1DX5
Crystal structure of the thrombin-thrombomodulin complex
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004252 | molecular_function | serine-type endopeptidase activity |
| A | 0005576 | cellular_component | extracellular region |
| A | 0006508 | biological_process | proteolysis |
| A | 0007596 | biological_process | blood coagulation |
| B | 0004252 | molecular_function | serine-type endopeptidase activity |
| B | 0005576 | cellular_component | extracellular region |
| B | 0006508 | biological_process | proteolysis |
| B | 0007596 | biological_process | blood coagulation |
| C | 0004252 | molecular_function | serine-type endopeptidase activity |
| C | 0005576 | cellular_component | extracellular region |
| C | 0006508 | biological_process | proteolysis |
| C | 0007596 | biological_process | blood coagulation |
| D | 0004252 | molecular_function | serine-type endopeptidase activity |
| D | 0005576 | cellular_component | extracellular region |
| D | 0006508 | biological_process | proteolysis |
| D | 0007596 | biological_process | blood coagulation |
| I | 0004888 | molecular_function | transmembrane signaling receptor activity |
| I | 0005509 | molecular_function | calcium ion binding |
| I | 0016020 | cellular_component | membrane |
| J | 0004888 | molecular_function | transmembrane signaling receptor activity |
| J | 0005509 | molecular_function | calcium ion binding |
| J | 0016020 | cellular_component | membrane |
| K | 0004888 | molecular_function | transmembrane signaling receptor activity |
| K | 0005509 | molecular_function | calcium ion binding |
| K | 0016020 | cellular_component | membrane |
| L | 0004888 | molecular_function | transmembrane signaling receptor activity |
| L | 0005509 | molecular_function | calcium ion binding |
| L | 0016020 | cellular_component | membrane |
| M | 0004252 | molecular_function | serine-type endopeptidase activity |
| M | 0005509 | molecular_function | calcium ion binding |
| M | 0006508 | biological_process | proteolysis |
| M | 0007596 | biological_process | blood coagulation |
| N | 0004252 | molecular_function | serine-type endopeptidase activity |
| N | 0005509 | molecular_function | calcium ion binding |
| N | 0006508 | biological_process | proteolysis |
| N | 0007596 | biological_process | blood coagulation |
| O | 0004252 | molecular_function | serine-type endopeptidase activity |
| O | 0005509 | molecular_function | calcium ion binding |
| O | 0006508 | biological_process | proteolysis |
| O | 0007596 | biological_process | blood coagulation |
| P | 0004252 | molecular_function | serine-type endopeptidase activity |
| P | 0005509 | molecular_function | calcium ion binding |
| P | 0006508 | biological_process | proteolysis |
| P | 0007596 | biological_process | blood coagulation |
Functional Information from PROSITE/UniProt
| site_id | PS00010 |
| Number of Residues | 12 |
| Details | ASX_HYDROXYL Aspartic acid and asparagine hydroxylation site. ChNlpgtFeCiC |
| Chain | Residue | Details |
| I | CYS437-CYS448 |
| site_id | PS00134 |
| Number of Residues | 6 |
| Details | TRYPSIN_HIS Serine proteases, trypsin family, histidine active site. LTAAHC |
| Chain | Residue | Details |
| M | LEU53-CYS58 |
| site_id | PS00135 |
| Number of Residues | 12 |
| Details | TRYPSIN_SER Serine proteases, trypsin family, serine active site. DAceGDSGGPFV |
| Chain | Residue | Details |
| M | ASP189-VAL200 |
| site_id | PS01186 |
| Number of Residues | 15 |
| Details | EGF_2 EGF-like domain signature 2. CeCpeGYilddgfi.C |
| Chain | Residue | Details |
| I | CYS407-CYS421 |
| site_id | PS01187 |
| Number of Residues | 24 |
| Details | EGF_CA Calcium-binding EGF-like domain signature. DiDECenggf.........Csgv....ChNlpgtFeC |
| Chain | Residue | Details |
| I | ASP423-CYS446 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 160 |
| Details | Domain: {"description":"EGF-like 4","evidences":[{"source":"PROSITE-ProRule","id":"PRU00076","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 144 |
| Details | Domain: {"description":"EGF-like 5","evidences":[{"source":"PROSITE-ProRule","id":"PRU00076","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 8 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1016 |
| Details | Domain: {"description":"Peptidase S1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00274","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 88 |
| Details | Region: {"description":"High affinity receptor-binding region which is also known as the TP508 peptide"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 12 |
| Details | Active site: {"description":"Charge relay system"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 4 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) (complex) asparagine","evidences":[{"source":"PubMed","id":"16335952","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19139490","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19159218","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19838169","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"873923","evidenceCode":"ECO:0000269"}]} |
| 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 |
| M | ASP102 | |
| M | SER195 | |
| M | GLY193 | |
| M | HIS57 |
| site_id | CSA10 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1a0j |
| Chain | Residue | Details |
| N | ASP102 | |
| N | SER195 | |
| N | HIS57 |
| site_id | CSA11 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1a0j |
| Chain | Residue | Details |
| O | ASP102 | |
| O | SER195 | |
| O | HIS57 |
| site_id | CSA12 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1a0j |
| Chain | Residue | Details |
| P | ASP102 | |
| P | SER195 | |
| P | HIS57 |
| site_id | CSA2 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1a0j |
| Chain | Residue | Details |
| N | ASP102 | |
| N | SER195 | |
| N | GLY193 | |
| N | HIS57 |
| site_id | CSA3 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1a0j |
| Chain | Residue | Details |
| O | ASP102 | |
| O | SER195 | |
| O | GLY193 | |
| O | HIS57 |
| site_id | CSA4 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1a0j |
| Chain | Residue | Details |
| P | ASP102 | |
| P | SER195 | |
| P | GLY193 | |
| P | HIS57 |
| site_id | CSA5 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1a0j |
| Chain | Residue | Details |
| M | ASP102 | |
| M | SER195 | |
| M | HIS57 | |
| M | GLY196 |
| site_id | CSA6 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1a0j |
| Chain | Residue | Details |
| N | ASP102 | |
| N | SER195 | |
| N | HIS57 | |
| N | GLY196 |
| site_id | CSA7 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1a0j |
| Chain | Residue | Details |
| O | ASP102 | |
| O | SER195 | |
| O | HIS57 | |
| O | GLY196 |
| site_id | CSA8 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1a0j |
| Chain | Residue | Details |
| P | ASP102 | |
| P | SER195 | |
| P | HIS57 | |
| P | GLY196 |
| site_id | CSA9 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1a0j |
| Chain | Residue | Details |
| M | ASP102 | |
| M | SER195 | |
| M | HIS57 |
