1MKX
THE CO-CRYSTAL STRUCTURE OF UNLIGANDED BOVINE ALPHA-THROMBIN AND PRETHROMBIN-2: MOVEMENT OF THE YPPW SEGMENT AND ACTIVE SITE RESIDUES UPON LIGAND BINDING
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| H | 0004252 | molecular_function | serine-type endopeptidase activity |
| H | 0005509 | molecular_function | calcium ion binding |
| H | 0006508 | biological_process | proteolysis |
| H | 0007596 | biological_process | blood coagulation |
| K | 0004252 | molecular_function | serine-type endopeptidase activity |
| K | 0005509 | molecular_function | calcium ion binding |
| K | 0005576 | cellular_component | extracellular region |
| K | 0006508 | biological_process | proteolysis |
| K | 0007596 | biological_process | blood coagulation |
| L | 0004252 | molecular_function | serine-type endopeptidase activity |
| L | 0005576 | cellular_component | extracellular region |
| L | 0006508 | biological_process | proteolysis |
| L | 0007596 | biological_process | blood coagulation |
Functional Information from PROSITE/UniProt
| site_id | PS00134 |
| Number of Residues | 6 |
| Details | TRYPSIN_HIS Serine proteases, trypsin family, histidine active site. LTAAHC |
| Chain | Residue | Details |
| H | LEU53-CYS58 | |
| K | LEU53-CYS58 |
| site_id | PS00135 |
| Number of Residues | 12 |
| Details | TRYPSIN_SER Serine proteases, trypsin family, serine active site. DAceGDSGGPFV |
| Chain | Residue | Details |
| H | ASP189-VAL200 | |
| K | ASP189-VAL200 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 508 |
| Details | Domain: {"description":"Peptidase S1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00274","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 44 |
| Details | Region: {"description":"High affinity receptor-binding region which is also known as the TP508 peptide","evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 6 |
| Details | Active site: {"description":"Charge relay system"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"book","publicationDate":"1975","firstPage":"25","lastPage":"46","publisher":"Leiden University Press","address":"Leiden","bookName":"Boerhaave symposium on prothrombin and related coagulation factors","editors":["Hemker H.C.","Veltkamp J.J."],"authors":["Magnusson S.","Sottrup-Jensen L.","Petersen T.E.","Claeys H."]}}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| Details | Site: {"description":"Cleavage; by factor Xa","evidences":[{"source":"UniProtKB","id":"P00734","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1a0j |
| Chain | Residue | Details |
| K | ASP102 | |
| K | SER195 | |
| K | GLY193 | |
| K | HIS57 |
| site_id | CSA2 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1a0j |
| Chain | Residue | Details |
| H | ASP102 | |
| H | SER195 | |
| H | GLY193 | |
| H | HIS57 |
| site_id | CSA3 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1a0j |
| Chain | Residue | Details |
| K | ASP102 | |
| K | SER195 | |
| K | HIS57 | |
| K | GLY196 |
| site_id | CSA4 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1a0j |
| Chain | Residue | Details |
| H | ASP102 | |
| H | SER195 | |
| H | HIS57 | |
| H | GLY196 |
| site_id | CSA5 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1a0j |
| Chain | Residue | Details |
| K | ASP102 | |
| K | SER195 | |
| K | HIS57 |
| site_id | CSA6 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1a0j |
| Chain | Residue | Details |
| H | ASP102 | |
| H | SER195 | |
| H | HIS57 |






