SCOPe 2.06: Domain d1agsa2: 1ags A:1-79

Lineage for d1agsa2 (1ags A:1-79)

1. Root: SCOPe 2.06

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

3. Fold c.47: Thioredoxin fold [52832] (2 superfamilies)
   core: 3 layers, a/b/a; mixed beta-sheet of 4 strands, order 4312; strand 3 is antiparallel to the rest

4. Superfamily c.47.1: Thioredoxin-like [52833] (24 families)

5. Family c.47.1.5: Glutathione S-transferase (GST), N-terminal domain [52862] (19 proteins)

6. Protein Class alpha GST [81360] (8 species)

7. Species Human (Homo sapiens), (a1-1) [TaxId:9606] [52870] (30 PDB entries)
   Uniprot P08263

8. Domain d1agsa2: 1ags A:1-79 [32985]
   Other proteins in same PDB: d1agsa1, d1agsb1
   complexed with gtx; mutant

Details for d1agsa2

PDB Entry: 1ags, 2.5 Å

PDB Description: a surface mutant (g82r) of a human alpha-glutathione s-transferase shows decreased thermal stability and a new mode of molecular association in the crystal

PDB Compounds: (A:) glutathione s-transferase alpha

SCOPe Domain Sequences for d1agsa2:

Sequence; same for both SEQRES and ATOM records:

>d1agsa2 c.47.1.5 (A:1-79) Class alpha GST {Human (Homo sapiens), (a1-1) [TaxId: 9606]}
aekpklhyfnargrmestrwllaaagvefeekfiksaedldklrndgylmfqqvpmveid
gmklvqtrailnyiaskyn

Timeline for d1agsa2:

• d1agsa2 first appeared (with stable ids) in SCOP 1.55
  
• d1agsa2 appears in SCOPe 2.05
  
• d1agsa2 appears in SCOPe 2.07
  
• d1agsa2 appears in the current release, SCOPe 2.08