Structure of PDB 1ppe Chain E Binding Site BS01

Receptor Information

>1ppe Chain E (length=223) Species: 9913 (Bos taurus)

IVGGYTCGANTVPYQVSLNSGYHFCGGSLINSQWVVSAAHCYKSGIQVRL
GEDNINVVEGNEQFISASKSIVHPSYNSNTLNNDIMLIKLKSAASLNSRV
ASISLPTSCASAGTQCLISGWGNTKSSGTSYPDVLKCLKAPILSDSSCKS
AYPGQITSNMFCAGYLEGGKDSCQGDSGGPVVCSGKLQGIVSWGSGCAQK
NKPGVYTKVCNYVSWIKQTIASN

Ligand information

>1ppe Chain I (length=29) Species: 3661 (Cucurbita maxima)

RVCPRILMECKKDSDCLAECVCLEHGYCG

Receptor-Ligand Complex Structure

Structure summary

• PDB: 1ppe The refined 2.0 A X-ray crystal structure of the complex formed between bovine beta-trypsin and CMTI-I, a trypsin inhibitor from squash seeds (Cucurbita maxima). Topological similarity of the squash seed inhibitors with the carboxypeptidase A inhibitor from potatoes
• Resolution: 2.0 Å
• Binding residue (original residue number in PDB): Y39 F41 H57 L99 Y151 D189 S190 Q192 G193 S195 S214 W215 G216 S217
• Binding residue (residue number reindexed from 1): Y22 F24 H40 L81 Y131 D171 S172 Q174 G175 S177 S192 W193 G194 S195

Enzymatic activity

• Catalytic site (original residue number in PDB): G193 S195 G196
• Catalytic site (residue number reindexed from 1): G175 S177 G178
• Enzyme Commision number: 3.4.21.4: trypsin.

Gene Ontology

Molecular Function

• GO:0004175 endopeptidase activity
• GO:0004252 serine-type endopeptidase activity
• GO:0005515 protein binding
• GO:0008236 serine-type peptidase activity
• GO:0046872 metal ion binding
• GO:0097655 serpin family protein binding

Biological Process

• GO:0006508 proteolysis
• GO:0007586 digestion

Cellular Component

• GO:0005576 extracellular region
• GO:0005615 extracellular space
• GO:0097180 serine protease inhibitor complex

External links

• PDB: RCSB:1ppe, PDBe:1ppe, PDBj:1ppe
• PDBsum: 1ppe
• PubMed: 2914611
• UniProt: P00760|TRY1_BOVIN Serine protease 1 (Gene Name=PRSS1)