SCOP 1.73: Domain d1lbkb2: 1lbk B:1-76

Lineage for d1lbkb2 (1lbk B:1-76)

1. Root: SCOP 1.73

2. Class c: Alpha and beta proteins (a/b) [51349] (141 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] (22 families)

5. Family c.47.1.5: Glutathione S-transferase (GST), N-terminal domain [52862] (18 proteins)

6. Protein Class pi GST [81358] (4 species)

7. Species Human (Homo sapiens) [TaxId:9606] [52864] (39 PDB entries)

8. Domain d1lbkb2: 1lbk B:1-76 [73812]
   Other proteins in same PDB: d1lbka1, d1lbkb1
   complexed with gsh, mes, so4

Details for d1lbkb2

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

PDB Compounds: (B:) Glutathione S-transferase class pi chimaera (CODA)

SCOP Domain Sequences for d1lbkb2:

Sequence; same for both SEQRES and ATOM records:

>d1lbkb2 c.47.1.5 (B:1-76) Class pi GST {Human (Homo sapiens) [TaxId: 9606]}
ppytvvyfpvrgrcaalrmlladqgqswkeevvtvetwqegslkasclygqlpkfqdgdl
tlyqsntilrhlgrtl

Timeline for d1lbkb2:

• d1lbkb2 first appeared in SCOP 1.61
  
• d1lbkb2 appears in SCOP 1.71
  
• d1lbkb2 appears in SCOP 1.75
  
• d1lbkb2 appears in the current release, SCOPe 2.08