X-ray diffraction
2.3Å resolution

The crystal structure of Klebsiella pneumoniae acetolactate synthase with enzyme-bound cofactors


Function and Biology Details

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Entry contents:
1 distinct polypeptide molecule
Acetolactate synthase, catabolic Chains: A, B
Molecule details ›
Chains: A, B
Length: 566 amino acids
Theoretical weight: 61.36 KDa
Source organism: Klebsiella pneumoniae
Expression system: Escherichia coli BL21(DE3)
  • Canonical: P27696 (Residues: 1-559; Coverage: 100%)
Gene names: budB, ilvK
Sequence domains:
Structure domains:

Ligands and Environments

Cofactor: Ligand TPP 2 x TPP
3 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 14-BM-D
Spacegroup: C2221
Unit cell:
a: 116.822Å b: 160.573Å c: 129.374Å
α: 90° β: 90° γ: 90°
R R work R free
0.165 0.165 0.214
Expression system: Escherichia coli BL21(DE3)