1CGI
THREE-DIMENSIONAL STRUCTURE OF THE COMPLEXES BETWEEN BOVINE CHYMOTRYPSINOGEN*A AND TWO RECOMBINANT VARIANTS OF HUMAN PANCREATIC SECRETORY TRYPSIN INHIBITOR (KAZAL-TYPE)
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| E | 0004252 | molecular_function | serine-type endopeptidase activity |
| E | 0005515 | molecular_function | protein binding |
| E | 0005576 | cellular_component | extracellular region |
| E | 0006508 | biological_process | proteolysis |
| E | 0007586 | biological_process | digestion |
| E | 0008236 | molecular_function | serine-type peptidase activity |
| E | 0097180 | cellular_component | serine protease inhibitor complex |
| E | 0097655 | molecular_function | serpin family protein binding |
| I | 0004866 | molecular_function | endopeptidase inhibitor activity |
| I | 0004867 | molecular_function | serine-type endopeptidase inhibitor activity |
| I | 0005515 | molecular_function | protein binding |
| I | 0005576 | cellular_component | extracellular region |
| I | 0005615 | cellular_component | extracellular space |
| I | 0007204 | biological_process | positive regulation of cytosolic calcium ion concentration |
| I | 0007263 | biological_process | nitric oxide mediated signal transduction |
| I | 0010751 | biological_process | negative regulation of nitric oxide mediated signal transduction |
| I | 0030414 | molecular_function | peptidase inhibitor activity |
| I | 0031667 | biological_process | response to nutrient levels |
| I | 0045471 | biological_process | response to ethanol |
| I | 0048240 | biological_process | sperm capacitation |
| I | 0050679 | biological_process | positive regulation of epithelial cell proliferation |
| I | 0050732 | biological_process | negative regulation of peptidyl-tyrosine phosphorylation |
| I | 0060046 | biological_process | regulation of acrosome reaction |
| I | 0070062 | cellular_component | extracellular exosome |
| I | 0071375 | biological_process | cellular response to peptide hormone stimulus |
| I | 0090187 | biological_process | positive regulation of pancreatic juice secretion |
| I | 0090277 | biological_process | positive regulation of peptide hormone secretion |
| I | 0090281 | biological_process | negative regulation of calcium ion import |
| I | 2001256 | biological_process | regulation of store-operated calcium entry |
Functional Information from PROSITE/UniProt
| site_id | PS00282 |
| Number of Residues | 23 |
| Details | KAZAL_1 Kazal serine protease inhibitors family signature. CtyeyRpvCgTdgdtYpneCvl.C |
| Chain | Residue | Details |
| I | CYS16-CYS38 |
| site_id | PS00134 |
| Number of Residues | 6 |
| Details | TRYPSIN_HIS Serine proteases, trypsin family, histidine active site. VTAAHC |
| Chain | Residue | Details |
| E | VAL53-CYS58 |
| site_id | PS00135 |
| Number of Residues | 12 |
| Details | TRYPSIN_SER Serine proteases, trypsin family, serine active site. SScmGDSGGPLV |
| Chain | Residue | Details |
| E | SER189-VAL200 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | SITE: Reactive bond for trypsin => ECO:0000250|UniProtKB:P09036, ECO:0000255|PROSITE-ProRule:PRU00798 |
| Chain | Residue | Details |
| I | TYR18 | |
| E | ASP102 | |
| E | SER195 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | SITE: Necessary for sperm binding => ECO:0000250|UniProtKB:P09036 |
| Chain | Residue | Details |
| I | TYR20 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1a0j |
| Chain | Residue | Details |
| E | ASP102 | |
| E | HIS57 |
| site_id | CSA2 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1a0j |
| Chain | Residue | Details |
| E | SER195 | |
| E | GLY196 |
| site_id | CSA3 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1a0j |
| Chain | Residue | Details |
| E | SER195 | |
| E | GLY193 |
| site_id | CSA4 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1a0j |
| Chain | Residue | Details |
| E | ASP102 | |
| E | SER195 | |
| E | HIS57 |
| site_id | CSA5 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1a0j |
| Chain | Residue | Details |
| E | ASP102 | |
| E | SER195 | |
| E | HIS57 | |
| E | GLY196 |
| site_id | CSA6 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1a0j |
| Chain | Residue | Details |
| E | ASP102 | |
| E | SER195 | |
| E | GLY193 | |
| E | HIS57 |
| site_id | MCSA1 |
| Number of Residues | 5 |
| Details | M-CSA 387 |
| Chain | Residue | Details |
| E | HIS57 | electrostatic stabiliser, proton shuttle (general acid/base) |
| E | ASP102 | modifies pKa |
| E | GLY193 | electrostatic stabiliser |
| E | SER195 | covalent catalysis |
| E | GLY196 | electrostatic stabiliser |
