Lineage for d1poxb3 (1pox B:366-593)

  1. Root: SCOP 1.67
  2. 383641Class c: Alpha and beta proteins (a/b) [51349] (130 folds)
  3. 393047Fold 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. 393048Superfamily c.36.1: Thiamin diphosphate-binding fold (THDP-binding) [52518] (8 families) (S)
    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. 393191Family c.36.1.9: Pyruvate oxidase and decarboxylase PP module [88749] (7 proteins)
    the N-terminal, Pyr module is separated from the C-terminal, PP module by an alpa/beta domain of Rossmann-like topology
  6. 393263Protein Pyruvate oxidase [88754] (1 species)
  7. 393264Species Lactobacillus plantarum [TaxId:1590] [88755] (2 PDB entries)
  8. 393266Domain d1poxb3: 1pox B:366-593 [31796]
    Other proteins in same PDB: d1poxa1, d1poxa2, d1poxb1, d1poxb2
    complexed with fad, gol, mg, na, tpp; mutant

Details for d1poxb3

PDB Entry: 1pox (more details), 2.1 Å

PDB Description: the refined structures of a stabilized mutant and of wild-type pyruvate oxidase from lactobacillus plantarum

SCOP Domain Sequences for d1poxb3:

Sequence; same for both SEQRES and ATOM records: (download)

>d1poxb3 c.36.1.9 (B:366-593) Pyruvate oxidase {Lactobacillus plantarum}

SCOP Domain Coordinates for d1poxb3:

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Timeline for d1poxb3: