7X1R
Cryo-EM structure of human thioredoxin reductase bound by Au
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004791 | molecular_function | thioredoxin-disulfide reductase (NADPH) activity |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0016668 | molecular_function | oxidoreductase activity, acting on a sulfur group of donors, NAD(P) as acceptor |
| A | 0045454 | biological_process | cell redox homeostasis |
| A | 0050660 | molecular_function | flavin adenine dinucleotide binding |
| B | 0004791 | molecular_function | thioredoxin-disulfide reductase (NADPH) activity |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0016668 | molecular_function | oxidoreductase activity, acting on a sulfur group of donors, NAD(P) as acceptor |
| B | 0045454 | biological_process | cell redox homeostasis |
| B | 0050660 | molecular_function | flavin adenine dinucleotide binding |
Functional Information from PROSITE/UniProt
| site_id | PS00076 |
| Number of Residues | 11 |
| Details | PYRIDINE_REDOX_1 Pyridine nucleotide-disulphide oxidoreductases class-I active site. GGtCVnvGCIP |
| Chain | Residue | Details |
| A | GLY56-PRO66 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | ACT_SITE: Proton acceptor => ECO:0000250 |
| Chain | Residue | Details |
| A | HIS472 | |
| B | HIS472 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 24 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:17512005, ECO:0007744|PDB:2J3N |
| Chain | Residue | Details |
| A | SER22 | |
| A | LYS315 | |
| A | ASP334 | |
| A | HIS472 | |
| B | SER22 | |
| B | ASP42 | |
| B | THR58 | |
| B | GLY63 | |
| B | TYR131 | |
| B | ARG166 | |
| B | ALA198 | |
| A | ASP42 | |
| B | ARG221 | |
| B | GLY292 | |
| B | LYS315 | |
| B | ASP334 | |
| B | HIS472 | |
| A | THR58 | |
| A | GLY63 | |
| A | TYR131 | |
| A | ARG166 | |
| A | ALA198 | |
| A | ARG221 | |
| A | GLY292 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0007744|PDB:2J3N |
| Chain | Residue | Details |
| A | THR161 | |
| A | GLU341 | |
| B | THR161 | |
| B | GLU341 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0007744|PDB:2ZZ0, ECO:0007744|PDB:2ZZB, ECO:0007744|PDB:3QFA |
| Chain | Residue | Details |
| A | TYR200 | |
| B | TYR200 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000250|UniProtKB:O89049 |
| Chain | Residue | Details |
| A | ARG226 | |
| B | ARG226 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 2 |
| Details | MOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:Q9JMH6 |
| Chain | Residue | Details |
| A | LYS68 | |
| B | LYS68 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphotyrosine => ECO:0007744|PubMed:15592455 |
| Chain | Residue | Details |
| A | TYR131 | |
| B | TYR131 |
| site_id | SWS_FT_FI8 |
| Number of Residues | 4 |
| Details | CROSSLNK: Cysteinyl-selenocysteine (Cys-Sec) => ECO:0000250 |
| Chain | Residue | Details |
| A | CYS497 | |
| A | SEC498 | |
| B | CYS497 | |
| B | SEC498 |
