› 1qmg

X-ray diffraction
1.6Å resolution

Acetohydroxyacid isomeroreductase complexed with its reaction product dihydroxy-methylvalerate, manganese and ADP-ribose.

Released:
DOI: 10.2210/pdb1qmg/pdb
PDB entry 1qmg coloured by chain, front view.
PDB entry 1qmg coloured by chain, side view.
PDB entry 1qmg coloured by chain, top view.
Source organism: Spinacia oleracea
Primary publication:
Structure of spinach acetohydroxyacid isomeroreductase complexed with its reaction product dihydroxymethylvalerate, manganese and (phospho)-ADP-ribose.
Thomazeau K, Dumas R, Halgand F, Forest E, Douce R, Biou V
Acta Crystallogr D Biol Crystallogr 56 389-97 (2000)
PMID: 10739911

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:
  • not assigned
Sequence domains:
Structure domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-169546 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Ketol-acid reductoisomerase, chloroplastic Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 524 amino acids
Theoretical weight: 57.05 KDa
Source organism: Spinacia oleracea
Expression system: Escherichia coli
UniProt:
  • Canonical: Q01292 (Residues: 72-595; Coverage: 88%)
Gene name: AHRI
Sequence domains:
Structure domains:

Ligands and Environments

4 bound ligands:
Ligand APX 4 x APX
Ligand MN 8 x MN
Ligand SO4 1 x SO4
Ligand DMV 4 x DMV
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE BM14
Spacegroup: P21
Unit cell:
a: 110.8Å b: 61.2Å c: 161.7Å
α: 90° β: 95° γ: 90°
R-values:
R R work R free
0.196 0.196 0.224
Expression system: Escherichia coli

Quick links

Citations

15 citation in other articles

Supra-domains: evolutionary units larger than single protein domains.
Vogel et al. (2004)
14 more

6 mentions without citation

Bacterial Branched-Chain Amino Acid Biosynthesis: Structures, Mechanisms, and Drugability.
Amorim Franco et al. (2017)
5 more