Structure of PDB 2stb Chain E Binding Site BS02

Receptor Information

>2stb Chain E (length=222) Species: 8030 (Salmo salar)

IVGGYECKPYSQPHQVSLNSGYHFCGGSLVNENWVVSAAHCYKSRVEVRL
GEHNIKVTEGSEQFISSSRVIRHPNYSSYNIDNDIMLIKLSKPATLNTYV
QPVALPTSCAPAGTMCTVSGWGNTMSSTADSNKLQCLNIPILSYSDCNNS
YPGMITNAMFCAGYLEGGKDSCQGDSGGPVVCNGELQGVVSWGYGCAEPG
NPGVYAKVCIFNDWLTSTMASY

Ligand information

• Ligand ID: CA
• InChI: InChI=1S/Ca/q+2
• InChIKey: BHPQYMZQTOCNFJ-UHFFFAOYSA-N
• SMILES:
  CACTVS 3.341: [Ca++]
  ACDLabs 10.04
  OpenEye OEToolkits 1.5.0: [Ca+2]
• Formula: Ca
• Name: CALCIUM ION
• DrugBank: DB14577
• PDB chain: 2stb Chain E Residue 700

Receptor-Ligand Complex Structure

Structure summary

• 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): E70 N72 V75 E77 E80
• Binding residue (residue number reindexed from 1): E52 N54 V57 E59 E62
• Annotation score: 4

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

External links

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