Structure of PDB 1dpo Chain A

Receptor sequence

>1dpoA (length=223) Species: 10117 (Rattus rattus)

IVGGYTCQENSVPYQVSLNSGYHFCGGSLINDQWVVSAAHCYKSRIQVRL
GEHNINVLEGNEQFVNAAKIIKHPNFDRKTLNNDIMLIKLSSPVKLNARV
ATVALPSSCAPAGTQCLISGWGNTLSSGVNEPDLLQCLDAPLLPQADCEA
SYPGKITDNMVCVGFLEGGKDSCQGDCGGPVVCNGELQGIVSWGYGCALP
DNPGVYTKVCNYVDWIQDTIAAN

3D structure

• PDB: 1dpo 1.59 A structure of trypsin at 120 K: comparison of low temperature and room temperature structures.
• Chain: A
• Resolution: 1.59 Å

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.

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	CA	A	E70 N72 V75 E80	E52 N54 V57 E62
BS02	SO4	A	N100 N179	N82 N159
BS03	SO4	A	A132 P164 Q165	A112 P144 Q145
BS04	BEN	A	D189 S190 C191 Q192 C195 W215 G216 G219	D171 S172 C173 Q174 C177 W193 G194 G196
BS05	BEN	A	A221 P222	A198 P200

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)