SCOP 1.73: Domain d1wntd1: 1wnt D:1-244

Lineage for d1wntd1 (1wnt D:1-244)

1. Root: SCOP 1.73

2. Class c: Alpha and beta proteins (a/b) [51349] (141 folds)

3. Fold c.2: NAD(P)-binding Rossmann-fold domains [51734] (1 superfamily)
   core: 3 layers, a/b/a; parallel beta-sheet of 6 strands, order 321456
   The nucleotide-binding modes of this and the next two folds/superfamilies are similar

4. Superfamily c.2.1: NAD(P)-binding Rossmann-fold domains [51735] (12 families)

5. Family c.2.1.2: Tyrosine-dependent oxidoreductases [51751] (70 proteins)
   also known as short-chain dehydrogenases and SDR family
   parallel beta-sheet is extended by 7th strand, order 3214567; left-handed crossover connection between strands 6 and 7

6. Protein Carbonyl reductase [51765] (2 species)

7. Species Human (Homo sapiens) [TaxId:9606] [102144] (2 PDB entries)
   dicarbonyl/L-xylulose reductase

8. Domain d1wntd1: 1wnt D:1-244 [121105]
   automatically matched to d1pr9a_
   complexed with nap

Details for d1wntd1

PDB Entry: 1wnt, 2.3 Å

PDB Description: structure of the tetrameric form of human l-xylulose reductase

PDB Compounds: (D:) L-xylulose reductase

SCOP Domain Sequences for d1wntd1:

Sequence; same for both SEQRES and ATOM records:

>d1wntd1 c.2.1.2 (D:1-244) Carbonyl reductase {Human (Homo sapiens) [TaxId: 9606]}
melflagrrvlvtgagkgigrgtvqalhatgarvvavsrtqadldslvrecpgiepvcvd
lgdweateralgsvgpvdllvnnaavallqpflevtkeafdrsfevnlraviqvsqivar
gliargvpgaivnvssqcsqravtnhsvycstkgaldmltkvmalelgphkirvnavnpt
vvmtsmgqatwsdphkaktmlnriplgkfaevehvvnailfllsdrsgmttgstlpvegg
fwac

Timeline for d1wntd1:

• d1wntd1 is new in SCOP 1.73
  
• d1wntd1 appears in SCOP 1.75
  
• d1wntd1 appears in the current release, SCOPe 2.08, called d1wntd_