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 | 0008233 | molecular_function | peptidase activity |
| E | 0008236 | molecular_function | serine-type peptidase activity |
| E | 0016787 | molecular_function | hydrolase 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 | 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 | 0048240 | biological_process | sperm capacitation |
| I | 0060046 | biological_process | regulation of acrosome reaction |
| I | 0070062 | cellular_component | extracellular exosome |
| 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 | 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 |
| site_id | PS00282 |
| Number of Residues | 23 |
| Details | KAZAL_1 Kazal serine protease inhibitors family signature. CtyeyRpvCgTdgdtYpneCvl.C |
| Chain | Residue | Details |
| I | CYS16-CYS38 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | Propeptide: {"featureId":"PRO_0000027625"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | Propeptide: {"featureId":"PRO_0000027627"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 227 |
| Details | Domain: {"description":"Peptidase S1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00274","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 3 |
| Details | Active site: {"description":"Charge relay system"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 53 |
| Details | Domain: {"description":"Kazal-like","evidences":[{"source":"PROSITE-ProRule","id":"PRU00798","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 1 |
| Details | Site: {"description":"Reactive bond for trypsin","evidences":[{"source":"UniProtKB","id":"P09036","evidenceCode":"ECO:0000250"},{"source":"PROSITE-ProRule","id":"PRU00798","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 1 |
| Details | Site: {"description":"Necessary for sperm binding","evidences":[{"source":"UniProtKB","id":"P09036","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
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 |
