3ITJ
Crystal structure of Saccharomyces cerevisiae thioredoxin reductase 1 (Trr1)
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004791 | molecular_function | thioredoxin-disulfide reductase (NADPH) activity |
| A | 0005515 | molecular_function | protein binding |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005739 | cellular_component | mitochondrion |
| A | 0005758 | cellular_component | mitochondrial intermembrane space |
| A | 0005829 | cellular_component | cytosol |
| A | 0008198 | molecular_function | ferrous iron binding |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0019430 | biological_process | removal of superoxide radicals |
| A | 0034599 | biological_process | cellular response to oxidative stress |
| A | 0045454 | biological_process | cell redox homeostasis |
| B | 0004791 | molecular_function | thioredoxin-disulfide reductase (NADPH) activity |
| B | 0005515 | molecular_function | protein binding |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005739 | cellular_component | mitochondrion |
| B | 0005758 | cellular_component | mitochondrial intermembrane space |
| B | 0005829 | cellular_component | cytosol |
| B | 0008198 | molecular_function | ferrous iron binding |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0019430 | biological_process | removal of superoxide radicals |
| B | 0034599 | biological_process | cellular response to oxidative stress |
| B | 0045454 | biological_process | cell redox homeostasis |
| C | 0004791 | molecular_function | thioredoxin-disulfide reductase (NADPH) activity |
| C | 0005515 | molecular_function | protein binding |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0005739 | cellular_component | mitochondrion |
| C | 0005758 | cellular_component | mitochondrial intermembrane space |
| C | 0005829 | cellular_component | cytosol |
| C | 0008198 | molecular_function | ferrous iron binding |
| C | 0016491 | molecular_function | oxidoreductase activity |
| C | 0019430 | biological_process | removal of superoxide radicals |
| C | 0034599 | biological_process | cellular response to oxidative stress |
| C | 0045454 | biological_process | cell redox homeostasis |
| D | 0004791 | molecular_function | thioredoxin-disulfide reductase (NADPH) activity |
| D | 0005515 | molecular_function | protein binding |
| D | 0005737 | cellular_component | cytoplasm |
| D | 0005739 | cellular_component | mitochondrion |
| D | 0005758 | cellular_component | mitochondrial intermembrane space |
| D | 0005829 | cellular_component | cytosol |
| D | 0008198 | molecular_function | ferrous iron binding |
| D | 0016491 | molecular_function | oxidoreductase activity |
| D | 0019430 | biological_process | removal of superoxide radicals |
| D | 0034599 | biological_process | cellular response to oxidative stress |
| D | 0045454 | biological_process | cell redox homeostasis |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 39 |
| Details | BINDING SITE FOR RESIDUE FAD A 400 |
| Chain | Residue |
| A | ILE8 |
| A | ALA36 |
| A | ASN37 |
| A | ILE39 |
| A | ALA40 |
| A | GLY43 |
| A | GLN44 |
| A | LEU45 |
| A | THR48 |
| A | ILE51 |
| A | ASN53 |
| A | GLY9 |
| A | THR85 |
| A | VAL86 |
| A | THR118 |
| A | GLY119 |
| A | TRP134 |
| A | CYS144 |
| A | GLY286 |
| A | ASP287 |
| A | ARG294 |
| A | GLN295 |
| A | SER10 |
| A | ALA296 |
| A | SER299 |
| A | HOH323 |
| A | HOH328 |
| A | HOH332 |
| A | HOH335 |
| A | HOH337 |
| A | HOH352 |
| A | HOH377 |
| D | TYR20 |
| A | GLY11 |
| A | PRO12 |
| A | ALA13 |
| A | TYR31 |
| A | GLU32 |
| A | GLY33 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CIT A 501 |
| Chain | Residue |
| A | ASP163 |
| A | SER164 |
| A | ARG189 |
| A | GLY248 |
| A | HIS249 |
| A | HOH386 |
| site_id | AC3 |
| Number of Residues | 39 |
| Details | BINDING SITE FOR RESIDUE FAD B 401 |
| Chain | Residue |
| B | ILE8 |
| B | GLY9 |
| B | SER10 |
| B | GLY11 |
| B | PRO12 |
| B | ALA13 |
| B | TYR31 |
| B | GLU32 |
| B | GLY33 |
| B | ALA36 |
| B | ASN37 |
| B | ILE39 |
| B | ALA40 |
| B | GLY43 |
| B | GLN44 |
| B | LEU45 |
| B | THR48 |
| B | ILE51 |
| B | ASN53 |
| B | GLU84 |
| B | THR85 |
| B | VAL86 |
| B | THR118 |
| B | GLY119 |
| B | TRP134 |
| B | GLN135 |
| B | CYS144 |
| B | GLY286 |
| B | ASP287 |
| B | ARG294 |
| B | GLN295 |
| B | ALA296 |
| B | SER299 |
| B | HOH323 |
| B | HOH326 |
| B | HOH327 |
| B | HOH329 |
| B | HOH334 |
| C | TYR20 |
| site_id | AC4 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE CIT B 502 |
| Chain | Residue |
| B | GLY160 |
| B | GLY161 |
| B | ARG184 |
| B | LYS185 |
| B | ARG189 |
| B | ILE247 |
| B | HOH341 |
| B | HOH355 |
| B | HOH356 |
| B | HOH358 |
| B | HOH391 |
| site_id | AC5 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE CIT B 506 |
| Chain | Residue |
| B | HIS249 |
| B | HOH325 |
| B | HOH380 |
| B | ASP163 |
| B | SER164 |
| B | ARG189 |
| B | GLY248 |
| site_id | AC6 |
| Number of Residues | 38 |
| Details | BINDING SITE FOR RESIDUE FAD C 402 |
| Chain | Residue |
| B | TYR20 |
| C | ILE8 |
| C | GLY9 |
| C | SER10 |
| C | GLY11 |
| C | PRO12 |
| C | ALA13 |
| C | TYR31 |
| C | GLU32 |
| C | GLY33 |
| C | ALA36 |
| C | ILE39 |
| C | ALA40 |
| C | GLY43 |
| C | GLN44 |
| C | LEU45 |
| C | THR48 |
| C | ILE51 |
| C | ASN53 |
| C | GLU84 |
| C | THR85 |
| C | VAL86 |
| C | THR118 |
| C | GLY119 |
| C | CYS141 |
| C | CYS144 |
| C | GLY286 |
| C | ASP287 |
| C | ARG294 |
| C | GLN295 |
| C | ALA296 |
| C | SER299 |
| C | HOH325 |
| C | HOH326 |
| C | HOH331 |
| C | HOH332 |
| C | HOH333 |
| C | HOH337 |
| site_id | AC7 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE CIT C 503 |
| Chain | Residue |
| A | GLU234 |
| C | MET125 |
| C | GLY161 |
| C | ARG184 |
| C | ARG189 |
| C | ILE247 |
| C | HOH366 |
| site_id | AC8 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE CIT C 505 |
| Chain | Residue |
| C | GLY162 |
| C | ASP163 |
| C | SER164 |
| C | ARG189 |
| C | GLY248 |
| C | HIS249 |
| C | ARG294 |
| C | HOH371 |
| C | HOH380 |
| site_id | AC9 |
| Number of Residues | 38 |
| Details | BINDING SITE FOR RESIDUE FAD D 403 |
| Chain | Residue |
| A | TYR20 |
| D | ILE8 |
| D | GLY9 |
| D | SER10 |
| D | GLY11 |
| D | PRO12 |
| D | ALA13 |
| D | TYR31 |
| D | GLU32 |
| D | GLY33 |
| D | ALA36 |
| D | ASN37 |
| D | ILE39 |
| D | ALA40 |
| D | GLY43 |
| D | GLN44 |
| D | THR48 |
| D | ILE51 |
| D | ASN53 |
| D | GLU84 |
| D | THR85 |
| D | VAL86 |
| D | ALA117 |
| D | THR118 |
| D | GLY119 |
| D | ALA140 |
| D | ILE255 |
| D | GLY286 |
| D | ASP287 |
| D | ARG294 |
| D | GLN295 |
| D | ALA296 |
| D | SER299 |
| D | HOH324 |
| D | HOH334 |
| D | HOH336 |
| D | HOH339 |
| D | HOH341 |
| site_id | BC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CIT D 504 |
| Chain | Residue |
| C | LYS232 |
| D | ARG184 |
| D | ILE247 |
| D | HOH352 |
| D | HOH357 |
Functional Information from PROSITE/UniProt
| site_id | PS00573 |
| Number of Residues | 23 |
| Details | PYRIDINE_REDOX_2 Pyridine nucleotide-disulphide oxidoreductases class-II active site. CavCDGavpiFrnkpLaVIGGGD |
| Chain | Residue | Details |
| A | CYS141-ASP163 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 32 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:18930846, ECO:0000269|PubMed:20235561 |
| Chain | Residue | Details |
| A | SER10 | |
| B | ILE39 | |
| B | GLN44 | |
| B | ASN53 | |
| B | VAL86 | |
| B | CYS144 | |
| B | ASP287 | |
| B | ARG294 | |
| C | SER10 | |
| C | ILE39 | |
| C | GLN44 | |
| A | ILE39 | |
| C | ASN53 | |
| C | VAL86 | |
| C | CYS144 | |
| C | ASP287 | |
| C | ARG294 | |
| D | SER10 | |
| D | ILE39 | |
| D | GLN44 | |
| D | ASN53 | |
| D | VAL86 | |
| A | GLN44 | |
| D | CYS144 | |
| D | ASP287 | |
| D | ARG294 | |
| A | ASN53 | |
| A | VAL86 | |
| A | CYS144 | |
| A | ASP287 | |
| A | ARG294 | |
| B | SER10 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:18407956 |
| Chain | Residue | Details |
| A | SER302 | |
| B | SER302 | |
| C | SER302 | |
| D | SER302 |
