Lineage for d1ozha2 (1ozh A:7-187)

  1. Root: SCOP 1.69
  2. 473232Class c: Alpha and beta proteins (a/b) [51349] (136 folds)
  3. 483377Fold 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. 483378Superfamily 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. 483379Family 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. 483421Protein Catabolic acetolactate synthase [102328] (1 species)
  7. 483422Species Klebsiella pneumoniae [TaxId:573] [102329] (3 PDB entries)
  8. 483423Domain d1ozha2: 1ozh A:7-187 [93834]
    Other proteins in same PDB: d1ozha1, d1ozha3, d1ozhb1, d1ozhb3, d1ozhc1, d1ozhc3, d1ozhd1, d1ozhd3

Details for d1ozha2

PDB Entry: 1ozh (more details), 2 Å

PDB Description: The crystal structure of Klebsiella pneumoniae acetolactate synthase with enzyme-bound cofactor and with an unusual intermediate.

SCOP Domain Sequences for d1ozha2:

Sequence, based on SEQRES records: (download)

>d1ozha2 c.36.1.5 (A:7-187) Catabolic acetolactate synthase {Klebsiella pneumoniae}

Sequence, based on observed residues (ATOM records): (download)

>d1ozha2 c.36.1.5 (A:7-187) Catabolic acetolactate synthase {Klebsiella pneumoniae}

SCOP Domain Coordinates for d1ozha2:

Click to download the PDB-style file with coordinates for d1ozha2.
(The format of our PDB-style files is described here.)

Timeline for d1ozha2: