SCOP 1.75: Domain d2g25b1: 2g25 B:471-700

Lineage for d2g25b1 (2g25 B:471-700)

1. Root: SCOP 1.75

2. Class c: Alpha and beta proteins (a/b) [51349] (147 folds)

3. Fold c.36: Thiamin diphosphate-binding fold (THDP-binding) [52517] (1 superfamily)
   3 layers: a/b/a; parallel beta-sheet of 6 strands, order 213465

4. Superfamily c.36.1: Thiamin diphosphate-binding fold (THDP-binding) [52518] (8 families)
   there are two different functional modules of this fold: pyridine-binding (Pyr) and pyrophosphate-binding (PP) modules
   two Pyr and two PP modules assemble together in a conserved heterotetrameric core that binds two THDP coenzyme molecules

5. Family c.36.1.6: TK-like Pyr module [88735] (2 proteins)
   different order of the modules, PP module is N-terminal, Pyr module is next to it followed by a Rossmann-like domain

6. Protein Pyruvate dehydrogenase E1 component, Pyr module [88739] (1 species)
   E1A and E1B fused together in a single-chain protein

7. Species Escherichia coli [TaxId:562] [88740] (8 PDB entries)

8. Domain d2g25b1: 2g25 B:471-700 [134526]
   Other proteins in same PDB: d2g25a2, d2g25a3, d2g25b2, d2g25b3
   automatically matched to d1l8aa2
   complexed with mg, po4, tdk

Details for d2g25b1

PDB Entry: 2g25, 2.1 Å

PDB Description: e. coli pyruvate dehydrogenase phosphonolactylthiamin diphosphate complex

PDB Compounds: (B:) Pyruvate dehydrogenase E1 component

SCOP Domain Sequences for d2g25b1:

Sequence; same for both SEQRES and ATOM records:

>d2g25b1 c.36.1.6 (B:471-700) Pyruvate dehydrogenase E1 component, Pyr module {Escherichia coli [TaxId: 562]}
eklelpslqdfgalleeqskeisttiafvralnvmlknksikdrlvpiiadeartfgmeg
lfrqigiyspngqqytpqdreqvayykedekgqilqeginelgagcswlaaatsystnnl
pmipfyiyysmfgfqrigdlcwaagdqqargfliggtsgrttlngeglqhedghshiqsl
tipncisydpayayevavimhdglermygekqenvyyyittlnenyhmpa

Timeline for d2g25b1:

• d2g25b1 first appeared in SCOP 1.73
  
• d2g25b1 appears in SCOPe 2.01
  
• d2g25b1 appears in the current release, SCOPe 2.08