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1PPE

THE REFINED 2.0 ANGSTROMS 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

Functional Information from GO Data
ChainGOidnamespacecontents
E0004175molecular_functionendopeptidase activity
E0004252molecular_functionserine-type endopeptidase activity
E0005515molecular_functionprotein binding
E0005576cellular_componentextracellular region
E0005615cellular_componentextracellular space
E0006508biological_processproteolysis
E0007586biological_processdigestion
E0008233molecular_functionpeptidase activity
E0008236molecular_functionserine-type peptidase activity
E0016787molecular_functionhydrolase activity
E0046872molecular_functionmetal ion binding
E0097180cellular_componentserine protease inhibitor complex
E0097655molecular_functionserpin family protein binding
I0004866molecular_functionendopeptidase inhibitor activity
I0004867molecular_functionserine-type endopeptidase inhibitor activity
I0005576cellular_componentextracellular region
I0030414molecular_functionpeptidase inhibitor activity
Functional Information from PROSITE/UniProt
site_idPS00134
Number of Residues6
DetailsTRYPSIN_HIS Serine proteases, trypsin family, histidine active site. VSAAHC
ChainResidueDetails
EVAL53-CYS58

site_idPS00135
Number of Residues12
DetailsTRYPSIN_SER Serine proteases, trypsin family, serine active site. DScqGDSGGPVV
ChainResidueDetails
EASP189-VAL200

site_idPS00286
Number of Residues20
DetailsSQUASH_INHIBITOR Squash family of serine protease inhibitors signature. CPrilmeCkkDsDClaeCvC
ChainResidueDetails
ICYS3-CYS22

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues220
DetailsDomain: {"description":"Peptidase S1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00274","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues3
DetailsActive site: {"description":"Charge relay system"}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues7
DetailsBinding site: {}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues28
DetailsPeptide: {"description":"Trypsin inhibitor 1","featureId":"PRO_0000044376"}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues1
DetailsSite: {"description":"Reactive bond"}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1a0j
ChainResidueDetails
EASP102
EHIS57

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1a0j
ChainResidueDetails
ESER195
EGLY196

site_idCSA3
Number of Residues2
DetailsAnnotated By Reference To The Literature 1a0j
ChainResidueDetails
ESER195
EGLY193

site_idCSA4
Number of Residues3
DetailsAnnotated By Reference To The Literature 1a0j
ChainResidueDetails
EASP102
ESER195
EHIS57

site_idCSA5
Number of Residues4
DetailsAnnotated By Reference To The Literature 1a0j
ChainResidueDetails
EASP102
ESER195
EGLY193
EHIS57

site_idCSA6
Number of Residues4
DetailsAnnotated By Reference To The Literature 1a0j
ChainResidueDetails
EASP102
ESER195
EHIS57
EGLY196

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PDB entries from 2025-07-23

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