA Trypsin-1

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