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3Dee - Database of Protein Domain Definitions |
Class | Oxidoreductase |
Compound | Mol_id: 1; Molecule: Trypanothione Reductase; Chain: A, B, C, D; Ec: 1.6.4.8; Engineered: Yes; Biological_unit: Homodimer; Other_details: Monoclinic Crystal Form, Tetramer In The Asymmetric Unit |
Author | C.Strickland,P.Karplus |
Model type | XRAY |
Resolution | 2.200000 |
Domain | Segment | FROM | TO | See Domain | Enter Classification |
---|---|---|---|---|---|
1feaa-1 | 1 | A:1:- | A:163:- | Rasmol | Enter |
2 | A:286:- | A:360:- | |||
Class | (from SCOP) : Alpha and beta (a/b) | ||||
Fold | (from SCOP) : FAD (also NAD)-binding motif | ||||
1feaa-2 | 1 | A:164:- | A:285:- | Rasmol | Enter |
Class | (from SCOP) : Alpha and beta (a/b) | ||||
Fold | (from SCOP) : FAD (also NAD)-binding motif | ||||
1feaa-3 | 1 | A:361:- | A:487:- | 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]
Domain | Segment | FROM | TO | See Domain | Enter Classification |
---|---|---|---|---|---|
1feab-1 | 1 | B:1:- | B:163:- | Rasmol | Enter |
2 | B:285:- | B:359:- | |||
Class | (from SCOP) : Alpha and beta (a/b) | ||||
Fold | (from SCOP) : FAD (also NAD)-binding motif | ||||
1feab-2 | 1 | B:164:- | B:284:- | Rasmol | Enter |
Class | (from SCOP) : Alpha and beta (a/b) | ||||
Fold | (from SCOP) : FAD (also NAD)-binding motif | ||||
1feab-3 | 1 | B:360:- | B:484:- | 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]
Domain | Segment | FROM | TO | See Domain | Enter Classification |
---|---|---|---|---|---|
1feac-1 | 1 | C:1:- | C:163:- | Rasmol | Enter |
2 | C:286:- | C:360:- | |||
Class | (from SCOP) : Alpha and beta (a/b) | ||||
Fold | (from SCOP) : FAD (also NAD)-binding motif | ||||
1feac-2 | 1 | C:164:- | C:285:- | Rasmol | Enter |
Class | (from SCOP) : Alpha and beta (a/b) | ||||
Fold | (from SCOP) : FAD (also NAD)-binding motif | ||||
1feac-3 | 1 | C:361:- | C:487:- | 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]
Domain | Segment | FROM | TO | See Domain | Enter Classification |
---|---|---|---|---|---|
1fead-1 | 1 | D:1:- | D:163:- | Rasmol | Enter |
2 | D:285:- | D:359:- | |||
Class | (from SCOP) : Alpha and beta (a/b) | ||||
Fold | (from SCOP) : FAD (also NAD)-binding motif | ||||
1fead-2 | 1 | D:164:- | D:284:- | Rasmol | Enter |
Class | (from SCOP) : Alpha and beta (a/b) | ||||
Fold | (from SCOP) : FAD (also NAD)-binding motif | ||||
1fead-3 | 1 | D:360:- | D:484:- | 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]