Lineage for d1powa3 (1pow A:366-593)

  1. Root: SCOP 1.65
  2. 305035Class c: Alpha and beta proteins (a/b) [51349] (121 folds)
  3. 312976Fold 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. 312977Superfamily 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. 313084Family c.36.1.9: Pyruvate oxidase and decarboxylase PP module [88749] (5 proteins)
    the N-terminal, Pyr module is separated from the C-terminal, PP module by an alpa/beta domain of Rossmann-like topology
  6. 313130Protein Pyruvate oxidase [88754] (1 species)
  7. 313131Species Lactobacillus plantarum [TaxId:1590] [88755] (2 PDB entries)
  8. 313134Domain d1powa3: 1pow A:366-593 [31798]
    Other proteins in same PDB: d1powa1, d1powa2, d1powb1, d1powb2

Details for d1powa3

PDB Entry: 1pow (more details), 2.5 Å

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

SCOP Domain Sequences for d1powa3:

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

>d1powa3 c.36.1.9 (A:366-593) Pyruvate oxidase {Lactobacillus plantarum}
kqegplqayqvlravnkiaepdaiysidvgdinlnanrhlkltpsnrhitsnlfatmgvg
ipgaiaaklnyperqvfnlagdggasmtmqdlatqvqyhlpvinvvftncqygfikdeqe
dtnqndfigvefndidfskiadgvhmqafrvnkieqlpdvfeqakaiaqhepvlidavit
gdrplpaeklrldsamssaadieafkqryeaqdlqplstylkqfgldd

SCOP Domain Coordinates for d1powa3:

Click to download the PDB-style file with coordinates for d1powa3.
(The format of our PDB-style files is described here.)

Timeline for d1powa3: