Lineage for d1feac1 (1fea C:1-169,C:287-357)

  1. Root: SCOPe 2.08
  2. 2826024Class c: Alpha and beta proteins (a/b) [51349] (148 folds)
  3. 2849308Fold 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
  4. 2849309Superfamily c.3.1: FAD/NAD(P)-binding domain [51905] (9 families) (S)
  5. 2849878Family 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
  6. 2850224Protein Trypanothione reductase, N- and C-terminal domain [418954] (3 species)
  7. 2850225Species Crithidia fasciculata [TaxId:5656] [419410] (6 PDB entries)
  8. 2850232Domain d1feac1: 1fea C:1-169,C:287-357 [30501]
    Other proteins in same PDB: d1feaa2, d1feaa3, d1feab2, d1feab3, d1feac2, d1feac3, d1fead2, d1fead3
    complexed with fad
    has additional insertions and/or extensions that are not grouped together

Details for d1feac1

PDB Entry: 1fea (more details), 2.2 Å

PDB Description: unliganded crithidia fasciculata trypanothione reductase at 2.2 angstrom resolution
PDB Compounds: (C:) trypanothione reductase

SCOPe 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, N- and C-terminal domain {Crithidia fasciculata [TaxId: 5656]}

SCOPe Domain Coordinates for d1feac1:

Click to download the PDB-style file with coordinates for d1feac1.
(The format of our PDB-style files is described here.)

Timeline for d1feac1: