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

  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. 483525Family c.36.1.9: Pyruvate oxidase and decarboxylase PP module [88749] (7 proteins)
    the N-terminal, Pyr module is separated from the C-terminal, PP module by an alpa/beta domain of Rossmann-like topology
  6. 483567Protein Catabolic acetolactate synthase [102333] (1 species)
  7. 483568Species Klebsiella pneumoniae [TaxId:573] [102334] (3 PDB entries)
  8. 483574Domain d1ozfb3: 1ozf B:367-554 [93826]
    Other proteins in same PDB: d1ozfa1, d1ozfa2, d1ozfb1, d1ozfb2

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

SCOP 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}
nqfalhplrivramqdivnsdvtltvdmgsfhiwiarylytfrarqvmisngqqtmgval
pwaigawlvnperkvvsvsgdggflqssmeletavrlkanvlhliwvdngynmvaiqeek
kyqrlsgvefgpmdfkayaesfgakgfavesaealeptlraamdvdgpavvaipvdyrdn
pllmgqlh

SCOP Domain Coordinates for d1ozfb3:

Click to download the PDB-style file with coordinates for d1ozfb3.
(The format of our PDB-style files is described here.)

Timeline for d1ozfb3: