5MJK
Crystal Structure of Lactococcus lactis Thioredoxin Reductase (FO conformation)
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0004791 | molecular_function | thioredoxin-disulfide reductase (NADPH) activity |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0019430 | biological_process | removal of superoxide radicals |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0004791 | molecular_function | thioredoxin-disulfide reductase (NADPH) activity |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0019430 | biological_process | removal of superoxide radicals |
| C | 0000166 | molecular_function | nucleotide binding |
| C | 0004791 | molecular_function | thioredoxin-disulfide reductase (NADPH) activity |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0016491 | molecular_function | oxidoreductase activity |
| C | 0019430 | biological_process | removal of superoxide radicals |
| D | 0000166 | molecular_function | nucleotide binding |
| D | 0004791 | molecular_function | thioredoxin-disulfide reductase (NADPH) activity |
| D | 0005737 | cellular_component | cytoplasm |
| D | 0016491 | molecular_function | oxidoreductase activity |
| D | 0019430 | biological_process | removal of superoxide radicals |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 32 |
| Details | binding site for residue FAD A 401 |
| Chain | Residue |
| A | GLY12 |
| A | THR46 |
| A | ASN51 |
| A | GLY81 |
| A | VAL83 |
| A | ALA110 |
| A | THR111 |
| A | GLY112 |
| A | CYS137 |
| A | VAL243 |
| A | PHE246 |
| A | GLY14 |
| A | GLY276 |
| A | ASP277 |
| A | ARG284 |
| A | GLN285 |
| A | ILE286 |
| A | ALA289 |
| A | HOH509 |
| A | HOH511 |
| A | HOH519 |
| A | HOH522 |
| A | PRO15 |
| A | HOH524 |
| A | HOH528 |
| A | HOH537 |
| A | ALA16 |
| A | GLU35 |
| A | ARG36 |
| A | GLY41 |
| A | GLN42 |
| A | ASN45 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | binding site for residue SO4 A 402 |
| Chain | Residue |
| A | GLY153 |
| A | ASP154 |
| A | SER155 |
| A | ARG180 |
| site_id | AC3 |
| Number of Residues | 30 |
| Details | binding site for residue FAD B 401 |
| Chain | Residue |
| B | GLY12 |
| B | GLY14 |
| B | PRO15 |
| B | ALA16 |
| B | GLU35 |
| B | ARG36 |
| B | GLY41 |
| B | GLN42 |
| B | ASN45 |
| B | THR46 |
| B | ASN51 |
| B | GLY81 |
| B | VAL83 |
| B | ALA110 |
| B | THR111 |
| B | GLY112 |
| B | CYS137 |
| B | VAL243 |
| B | PHE246 |
| B | GLY276 |
| B | ASP277 |
| B | ARG284 |
| B | GLN285 |
| B | ILE286 |
| B | HOH513 |
| B | HOH523 |
| B | HOH531 |
| B | HOH535 |
| B | HOH544 |
| B | HOH560 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | binding site for residue SO4 B 402 |
| Chain | Residue |
| B | GLY153 |
| B | ASP154 |
| B | SER155 |
| B | ARG180 |
| site_id | AC5 |
| Number of Residues | 32 |
| Details | binding site for residue FAD C 401 |
| Chain | Residue |
| C | HOH535 |
| C | HOH544 |
| C | HOH551 |
| C | GLY12 |
| C | GLY14 |
| C | PRO15 |
| C | ALA16 |
| C | GLU35 |
| C | ARG36 |
| C | GLY41 |
| C | GLN42 |
| C | THR46 |
| C | ASN51 |
| C | GLY81 |
| C | VAL83 |
| C | ALA110 |
| C | THR111 |
| C | GLY112 |
| C | CYS137 |
| C | VAL243 |
| C | PHE246 |
| C | GLY276 |
| C | ASP277 |
| C | ARG284 |
| C | GLN285 |
| C | ILE286 |
| C | HOH511 |
| C | HOH512 |
| C | HOH513 |
| C | HOH523 |
| C | HOH528 |
| C | HOH530 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | binding site for residue SO4 C 402 |
| Chain | Residue |
| C | GLY153 |
| C | ASP154 |
| C | SER155 |
| C | ARG180 |
| site_id | AC7 |
| Number of Residues | 33 |
| Details | binding site for residue FAD D 401 |
| Chain | Residue |
| D | GLY12 |
| D | GLY14 |
| D | PRO15 |
| D | ALA16 |
| D | GLU35 |
| D | ARG36 |
| D | VAL38 |
| D | GLY41 |
| D | GLN42 |
| D | THR46 |
| D | ASN51 |
| D | GLY81 |
| D | VAL83 |
| D | ALA110 |
| D | THR111 |
| D | GLY112 |
| D | CYS137 |
| D | VAL243 |
| D | PHE246 |
| D | GLY276 |
| D | ASP277 |
| D | ARG284 |
| D | GLN285 |
| D | ILE286 |
| D | ALA289 |
| D | HOH506 |
| D | HOH509 |
| D | HOH510 |
| D | HOH518 |
| D | HOH520 |
| D | HOH526 |
| D | HOH527 |
| D | HOH528 |
| site_id | AC8 |
| Number of Residues | 4 |
| Details | binding site for residue SO4 D 402 |
| Chain | Residue |
| D | GLY153 |
| D | ASP154 |
| D | SER155 |
| D | ARG180 |
Functional Information from PROSITE/UniProt
| site_id | PS00573 |
| Number of Residues | 21 |
| Details | PYRIDINE_REDOX_2 Pyridine nucleotide-disulphide oxidoreductases class-II active site. CavCDGaf..FrnqeIlVIGGGD |
| Chain | Residue | Details |
| A | CYS134-ASP154 |






