2AFQ
1.9 angstrom crystal structure of wild-type human thrombin in the sodium free state
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 | 0005509 | molecular_function | calcium ion binding |
| 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 |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE GOL D 1001 |
| Chain | Residue |
| D | HIS57 |
| D | TYR60 |
| D | LEU99 |
| D | HOH302 |
| D | HOH413 |
| D | HOH602 |
| D | HOH634 |
| D | HOH637 |
| D | HOH761 |
| site_id | AC2 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE GOL B 1002 |
| Chain | Residue |
| B | HIS57 |
| B | TYR60 |
| B | GLU192 |
| B | TRP215 |
| B | HOH336 |
| B | HOH552 |
| B | HOH612 |
| B | HOH640 |
| site_id | AC3 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE GOL D 1003 |
| Chain | Residue |
| D | PRO111 |
| D | PRO166 |
| D | ASP170 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE GOL B 1004 |
| Chain | Residue |
| B | ALA129 |
| B | HIS230 |
| B | PHE232 |
| B | ARG233 |
| B | HOH648 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL B 1005 |
| Chain | Residue |
| B | PHE34 |
| B | GLN38 |
| B | ARG67 |
| B | ARG73 |
| B | HOH464 |
| B | HOH642 |
| site_id | AC6 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE GOL D 1006 |
| Chain | Residue |
| D | ASP116 |
| site_id | AC7 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE GOL D 1007 |
| Chain | Residue |
| B | ASP222 |
| B | HOH369 |
| D | LEU41 |
| D | CYS42 |
| D | HIS57 |
| D | LYS60 |
| D | GLU192 |
| D | GLY193 |
| D | SER195 |
| D | HOH522 |
Functional Information from PROSITE/UniProt
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 | 6 |
| Details | Active site: {"description":"Charge relay system"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| 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 |
| B | ASP102 | |
| B | SER195 | |
| B | GLY193 | |
| B | HIS57 |
| site_id | CSA2 |
| 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 | CSA3 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1a0j |
| Chain | Residue | Details |
| B | SER195 | |
| B | GLY193 |
| site_id | CSA4 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1a0j |
| Chain | Residue | Details |
| D | SER195 | |
| D | GLY193 |
| site_id | CSA5 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1a0j |
| Chain | Residue | Details |
| B | ASP102 | |
| B | SER195 | |
| B | HIS57 | |
| B | GLY196 |
| site_id | CSA6 |
| 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 | CSA7 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1a0j |
| Chain | Residue | Details |
| B | ASP102 | |
| B | SER195 | |
| B | HIS57 |
| site_id | CSA8 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1a0j |
| Chain | Residue | Details |
| D | ASP102 | |
| D | SER195 | |
| D | HIS57 |
