Lineage for d1q6za2 (1q6z A:2-181)

  1. Root: SCOP 1.71
  2. 570216Class c: Alpha and beta proteins (a/b) [51349] (134 folds)
  3. 581036Fold 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. 581037Superfamily 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. 581038Family c.36.1.5: Pyruvate oxidase and decarboxylase Pyr module [88724] (7 proteins)
    the N-terminal, Pyr module is separated from the C-terminal, PP module by an alpha/beta domain of Rossmann-like topology
  6. 581055Protein Benzoylformate decarboxylase [88731] (1 species)
  7. 581056Species Pseudomonas putida [TaxId:303] [88732] (5 PDB entries)
  8. 581057Domain d1q6za2: 1q6z A:2-181 [111656]
    Other proteins in same PDB: d1q6za1, d1q6za3
    complexed with ca, mg, tdp; mutant

Details for d1q6za2

PDB Entry: 1q6z (more details), 1 Å

PDB Description: high resolution structure of e28a mutant benzoylformate decarboxylase from pseudomonas putida complexed with thiamin thiazolone diphosphate

SCOP Domain Sequences for d1q6za2:

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

>d1q6za2 c.36.1.5 (A:2-181) Benzoylformate decarboxylase {Pseudomonas putida}

SCOP Domain Coordinates for d1q6za2:

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Timeline for d1q6za2: