8YS1
Crystal structure of rat thioredoxin, Wild-type
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004791 | molecular_function | thioredoxin-disulfide reductase (NADPH) activity |
| A | 0005576 | cellular_component | extracellular region |
| A | 0005634 | cellular_component | nucleus |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0009314 | biological_process | response to radiation |
| A | 0010269 | biological_process | response to selenium ion |
| A | 0014823 | biological_process | response to activity |
| A | 0015035 | molecular_function | protein-disulfide reductase activity |
| A | 0019725 | biological_process | cellular homeostasis |
| A | 0019899 | molecular_function | enzyme binding |
| A | 0030424 | cellular_component | axon |
| A | 0030425 | cellular_component | dendrite |
| A | 0043025 | cellular_component | neuronal cell body |
| A | 0043388 | biological_process | positive regulation of DNA binding |
| A | 0048678 | biological_process | response to axon injury |
| A | 0055114 | biological_process | obsolete oxidation-reduction process |
| A | 0071236 | biological_process | cellular response to antibiotic |
| A | 0071333 | biological_process | cellular response to glucose stimulus |
| A | 0071455 | biological_process | cellular response to hyperoxia |
| A | 0071466 | biological_process | cellular response to xenobiotic stimulus |
| A | 0071548 | biological_process | response to dexamethasone |
| A | 0097068 | biological_process | response to thyroxine |
| B | 0004791 | molecular_function | thioredoxin-disulfide reductase (NADPH) activity |
| B | 0005576 | cellular_component | extracellular region |
| B | 0005634 | cellular_component | nucleus |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0009314 | biological_process | response to radiation |
| B | 0010269 | biological_process | response to selenium ion |
| B | 0014823 | biological_process | response to activity |
| B | 0015035 | molecular_function | protein-disulfide reductase activity |
| B | 0019725 | biological_process | cellular homeostasis |
| B | 0019899 | molecular_function | enzyme binding |
| B | 0030424 | cellular_component | axon |
| B | 0030425 | cellular_component | dendrite |
| B | 0043025 | cellular_component | neuronal cell body |
| B | 0043388 | biological_process | positive regulation of DNA binding |
| B | 0048678 | biological_process | response to axon injury |
| B | 0055114 | biological_process | obsolete oxidation-reduction process |
| B | 0071236 | biological_process | cellular response to antibiotic |
| B | 0071333 | biological_process | cellular response to glucose stimulus |
| B | 0071455 | biological_process | cellular response to hyperoxia |
| B | 0071466 | biological_process | cellular response to xenobiotic stimulus |
| B | 0071548 | biological_process | response to dexamethasone |
| B | 0097068 | biological_process | response to thyroxine |
Functional Information from PROSITE/UniProt
| site_id | PS00194 |
| Number of Residues | 19 |
| Details | THIOREDOXIN_1 Thioredoxin family active site. VVdFSatWCGPCKmIkpfF |
| Chain | Residue | Details |
| A | VAL24-PHE42 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 206 |
| Details | Domain: {"description":"Thioredoxin","evidences":[{"source":"PROSITE-ProRule","id":"PRU00691","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | Active site: {"description":"Nucleophile","evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Site: {"description":"Deprotonates C-terminal active site Cys","evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| Details | Site: {"description":"Contributes to redox potential value","evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 4 |
| Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P10599","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"P10639","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 4 |
| Details | Modified residue: {"description":"S-nitrosocysteine","evidences":[{"source":"UniProtKB","id":"P10599","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"S-nitrosocysteine; alternate","evidences":[{"source":"UniProtKB","id":"P10599","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI9 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P10639","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
