5TO3
Crystal structure of thrombin mutant W215A/E217A fused to EGF456 of thrombomodulin via a 31-residue linker and bound to PPACK
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 | 0004888 | molecular_function | transmembrane signaling receptor activity |
| B | 0005509 | molecular_function | calcium ion binding |
| B | 0006508 | biological_process | proteolysis |
| B | 0016020 | cellular_component | membrane |
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 |
| B | CYS437-CYS448 |
| site_id | PS00134 |
| Number of Residues | 6 |
| Details | TRYPSIN_HIS Serine proteases, trypsin family, histidine active site. LTAAHC |
| Chain | Residue | Details |
| B | LEU54-CYS59 |
| site_id | PS00135 |
| Number of Residues | 12 |
| Details | TRYPSIN_SER Serine proteases, trypsin family, serine active site. DAceGDSGGPFV |
| Chain | Residue | Details |
| B | ASP214-VAL225 |
| site_id | PS01186 |
| Number of Residues | 15 |
| Details | EGF_2 EGF-like domain signature 2. CeCpeGYilddgfi.C |
| Chain | Residue | Details |
| B | CYS407-CYS421 |
| site_id | PS01187 |
| Number of Residues | 24 |
| Details | EGF_CA Calcium-binding EGF-like domain signature. DiDECenggf.........Csgv....ChNlpgtFeC |
| Chain | Residue | Details |
| B | ASP423-CYS446 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 22 |
| Details | Region: {"description":"High affinity receptor-binding region which is also known as the TP508 peptide"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 3 |
| Details | Active site: {"description":"Charge relay system"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| 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 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 40 |
| Details | Domain: {"description":"EGF-like 4","evidences":[{"source":"PROSITE-ProRule","id":"PRU00076","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 36 |
| Details | Domain: {"description":"EGF-like 5","evidences":[{"source":"PROSITE-ProRule","id":"PRU00076","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 2 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
