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

  1. Root: SCOPe 2.02
  2. 1143363Class c: Alpha and beta proteins (a/b) [51349] (147 folds)
  3. 1150729Fold 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. 1150730Superfamily c.2.1: NAD(P)-binding Rossmann-fold domains [51735] (13 families) (S)
  5. 1153510Family c.2.1.7: Aminoacid dehydrogenase-like, C-terminal domain [51883] (11 proteins)
    extra N-terminal helix displaces the C-terminal helix (following strand 6) from its usual position creating a family nicotineamide-binding site
  6. 1153659Protein Mitochondrial NAD(P)-dependent malic enzyme [51898] (3 species)
    includes C-terminal additional subdomains
  7. 1153720Species Pig roundworm (Ascaris suum) [TaxId:6253] [75117] (2 PDB entries)
  8. 1153724Domain d1llqb1: 1llq B:296-593 [74010]
    Other proteins in same PDB: d1llqa2, d1llqb2
    complexed with nad

Details for d1llqb1

PDB Entry: 1llq (more details), 2.3 Å

PDB Description: Crystal Structure of Malic Enzyme from Ascaris suum Complexed with Nicotinamide Adenine Dinucleotide
PDB Compounds: (B:) NAD-dependent malic enzyme

SCOPe Domain Sequences for d1llqb1:

Sequence; same for both SEQRES and ATOM records: (download)

>d1llqb1 c.2.1.7 (B:296-593) Mitochondrial NAD(P)-dependent malic enzyme {Pig roundworm (Ascaris suum) [TaxId: 6253]}
iqgtasvivaglltctrvtkklvsqekylffgagaastgiaemivhqmqnegiskeeacn
riylmdidglvtknrkemnprhvqfakdmpettsileviraarpgaligastvrgafnee
viramaeinerpiifalsnptskaectaeeaytftngaalyasgspfpnfelnghtykpg
qgnnayifpgvalgtilfqirhvdndlfllaakkvascvtedslkvgrvypqlkeireis
iqiavemakycykngtanlypqpedlekyvraqvynteyeelinatydwpeqdmrhgf

SCOPe Domain Coordinates for d1llqb1:

Click to download the PDB-style file with coordinates for d1llqb1.
(The format of our PDB-style files is described here.)

Timeline for d1llqb1:

View in 3D
Domains from same chain:
(mouse over for more information)
d1llqb2