SCOPe 2.04: Domain d3sqpa2: 3sqp A:166-290

Lineage for d3sqpa2 (3sqp A:166-290)

1. Root: SCOPe 2.04

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 d3sqpa2: 3sqp A:166-290 [261746]
   Other proteins in same PDB: d3sqpa3, d3sqpb3
   automated match to d3grsa2
   protein/RNA complex; complexed with 3j8, fad, gol, so4

Details for d3sqpa2

PDB Entry: 3sqp, 2.21 Å

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

PDB Compounds: (A:) glutathione reductase, mitochondrial

SCOPe Domain Sequences for d3sqpa2:

Sequence; same for both SEQRES and ATOM records:

>d3sqpa2 c.3.1.5 (A:166-290) Glutathione reductase {Human (Homo sapiens) [TaxId: 9606]}
sqipgaslgitsdgffqleelpgrsvivgagyiavemagilsalgsktslmirhdkvlrs
fdsmistncteelenagvevlkfsqvkevkktlsglevsmvtavpgrlpvmtmipdvdcl
lwaig

Timeline for d3sqpa2:

• d3sqpa2 is new in SCOPe 2.04-stable
  
• d3sqpa2 appears in SCOPe 2.05
  
• d3sqpa2 appears in the current release, SCOPe 2.08