SCOP 1.65: Domain d1llqb1: 1llq B:296-593

Lineage for d1llqb1 (1llq B:296-593)

1. Root: SCOP 1.65

2. Class c: Alpha and beta proteins (a/b) [51349] (121 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.2.1.7: Aminoacid dehydrogenase-like, C-terminal domain [51883] (10 proteins)
   extra N-terminal helix displaces the C-terminal helix (following strand 6) from its usual position creating a family nicotineamide-binding site

6. Protein Mitochondrial NAD(P)-dependenent malic enzyme [51898] (3 species)
   includes C-terminal additional subdomains

7. Species Pig roundworm (Ascaris suum) [TaxId:6253] [75117] (2 PDB entries)

8. Domain d1llqb1: 1llq B:296-593 [74010]
   Other proteins in same PDB: d1llqa2, d1llqb2
   complexed with nad

Details for d1llqb1

PDB Entry: 1llq, 2.3 Å

PDB Description: Crystal Structure of Malic Enzyme from Ascaris suum Complexed with Nicotinamide Adenine Dinucleotide

SCOP Domain Sequences for d1llqb1:

Sequence; same for both SEQRES and ATOM records:

>d1llqb1 c.2.1.7 (B:296-593) Mitochondrial NAD(P)-dependenent malic enzyme {Pig roundworm (Ascaris suum)}
iqgtasvivaglltctrvtkklvsqekylffgagaastgiaemivhqmqnegiskeeacn
riylmdidglvtknrkemnprhvqfakdmpettsileviraarpgaligastvrgafnee
viramaeinerpiifalsnptskaectaeeaytftngaalyasgspfpnfelnghtykpg
qgnnayifpgvalgtilfqirhvdndlfllaakkvascvtedslkvgrvypqlkeireis
iqiavemakycykngtanlypqpedlekyvraqvynteyeelinatydwpeqdmrhgf

Timeline for d1llqb1:

• d1llqb1 first appeared in SCOP 1.61
  
• d1llqb1 appears in SCOP 1.63
  
• d1llqb1 appears in SCOP 1.67
  
• d1llqb1 appears in the current release, SCOPe 2.08