6GND
Crystal structure of the complex of a Ferredoxin-Flavin Thioredoxin Reductase and a Thioredoxin from Clostridium acetobutylicum at 2.9 A resolution
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0016491 | molecular_function | oxidoreductase activity |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005829 | cellular_component | cytosol |
| B | 0015035 | molecular_function | protein-disulfide reductase activity |
| B | 0045454 | biological_process | cell redox homeostasis |
| C | 0000166 | molecular_function | nucleotide binding |
| C | 0016491 | molecular_function | oxidoreductase activity |
| D | 0005737 | cellular_component | cytoplasm |
| D | 0005829 | cellular_component | cytosol |
| D | 0015035 | molecular_function | protein-disulfide reductase activity |
| D | 0045454 | biological_process | cell redox homeostasis |
| E | 0000166 | molecular_function | nucleotide binding |
| E | 0016491 | molecular_function | oxidoreductase activity |
| F | 0005737 | cellular_component | cytoplasm |
| F | 0005829 | cellular_component | cytosol |
| F | 0015035 | molecular_function | protein-disulfide reductase activity |
| F | 0045454 | biological_process | cell redox homeostasis |
| G | 0000166 | molecular_function | nucleotide binding |
| G | 0016491 | molecular_function | oxidoreductase activity |
| H | 0005737 | cellular_component | cytoplasm |
| H | 0005829 | cellular_component | cytosol |
| H | 0015035 | molecular_function | protein-disulfide reductase activity |
| H | 0045454 | biological_process | cell redox homeostasis |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 18 |
| Details | binding site for residue FAD A 300 |
| Chain | Residue |
| A | GLY10 |
| A | ASN49 |
| A | VAL81 |
| A | ALA108 |
| A | MET109 |
| A | GLY254 |
| A | ASP255 |
| A | TYR261 |
| A | GLN262 |
| A | TYR263 |
| A | SER11 |
| A | GLY12 |
| A | PRO13 |
| A | LEU37 |
| A | SER38 |
| A | LEU43 |
| A | ALA44 |
| A | ILE47 |
| site_id | AC2 |
| Number of Residues | 19 |
| Details | binding site for residue FAD C 301 |
| Chain | Residue |
| C | GLY10 |
| C | SER11 |
| C | GLY12 |
| C | PRO13 |
| C | ALA14 |
| C | SER34 |
| C | LEU37 |
| C | SER38 |
| C | ALA44 |
| C | ASN49 |
| C | VAL81 |
| C | ALA108 |
| C | MET109 |
| C | GLY254 |
| C | ASP255 |
| C | TYR261 |
| C | GLN262 |
| C | TYR263 |
| C | EDO302 |
| site_id | AC3 |
| Number of Residues | 3 |
| Details | binding site for residue EDO C 302 |
| Chain | Residue |
| C | GLY33 |
| C | SER34 |
| C | FAD301 |
| site_id | AC4 |
| Number of Residues | 2 |
| Details | binding site for residue EDO G 302 |
| Chain | Residue |
| G | GLN262 |
| G | FAD301 |
| site_id | AC5 |
| Number of Residues | 24 |
| Details | binding site for Di-peptide FAD E 300 and GLN E 262 |
| Chain | Residue |
| C | GLN271 |
| E | SER11 |
| E | GLY12 |
| E | PRO13 |
| E | ALA14 |
| E | SER34 |
| E | LEU37 |
| E | SER38 |
| E | LYS40 |
| E | ALA44 |
| E | VAL46 |
| E | ILE47 |
| E | ASN49 |
| E | VAL81 |
| E | ALA108 |
| E | MET109 |
| E | GLY254 |
| E | ASP255 |
| E | PRO260 |
| E | TYR261 |
| E | TYR263 |
| E | MET264 |
| E | LYS265 |
| E | ALA266 |
| site_id | AC6 |
| Number of Residues | 23 |
| Details | binding site for Di-peptide FAD G 301 and GLN G 262 |
| Chain | Residue |
| A | GLN271 |
| G | SER11 |
| G | GLY12 |
| G | PRO13 |
| G | ALA14 |
| G | SER34 |
| G | LEU37 |
| G | SER38 |
| G | ALA44 |
| G | VAL46 |
| G | ASN49 |
| G | VAL81 |
| G | ALA108 |
| G | MET109 |
| G | GLY254 |
| G | ASP255 |
| G | PRO260 |
| G | TYR261 |
| G | TYR263 |
| G | MET264 |
| G | LYS265 |
| G | ALA266 |
| G | EDO302 |
