SCOP 1.73: Domain d2fr0a1: 2fr0 A:1657-1915

Lineage for d2fr0a1 (2fr0 A:1657-1915)

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 Erythromycin synthase, eryAI, 1st ketoreductase module [141909] (1 species)
   tandem repeat of two SDR-like modules resembling a dimer commonly founf in the family; only the second module retains the coenzyme-binding site

7. Species Saccharopolyspora erythraea [TaxId:1836] [141910] (2 PDB entries)

8. Domain d2fr0a1: 2fr0 A:1657-1915 [133959]
   complexed with ndp

Details for d2fr0a1

PDB Entry: 2fr0, 1.81 Å

PDB Description: The first ketoreductase of the erythromycin synthase (crystal form 1)

PDB Compounds: (A:) Erythromycin synthase, EryAI

SCOP Domain Sequences for d2fr0a1:

Sequence; same for both SEQRES and ATOM records:

>d2fr0a1 c.2.1.2 (A:1657-1915) Erythromycin synthase, eryAI, 1st ketoreductase module {Saccharopolyspora erythraea [TaxId: 1836]}
atddewkptgtvlvtggtggvggqiarwlarrgaphlllvsrsgpdadgagelvaeleal
garttvaacdvtdresvrellggigddvplsavfhaaatlddgtvdtltgerierasrak
vlgarnlheltreldltafvlfssfasafgapglggyapgnayldglaqqrrsdglpata
vawgtwagsgmaegpvadrfrrhgviemppetacralqnaldraevcpividvrwdrfll
aytaqrptrlfdeiddarr

Timeline for d2fr0a1:

• d2fr0a1 is new in SCOP 1.73
  
• d2fr0a1 appears in SCOP 1.75
  
• d2fr0a1 appears in the current release, SCOPe 2.08