SCOP 1.73: Domain d6gsub1: 6gsu B:85-217

Lineage for d6gsub1 (6gsu B:85-217)

1. Root: SCOP 1.73

2. Class a: All alpha proteins [46456] (258 folds)

3. Fold a.45: Glutathione S-transferase (GST), C-terminal domain [47615] (1 superfamily)
   core: 4 helices; bundle, closed, left-handed twist; right-handed superhelix

4. Superfamily a.45.1: Glutathione S-transferase (GST), C-terminal domain [47616] (1 family)
   this domains follows the thioredoxin-like N-terminal domain

5. Family a.45.1.1: Glutathione S-transferase (GST), C-terminal domain [47617] (18 proteins)

6. Protein Class mu GST [81348] (3 species)

7. Species Rat (Rattus norvegicus) [TaxId:10116] [47623] (16 PDB entries)

8. Domain d6gsub1: 6gsu B:85-217 [17636]
   Other proteins in same PDB: d6gsua2, d6gsub2
   complexed with gps, so4; mutant

Details for d6gsub1

PDB Entry: 6gsu, 1.85 Å

PDB Description: first-sphere and second-sphere electrostatic effects in the active site of a class mu glutathione transferase

PDB Compounds: (B:) mu class glutathione s-transferase of isoenzyme 3-3

SCOP Domain Sequences for d6gsub1:

Sequence; same for both SEQRES and ATOM records:

>d6gsub1 a.45.1.1 (B:85-217) Class mu GST {Rat (Rattus norvegicus) [TaxId: 10116]}
lcgeteeeriradivenqvmdnrmqlimlcynpdfekqkpeflktipekmklyseflgkr
pwfagdkvtyvdflaydildqyhifepkcldafpnlkdflarfeglkkisaymkssryls
tpifsklaqwsnk

Timeline for d6gsub1:

• d6gsub1 first appeared (with stable ids) in SCOP 1.55
  
• d6gsub1 appears in SCOP 1.71
  
• d6gsub1 appears in SCOP 1.75
  
• d6gsub1 appears in the current release, SCOPe 2.08