SCOPe 2.03: Domain d3q1la1: 3q1l A:2-127,A:330-358

Lineage for d3q1la1 (3q1l A:2-127,A:330-358)

1. Root: SCOPe 2.03

2. Class c: Alpha and beta proteins (a/b) [51349] (147 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.2.1.3: Glyceraldehyde-3-phosphate dehydrogenase-like, N-terminal domain [51800] (22 proteins)
   family members also share a common alpha+beta fold in C-terminal domain

6. Protein Aspartate beta-semialdehyde dehydrogenase [51813] (4 species)

7. Species Pneumococcus (Streptococcus pneumoniae) [TaxId:1313] [141917] (11 PDB entries)
   Uniprot Q8DQ00 2-127,330-357

8. Domain d3q1la1: 3q1l A:2-127,A:330-358 [215029]
   Other proteins in same PDB: d3q1la2, d3q1lb2, d3q1lc2, d3q1ld2
   automated match to d2gyya1
   complexed with dhl

Details for d3q1la1

PDB Entry: 3q1l, 2.3 Å

PDB Description: Crystals Structure of Aspartate beta-Semialdehyde Dehydrogenase from Streptococcus pneumoniae with cysteamine bound covalently to Cys 128

PDB Compounds: (A:) Aspartate beta-semialdehyde dehydrogenase

SCOPe Domain Sequences for d3q1la1:

Sequence; same for both SEQRES and ATOM records:

>d3q1la1 c.2.1.3 (A:2-127,A:330-358) Aspartate beta-semialdehyde dehydrogenase {Pneumococcus (Streptococcus pneumoniae) [TaxId: 1313]}
gytvavvgatgavgaqmikmleestlpidkirylasarsagkslkfkdqditieetteta
fegvdialfsagsstsakyapyavkagvvvvdntsyfrqnpdvplvvpevnahaldahng
iiacpnXaawnsvqiaetlherglvrptaelkfelk

Timeline for d3q1la1:

• d3q1la1 is new in SCOPe 2.03-stable
  
• d3q1la1 appears in SCOPe 2.04
  
• d3q1la1 appears in the current release, SCOPe 2.08