1GRG
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 | GLUTATHIONE REDUCTASE | polymer | 478 | 51741.8 | 1 | UniProt (P00390) Pfam (PF00070) Pfam (PF02852) In PDB | Homo sapiens (human) | |
| 2 | A | PHOSPHATE ION | non-polymer | 95.0 | 1 | Chemie (PO4) | |||
| 3 | A | FLAVIN-ADENINE DINUCLEOTIDE | non-polymer | 785.5 | 1 | Chemie (FAD) | |||
| 4 | water | water | 18.0 | 520 | Chemie (HOH) |
Sequence viewer
Contents of the asymmetric unit
| Polymers | Number of chains | 1 |
| Total formula weight | 51741.8 | |
| Non-Polymers* | Number of molecules | 2 |
| Total formula weight | 880.5 | |
| All* | Total formula weight | 52622.3 |
