SCOPe 2.06: Domain d3sqpb1: 3sqp B:18-165,B:291-363

Lineage for d3sqpb1 (3sqp B:18-165,B:291-363)

1. Root: SCOPe 2.06

2. Class c: Alpha and beta proteins (a/b) [51349] (148 folds)

3. Fold c.3: FAD/NAD(P)-binding domain [51904] (1 superfamily)
   core: 3 layers, b/b/a; central parallel beta-sheet of 5 strands, order 32145; top antiparallel beta-sheet of 3 strands, meander

4. Superfamily c.3.1: FAD/NAD(P)-binding domain [51905] (9 families)

5. Family c.3.1.5: FAD/NAD-linked reductases, N-terminal and central domains [51943] (15 proteins)
   duplication: both domains have similar folds and functions
   most members of the family contain common C-terminal alpha+beta domain

6. Protein Glutathione reductase [51944] (3 species)

7. Species Human (Homo sapiens) [TaxId:9606] [51945] (23 PDB entries)

8. Domain d3sqpb1: 3sqp B:18-165,B:291-363 [261599]
   Other proteins in same PDB: d3sqpa3, d3sqpb3
   automated match to d3grsa1
   protein/RNA complex; complexed with 3j8, fad, gol, so4

Details for d3sqpb1

PDB Entry: 3sqp, 2.21 Å

PDB Description: Structure of human glutathione reductase complexed with pyocyanin, an agent with antimalarial activity

PDB Compounds: (B:) glutathione reductase, mitochondrial

SCOPe Domain Sequences for d3sqpb1:

Sequence; same for both SEQRES and ATOM records:

>d3sqpb1 c.3.1.5 (B:18-165,B:291-363) Glutathione reductase {Human (Homo sapiens) [TaxId: 9606]}
vasydylvigggsgglasarraaelgaraavveshklggtcvnvgcvpkkvmwntavhse
fmhdhadygfpscegkfnwrvikekrdayvsrlnaiyqnnltkshieiirghaaftsdpk
ptievsgkkytaphiliatggmpstpheXrvpntkdlslnklgiqtddkghiivdefqnt
nvkgiyavgdvcgkalltpvaiaagrklahrlfeykedskld

Timeline for d3sqpb1:

• d3sqpb1 first appeared in SCOPe 2.04
  
• d3sqpb1 appears in SCOPe 2.05
  
• d3sqpb1 appears in SCOPe 2.07
  
• d3sqpb1 appears in the current release, SCOPe 2.08