SCOPe 2.05: Domain d2tprb1: 2tpr B:1-168,B:286-357

Lineage for d2tprb1 (2tpr B:1-168,B:286-357)

1. Root: SCOPe 2.05

2. Class c: Alpha and beta proteins (a/b) [51349] (148 folds)

3. 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

4. Superfamily c.3.1: FAD/NAD(P)-binding domain [51905] (9 families)

5. Family c.3.1.5: FAD/NAD-linked reductases, N-terminal and central domains [51943] (15 proteins)
   duplication: both domains have similar folds and functions
   most members of the family contain common C-terminal alpha+beta domain

6. Protein Trypanothione reductase [51947] (3 species)

7. Species Crithidia fasciculata [TaxId:5656] [51948] (6 PDB entries)

8. Domain d2tprb1: 2tpr B:1-168,B:286-357 [30507]
   Other proteins in same PDB: d2tpra3, d2tprb3
   complexed with fad

Details for d2tprb1

PDB Entry: 2tpr, 2.4 Å

PDB Description: x-ray structure of trypanothione reductase from crithidia fasciculata at 2.4 angstroms resolution

PDB Compounds: (B:) trypanothione reductase

SCOPe Domain Sequences for d2tprb1:

Sequence; same for both SEQRES and ATOM records:

>d2tprb1 c.3.1.5 (B:1-168,B:286-357) Trypanothione reductase {Crithidia fasciculata [TaxId: 5656]}
sraydlvvigagsggleagwnaaslhkkrvavidlqkhhgpphyaalggtcvnvgcvpkk
lmvtganymdtiresagfgweldresvrpnwkaliaaknkavsgindsyegmfadteglt
fhqgfgalqdnhtvlvresadpnsavletldteyillatgswpqhlgiXrvprsqtlqle
kagvevakngaikvdaysktnvdniyaigdvtdrvmltpvainegaafvdtvfankprat
d

Timeline for d2tprb1:

• d2tprb1 first appeared (with stable ids) in SCOP 1.55
  
• d2tprb1 appears in SCOPe 2.04
  
• d2tprb1 appears in SCOPe 2.06
  
• d2tprb1 appears in the current release, SCOPe 2.08