1E0F
Crystal structure of the human alpha-thrombin-haemadin complex: an exosite II-binding inhibitor
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 | 0005509 | molecular_function | calcium ion binding |
| D | 0006508 | biological_process | proteolysis |
| D | 0007596 | biological_process | blood coagulation |
| E | 0004252 | molecular_function | serine-type endopeptidase activity |
| E | 0005509 | molecular_function | calcium ion binding |
| E | 0006508 | biological_process | proteolysis |
| E | 0007596 | biological_process | blood coagulation |
| F | 0004252 | molecular_function | serine-type endopeptidase activity |
| F | 0005509 | molecular_function | calcium ion binding |
| F | 0006508 | biological_process | proteolysis |
| F | 0007596 | biological_process | blood coagulation |
| I | 0004857 | molecular_function | enzyme inhibitor activity |
| I | 0004867 | molecular_function | serine-type endopeptidase inhibitor activity |
| I | 0005576 | cellular_component | extracellular region |
| I | 0030414 | molecular_function | peptidase inhibitor activity |
| J | 0004857 | molecular_function | enzyme inhibitor activity |
| J | 0004867 | molecular_function | serine-type endopeptidase inhibitor activity |
| J | 0005576 | cellular_component | extracellular region |
| J | 0030414 | molecular_function | peptidase inhibitor activity |
| K | 0004857 | molecular_function | enzyme inhibitor activity |
| K | 0004867 | molecular_function | serine-type endopeptidase inhibitor activity |
| K | 0005576 | cellular_component | extracellular region |
| K | 0030414 | molecular_function | peptidase inhibitor activity |
Functional Information from PROSITE/UniProt
| site_id | PS00010 |
| Number of Residues | 12 |
| Details | ASX_HYDROXYL Aspartic acid and asparagine hydroxylation site. CpDgevgYtCdC |
| Chain | Residue | Details |
| I | CYS10-CYS21 |
| site_id | PS00134 |
| Number of Residues | 6 |
| Details | TRYPSIN_HIS Serine proteases, trypsin family, histidine active site. LTAAHC |
| Chain | Residue | Details |
| D | LEU53-CYS58 |
| site_id | PS00135 |
| Number of Residues | 12 |
| Details | TRYPSIN_SER Serine proteases, trypsin family, serine active site. DAceGDSGGPFV |
| Chain | Residue | Details |
| D | ASP189-VAL200 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 9 |
| Details | ACT_SITE: Charge relay system |
| Chain | Residue | Details |
| D | HIS57 | |
| D | ASP102 | |
| D | SER195 | |
| E | HIS57 | |
| E | ASP102 | |
| E | SER195 | |
| F | HIS57 | |
| F | ASP102 | |
| F | SER195 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 3 |
| Details | CARBOHYD: N-linked (GlcNAc...) (complex) asparagine => ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19139490, ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:19838169, ECO:0000269|PubMed:873923 |
| Chain | Residue | Details |
| D | ASN60 | |
| E | ASN60 | |
| F | ASN60 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1a0j |
| Chain | Residue | Details |
| D | ASP102 | |
| D | SER195 | |
| D | GLY193 | |
| D | HIS57 |
| site_id | CSA2 |
| 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 | CSA3 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1a0j |
| Chain | Residue | Details |
| F | ASP102 | |
| F | SER195 | |
| F | GLY193 | |
| F | HIS57 |
| site_id | CSA4 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1a0j |
| Chain | Residue | Details |
| D | ASP102 | |
| D | SER195 | |
| D | HIS57 | |
| D | GLY196 |
| 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 |
| F | ASP102 | |
| F | SER195 | |
| F | HIS57 | |
| F | GLY196 |
| site_id | CSA7 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1a0j |
| Chain | Residue | Details |
| D | ASP102 | |
| D | SER195 | |
| D | HIS57 |
| site_id | CSA8 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1a0j |
| Chain | Residue | Details |
| E | ASP102 | |
| E | SER195 | |
| E | HIS57 |
| site_id | CSA9 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1a0j |
| Chain | Residue | Details |
| F | ASP102 | |
| F | SER195 | |
| F | HIS57 |
