Lineage for d1ozfb3 (1ozf B:367-554)

  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.36.1.9: Pyruvate oxidase and decarboxylase PP module [88749] (8 proteins)
    the N-terminal, Pyr module is separated from the C-terminal, PP module by an alpa/beta domain of Rossmann-like topology
  6. Protein Catabolic acetolactate synthase [102333] (1 species)
  7. Species Klebsiella pneumoniae [TaxId:573] [102334] (3 PDB entries)
  8. Domain d1ozfb3: 1ozf B:367-554 [93826]
    Other proteins in same PDB: d1ozfa1, d1ozfa2, d1ozfb1, d1ozfb2
    complexed with mg, peg, po4, tpp

Details for d1ozfb3

PDB Entry: 1ozf (more details), 2.3 Å

PDB Description: The crystal structure of Klebsiella pneumoniae acetolactate synthase with enzyme-bound cofactors
PDB Compounds: (B:) Acetolactate synthase, catabolic

SCOPe Domain Sequences for d1ozfb3:

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

>d1ozfb3 c.36.1.9 (B:367-554) Catabolic acetolactate synthase {Klebsiella pneumoniae [TaxId: 573]}

SCOPe Domain Coordinates for d1ozfb3 are not available.

Timeline for d1ozfb3:

Domains from same chain:
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d1ozfb1, d1ozfb2
Domains from other chains:
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d1ozfa1, d1ozfa2, d1ozfa3