2FA4
Crystal Structure of Oxidized Form from Saccharomyces cerevisiae
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000011 | biological_process | vacuole inheritance |
| A | 0000103 | biological_process | sulfate assimilation |
| A | 0000139 | cellular_component | Golgi membrane |
| A | 0000324 | cellular_component | fungal-type vacuole |
| A | 0005515 | molecular_function | protein binding |
| A | 0005634 | cellular_component | nucleus |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005829 | cellular_component | cytosol |
| A | 0006749 | biological_process | glutathione metabolic process |
| A | 0006888 | biological_process | endoplasmic reticulum to Golgi vesicle-mediated transport |
| A | 0006890 | biological_process | retrograde vesicle-mediated transport, Golgi to endoplasmic reticulum |
| A | 0009263 | biological_process | deoxyribonucleotide biosynthetic process |
| A | 0015031 | biological_process | protein transport |
| A | 0015035 | molecular_function | protein-disulfide reductase activity |
| A | 0015036 | molecular_function | disulfide oxidoreductase activity |
| A | 0042144 | biological_process | vacuole fusion, non-autophagic |
| A | 0045454 | biological_process | cell redox homeostasis |
| A | 0120124 | cellular_component | membrane fusion priming complex |
| B | 0000011 | biological_process | vacuole inheritance |
| B | 0000103 | biological_process | sulfate assimilation |
| B | 0000139 | cellular_component | Golgi membrane |
| B | 0000324 | cellular_component | fungal-type vacuole |
| B | 0005515 | molecular_function | protein binding |
| B | 0005634 | cellular_component | nucleus |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005829 | cellular_component | cytosol |
| B | 0006749 | biological_process | glutathione metabolic process |
| B | 0006888 | biological_process | endoplasmic reticulum to Golgi vesicle-mediated transport |
| B | 0006890 | biological_process | retrograde vesicle-mediated transport, Golgi to endoplasmic reticulum |
| B | 0009263 | biological_process | deoxyribonucleotide biosynthetic process |
| B | 0015031 | biological_process | protein transport |
| B | 0015035 | molecular_function | protein-disulfide reductase activity |
| B | 0015036 | molecular_function | disulfide oxidoreductase activity |
| B | 0042144 | biological_process | vacuole fusion, non-autophagic |
| B | 0045454 | biological_process | cell redox homeostasis |
| B | 0120124 | cellular_component | membrane fusion priming complex |
Functional Information from PROSITE/UniProt
| site_id | PS00194 |
| Number of Residues | 19 |
| Details | THIOREDOXIN_1 Thioredoxin family active site. VVdFFatWCGPCKmIapmI |
| Chain | Residue | Details |
| A | VAL23-ILE41 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 204 |
| 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"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Site: {"description":"Deprotonates C-terminal active site Cys"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| Details | Site: {"description":"Contributes to redox potential value"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"18407956","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"19779198","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 6 |
| Details | Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)","evidences":[{"source":"PubMed","id":"22106047","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1mek |
| Chain | Residue | Details |
| A | CYS31 | |
| A | CYS34 | |
| A | PRO33 | |
| A | GLY32 |
| site_id | CSA2 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1mek |
| Chain | Residue | Details |
| B | CYS31 | |
| B | CYS34 | |
| B | PRO33 | |
| B | GLY32 |
| site_id | CSA3 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1mek |
| Chain | Residue | Details |
| A | CYS31 | |
| A | CYS34 |
| site_id | CSA4 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1mek |
| Chain | Residue | Details |
| B | CYS31 | |
| B | CYS34 |
