SCOP 1.63: Domain d1nnu.2: 1nnu B:,D:

Lineage for d1nnu.2 (1nnu B:,D:)

1. Root: SCOP 1.63

2. Class c: Alpha and beta proteins (a/b) [51349] (117 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] (10 families)

5. Family c.2.1.2: Tyrosine-dependent oxidoreductases [51751] (31 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 Enoyl-ACP reductase [51791] (4 species)

7. Species Malaria parasite (Plasmodium falciparum) [TaxId:5833] [82296] (4 PDB entries)

8. Domain d1nnu.2: 1nnu B:,D: [80673]
   complexed with nad, tct

Details for d1nnu.2

PDB Entry: 1nnu, 2.5 Å

PDB Description: Crystal Structure Analysis of Plasmodium falciparum enoyl-acyl-carrier-protein reductase with Triclosan Analog

SCOP Domain Sequences for d1nnu.2:

Sequence; same for both SEQRES and ATOM records:

>g1nnu.2 c.2.1.2 (B:,D:) Enoyl-ACP reductase {Malaria parasite (Plasmodium falciparum)}
edicfiagigdtngygwgiakelskrnvkiifgiwppvynifmknykngkfdndmiidkd
kkmnildmlpfdasfdtandideetknnkrynmlqnytiedvanlihqkygkinmlvhsl
anakevqkdllntsrkgyldalskssyslislckyfvnimkpqssiisltyhasqkvvpg
ygggmssakaalesdtrvlayhlgrnynirintisagplksraatainkXytfidyaiey
sekyaplrqkllstdigsvasfllsresraitgqtiyvdnglnimflpdd

Timeline for d1nnu.2:

• d1nnu.2 is new in SCOP 1.63
  
• d1nnu.2 appears in SCOP 1.65
  
• d1nnu.2 appears in the current release, SCOPe 2.08