SCOP 1.63: Domain d1lbkb1: 1lbk B:77-208

Lineage for d1lbkb1 (1lbk B:77-208)

1. Root: SCOP 1.63

2. Class a: All alpha proteins [46456] (171 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] (15 proteins)

6. Protein Class pi GST [81347] (3 species)

7. Species Human (Homo sapiens) [TaxId:9606] [47619] (33 PDB entries)

8. Domain d1lbkb1: 1lbk B:77-208 [73811]
   Other proteins in same PDB: d1lbka2, d1lbkb2
   complexed with gsh, mes, so4

Details for d1lbkb1

PDB Entry: 1lbk, 1.86 Å

PDB Description: crystal structure of a recombinant glutathione transferase, created by replacing the last seven residues of each subunit of the human class pi isoenzyme with the additional c-terminal helix of human class alpha isoenzyme

SCOP Domain Sequences for d1lbkb1:

Sequence; same for both SEQRES and ATOM records:

>d1lbkb1 a.45.1.1 (B:77-208) Class pi GST {Human (Homo sapiens)}
glygkdqqeaalvdmvndgvedlrckyisliytnyeagkddyvkalpgqlkpfetllsqn
qggktfivgdqisfadynlldlllihevlapgcldafpllsayvgrlsarpklkaflasp
eyvnlpmdeksl

Timeline for d1lbkb1:

• d1lbkb1 first appeared in SCOP 1.61
  
• d1lbkb1 appears in SCOP 1.65
  
• d1lbkb1 appears in the current release, SCOPe 2.08