![]() | 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 d1tytb2: 1tyt B:170-286 [30516] Other proteins in same PDB: d1tyta1, d1tyta3, d1tytb1, d1tytb3 complexed with fad |
PDB Entry: 1tyt (more details), 2.6 Å
SCOPe Domain Sequences for d1tytb2:
Sequence; same for both SEQRES and ATOM records: (download)
>d1tytb2 c.3.1.5 (B:170-286) Trypanothione reductase, middle domain {Crithidia fasciculata [TaxId: 5656]} egddlcitsneafyldeapkralcvgggyisiefagifnaykarggqvdlayrgdmilrg fdselrkqlteqlranginvrthenpakvtknadgtrhvvfesgaeadydvvmlaig
Timeline for d1tytb2: