Class c: Alpha and beta proteins (a/b) [51349] (148 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] (9 families) |
Family c.3.1.5: FAD/NAD-linked reductases, N-terminal and central domains [51943] (25 proteins) duplication: both domains have similar folds and functions most members of the family contain common C-terminal alpha+beta domain |
Protein Trypanothione reductase, middle domain [418955] (3 species) |
Domain d1feab2: 1fea B:170-286 [30500] Other proteins in same PDB: d1feaa1, d1feaa3, d1feab1, d1feab3, d1feac1, d1feac3, d1fead1, d1fead3 complexed with fad |
PDB Entry: 1fea (more details), 2.2 Å
SCOPe Domain Sequences for d1feab2:
Sequence; same for both SEQRES and ATOM records: (download)
>d1feab2 c.3.1.5 (B:170-286) Trypanothione reductase, middle domain {Crithidia fasciculata [TaxId: 5656]} gddlcitsneafyldeapkralcvgggyisiefagifnaykarggqvdlayrgdmilrgf dselrkqlteqlranginvrthenpakvtknadgtrhvvfesgaeadydvvmlaigr
Timeline for d1feab2: