› 3ulk

X-ray diffraction
2.3Å resolution

E. coli Ketol-acid reductoisomerase in complex with NADPH and Mg2+

Released:
DOI: 10.2210/pdb3ulk/pdb
PDB entry 3ulk coloured by chain, front view.
PDB entry 3ulk coloured by chain, side view.
PDB entry 3ulk coloured by chain, top view.
Source organism: Escherichia coli K-12
Primary publication:
Bacterial and plant ketol-acid reductoisomerases have different mechanisms of induced fit during the catalytic cycle.
Wong SH, Lonhienne TG, Winzor DJ, Schenk G, Guddat LW
J Mol Biol 424 168-79 (2012)
PMID: 23036858

Function and Biology Details

Reaction catalysed: 
(2R)-2,3-dihydroxy-3-methylbutanoate + NADP(+) = (2S)-2-hydroxy-2-methyl-3-oxobutanoate + NADPH
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-138776 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Ketol-acid reductoisomerase (NADP(+)) Chains: A, B
Molecule details ›
Chains: A, B
Length: 491 amino acids
Theoretical weight: 54.15 KDa
Source organism: Escherichia coli K-12
Expression system: Escherichia coli
UniProt:
  • Canonical: P05793 (Residues: 1-491; Coverage: 100%)
Gene names: JW3747, b3774, ilvC
Sequence domains:
Structure domains:

Ligands and Environments


Cofactor: Ligand NDP 2 x NDP
2 bound ligands:
Ligand SO4 9 x SO4
Ligand MG 4 x MG
1 modified residue:
Ligand CSX 2 x CSX

Experiments and Validation Details

Entry percentile scores
X-ray source: AUSTRALIAN SYNCHROTRON BEAMLINE MX1
Spacegroup: P6422
Unit cell:
a: 144.459Å b: 144.459Å c: 217.545Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.18 0.174 0.236
Expression system: Escherichia coli

Quick links

Citations

9 citation in other articles

Crystal structure of Mycobacterium tuberculosis ketol-acid reductoisomerase at 1.0 Å resolution - a potential target for anti-tuberculosis drug discovery.
Lv et al. (2016)
8 more

5 mentions without citation

Chemical approaches to detect and analyze protein sulfenic acids.
Furdui et al. (2014)
4 more