Lineage for d1po7a2 (1po7 A:2-181)

  1. Root: SCOPe 2.08
  2. Class c: Alpha and beta proteins (a/b) [51349] (148 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] (9 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. Family c.36.1.5: Pyruvate oxidase and decarboxylase Pyr module [88724] (8 proteins)
    the N-terminal, Pyr module is separated from the C-terminal, PP module by an alpha/beta domain of Rossmann-like topology
    automatically mapped to Pfam PF02776
  6. Protein Benzoylformate decarboxylase [88731] (1 species)
  7. Species Pseudomonas putida [TaxId:303] [88732] (7 PDB entries)
    Uniprot P20906
  8. Domain d1po7a2: 1po7 A:2-181 [111637]
    Other proteins in same PDB: d1po7a1, d1po7a3
    complexed with ca, mg, tzd; mutant

Details for d1po7a2

PDB Entry: 1po7 (more details), 1.2 Å

PDB Description: high resolution structure of e28a mutant benzoylformate decarboxylase from pseudomonas putida
PDB Compounds: (A:) Benzoylformate decarboxylase

SCOPe Domain Sequences for d1po7a2:

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

>d1po7a2 c.36.1.5 (A:2-181) Benzoylformate decarboxylase {Pseudomonas putida [TaxId: 303]}
asvhgttyellrrqgidtvfgnpgsnalpflkdfpedfryilalqeacvvgiadgyaqas
rkpafinlhsaagtgnamgalsnawnshsplivtagqqtramigvealltnvdaanlprp
lvkwsyepasaaevphamsraihmasmapqgpvylsvpyddwdkdadpqshhlfdrhvss

SCOPe Domain Coordinates for d1po7a2 are not available.

Timeline for d1po7a2:

View in 3D
Domains from same chain:
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d1po7a1, d1po7a3