1GRF
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 | 51636.2 | 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 | A | ACETAMIDE | non-polymer | 59.1 | 1 | Chemie (ACM) | |||
5 | water | water | 18.0 | 531 | Chemie (HOH) |
Sequence viewer
Contents of the asymmetric unit
Polymers | Number of chains | 1 |
Total formula weight | 51636.2 | |
Non-Polymers* | Number of molecules | 3 |
Total formula weight | 939.6 | |
All* | Total formula weight | 52575.8 |