Class c: Alpha and beta proteins (a/b) [51349] (117 folds) |
Fold c.3: FAD/NAD(P)-binding domain [51904] (1 superfamily) core: 3 layers, b/b/a; central parallel beta-sheet of 5 strands, order 32145; top antiparallel beta-sheet of 3 strands, meander |
Superfamily c.3.1: FAD/NAD(P)-binding domain [51905] (5 families) |
Family c.3.1.5: FAD/NAD-linked reductases, N-terminal and central domains [51943] (12 proteins) duplication: both domains have similar folds and functions most members of the family contain common C-terminal alpha+beta domain |
Protein Trypanothione reductase [51947] (2 species) |
Species Crithidia fasciculata [TaxId:5656] [51948] (6 PDB entries) |
Domain d1feac1: 1fea C:1-169,C:287-357 [30501] Other proteins in same PDB: d1feaa3, d1feab3, d1feac3, d1fead3 |
PDB Entry: 1fea (more details), 2.2 Å
SCOP Domain Sequences for d1feac1:
Sequence; same for both SEQRES and ATOM records: (download)
>d1feac1 c.3.1.5 (C:1-169,C:287-357) Trypanothione reductase {Crithidia fasciculata} sraydlvvigagsggleagwnaaslhkkrvavidlqkhhgpphyaalggtcvnvgcvpkk lmvtganymdtiresagfgweldresvrpnwkaliaaknkavsgindsyegmfadteglt fhqgfgalqdnhtvlvresadpnsavletldteyillatgswpqhlgieXvprsqtlqle kagvevakngaikvdaysktnvdniyaigdvtdrvmltpvainegaafvdtvfankprat d
Timeline for d1feac1: