![]() |
3Dee - Database of Protein Domain Definitions |
Class | Oxidoreductase |
Compound | Mol_id: 1; Molecule: Glutathione Reductase; Chain: Null; Synonym: Grtr; Ec: 1.6.4.2; Engineered: Yes; Mutation: A34e, R37w; Biological_unit: Active As Dimer; Other_details: Contains A Non-covalently Bound Fad And Oxidized Glutathione Substrate |
Author | V.S.Stoll,S.J.Simpson,R.L.Krauth-siegel,C.T.Walsh,E.F.Pai |
Model type | XRAY |
Resolution | 2.700000 |
Domain | Segment | FROM | TO | See Domain | Enter Classification |
---|---|---|---|---|---|
2grt-1 | 1 | -:18:- | -:160:- | Rasmol | Enter |
2 | -:290:- | -:365:- | |||
Class | (from SCOP) : Alpha and beta (a/b) | ||||
Fold | (from SCOP) : FAD (also NAD)-binding motif | ||||
2grt-2 | 1 | -:161:- | -:289:- | Rasmol | Enter |
Class | (from SCOP) : Alpha and beta (a/b) | ||||
Fold | (from SCOP) : FAD (also NAD)-binding motif | ||||
2grt-3 | 1 | -:366:- | -:478:- | Rasmol | Enter |
Class | (from SCOP) : Alpha and beta (a+b) | ||||
Fold | (from SCOP) : FAD/NAD-linked reductases, dimerisation (C-terminal) domain |
[Show alternative domain definitions for this chain]