SCOPe 2.08: Domain d6w7sa1: 6w7s A:1448-1654

Lineage for d6w7sa1 (6w7s A:1448-1654)

1. Root: SCOPe 2.08

2. Class c: Alpha and beta proteins (a/b) [51349] (148 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] (13 families)

5. Family c.2.1.2: Tyrosine-dependent oxidoreductases [51751] (73 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
   has additional subdomain(s) that are not in the common domain
   

6. Protein Erythromycin synthase, eryAI, 1st ketoreductase module, N-terminal domain [418934] (1 species)
   protein contains tandem repeat of two SDR-like modules resembling a dimer commonly found in the family; only the second module retains the coenzyme-binding site

7. Species Saccharopolyspora erythraea [TaxId:1836] [419372] (4 PDB entries)
   Uniprot Q5UNP6

8. Domain d6w7sa1: 6w7s A:1448-1654 [392914]
   Other proteins in same PDB: d6w7sa2, d6w7sl1, d6w7sl2
   automated match to d2fr1a2
   complexed with cl, mes

Details for d6w7sa1

PDB Entry: 6w7s, 2.25 Å

PDB Description: ketoreductase from module 1 of the 6-deoxyerythronolide b synthase (kr1) in complex with antibody fragment (fab) 2g10

PDB Compounds: (A:) EryAI

SCOPe Domain Sequences for d6w7sa1:

Sequence; same for both SEQRES and ATOM records:

>d6w7sa1 c.2.1.2 (A:1448-1654) Erythromycin synthase, eryAI, 1st ketoreductase module, N-terminal domain {Saccharopolyspora erythraea [TaxId: 1836]}
devsalryriewrptgageparldgtwlvakyagtadetstaarealesagarvrelvvd
arcgrdelaerlrsvgevagvlsllavdeaepeeaplalasladtlslvqamvsaelgcp
lwtvtesavatgpfervrnaahgalwgvgrvialenpavwgglvdvpagsvaelarhlaa
vvsggagedqlalradgvygrrwvraa

Timeline for d6w7sa1:

• d6w7sa1 first appeared in SCOPe 2.07