Structure of PDB 1dpo Chain A Binding Site BS01

Receptor Information

>1dpo Chain A (length=223) Species: 10117 (Rattus rattus)

IVGGYTCQENSVPYQVSLNSGYHFCGGSLINDQWVVSAAHCYKSRIQVRL
GEHNINVLEGNEQFVNAAKIIKHPNFDRKTLNNDIMLIKLSSPVKLNARV
ATVALPSSCAPAGTQCLISGWGNTLSSGVNEPDLLQCLDAPLLPQADCEA
SYPGKITDNMVCVGFLEGGKDSCQGDCGGPVVCNGELQGIVSWGYGCALP
DNPGVYTKVCNYVDWIQDTIAAN

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: 1dpo Chain A Residue 246

Receptor-Ligand Complex Structure

Structure summary

• PDB: 1dpo 1.59 A structure of trypsin at 120 K: comparison of low temperature and room temperature structures.
• Resolution: 1.59 Å
• Binding residue (original residue number in PDB): E70 N72 V75 E80
• Binding residue (residue number reindexed from 1): E52 N54 V57 E62
• Annotation score: 4

Enzymatic activity

• Catalytic site (original residue number in PDB): H57 D102 Q192 G193 D194 C195 G196
• Catalytic site (residue number reindexed from 1): H40 D84 Q174 G175 D176 C177 G178
• Enzyme Commision number: 3.4.21.4: trypsin.

Gene Ontology

Molecular Function

• GO:0004252 serine-type endopeptidase activity
• GO:0005509 calcium ion binding
• GO:0005515 protein binding
• GO:0008236 serine-type peptidase activity
• GO:0046872 metal ion binding

Biological Process

• GO:0006508 proteolysis
• GO:0007584 response to nutrient
• GO:0007586 digestion
• GO:0030574 collagen catabolic process

Cellular Component

• GO:0005576 extracellular region
• GO:0005615 extracellular space

External links

• PDB: RCSB:1dpo, PDBe:1dpo, PDBj:1dpo
• PDBsum: 1dpo
• PubMed: 1881877
• UniProt: P00763|TRY2_RAT Anionic trypsin-2 (Gene Name=Prss2)