1GRB
SUBSTRATE BINDING AND CATALYSIS BY GLUTATHIONE REDUCTASE AS DERIVED FROM REFINED ENZYME: SUBSTRATE CRYSTAL STRUCTURES AT 2 ANGSTROMS RESOLUTION
Entity
| Entity ID | Chain ID | Description | Type | Chain length | Formula weight | Number of molecules | DB Name (Accession) | Biological source | Descriptive keywords |
| 1 | A (A) | GLUTATHIONE REDUCTASE | polymer | 478 | 51636.2 | 1 | UniProt (P00390) Pfam (PF00070) Pfam (PF02852) | Homo sapiens (human) | |
| 2 | B (A) | PHOSPHATE ION | non-polymer | 95.0 | 1 | Chemie (PO4) | |||
| 3 | C (A) | FLAVIN-ADENINE DINUCLEOTIDE | non-polymer | 785.5 | 1 | Chemie (FAD) | |||
| 4 | D (A) | NICOTINAMIDE-ADENINE-DINUCLEOTIDE | non-polymer | 663.4 | 1 | Chemie (NAD) | |||
| 5 | E (A) | NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE | non-polymer | 745.4 | 1 | Chemie (NDP) | |||
| 6 | F (A) | water | water | 18.0 | 527 | Chemie (HOH) |
Sequence viewer
Contents of the asymmetric unit
| Polymers | Number of chains | 1 |
| Total formula weight | 51636.2 | |
| Non-Polymers* | Number of molecules | 4 |
| Total formula weight | 2289.4 | |
| All* | Total formula weight | 53925.6 |
