SCOPe 2.07: Domain d1nhw.2: 1nhw B:,D:

Lineage for d1nhw.2 (1nhw B:,D:)

1. Root: SCOPe 2.07

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] (71 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] (11 species)

7. Species Malaria parasite (Plasmodium falciparum) [TaxId:5833] [82296] (23 PDB entries)
   Uniprot Q9BJJ9 96-424 # fragment

8. Domain d1nhw.2: 1nhw B:,D: [80519]
   complexed with nad, tcc

Details for d1nhw.2

PDB Entry: 1nhw, 2.35 Å

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

PDB Compounds: (B:) enoyl-acyl carrier reductase, (D:) enoyl-acyl carrier reductase

SCOPe Domain Sequences for d1nhw.2:

Sequence; same for both SEQRES and ATOM records:

>g1nhw.2 c.2.1.2 (B:,D:) Enoyl-ACP reductase {Malaria parasite (Plasmodium falciparum) [TaxId: 5833]}
edicfiagigdtngygwgiakelskrnvkiifgiwppvynifmknykngkfdndmiidkd
kkmnildmlpfdasfdtandideetknnkrynmlqnytiedvanlihqkygkinmlvhsl
anakevqkdllntsrkgyldalskssyslislckyfvnimkpqssiisltyhasqkvvpg
ygggmssakaalesdtrvlayhlgrnynirintisagplksraatainkXytfidyaiey
sekyaplrqkllstdigsvasfllsresraitgqtiyvdnglnimflpdd

Timeline for d1nhw.2:

• d1nhw.2 first appeared in SCOP 1.63
  
• d1nhw.2 appears in SCOPe 2.06
  
• d1nhw.2 appears in the current release, SCOPe 2.08