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 | 0005829 | cellular_component | cytosol |
A | 0016491 | molecular_function | oxidoreductase activity |
A | 0019430 | biological_process | removal of superoxide radicals |
A | 0045454 | biological_process | cell redox homeostasis |
B | 0000166 | molecular_function | nucleotide binding |
B | 0004791 | molecular_function | thioredoxin-disulfide reductase (NADPH) activity |
B | 0005737 | cellular_component | cytoplasm |
B | 0005829 | cellular_component | cytosol |
B | 0016491 | molecular_function | oxidoreductase activity |
B | 0019430 | biological_process | removal of superoxide radicals |
B | 0045454 | biological_process | cell redox homeostasis |
C | 0000166 | molecular_function | nucleotide binding |
C | 0004791 | molecular_function | thioredoxin-disulfide reductase (NADPH) activity |
C | 0005737 | cellular_component | cytoplasm |
C | 0005829 | cellular_component | cytosol |
C | 0016491 | molecular_function | oxidoreductase activity |
C | 0019430 | biological_process | removal of superoxide radicals |
C | 0045454 | biological_process | cell redox homeostasis |
D | 0000166 | molecular_function | nucleotide binding |
D | 0004791 | molecular_function | thioredoxin-disulfide reductase (NADPH) activity |
D | 0005737 | cellular_component | cytoplasm |
D | 0005829 | cellular_component | cytosol |
D | 0016491 | molecular_function | oxidoreductase activity |
D | 0019430 | biological_process | removal of superoxide radicals |
D | 0045454 | biological_process | cell redox homeostasis |
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 |