8hs0

X-ray diffraction
1.42Å resolution

The mutant structure of DHAD V178W

Released:

Function and Biology Details

Reaction catalysed:
2,3-dihydroxy-3-methylbutanoate = 3-methyl-2-oxobutanoate + H(2)O
Biochemical function:
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
PDBe Complex ID:
PDB-CPX-192280 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Dihydroxy-acid dehydratase, chloroplastic Chain: A
Molecule details ›
Chain: A
Length: 574 amino acids
Theoretical weight: 61.23 KDa
Source organism: Arabidopsis thaliana
Expression system: Escherichia coli K-12
UniProt:
  • Canonical: Q9LIR4 (Residues: 36-608; Coverage: 94%)
Gene names: At3g23940, DHAD, F14O13.13
Sequence domains: Dehydratase family

Ligands and Environments

3 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRF BEAMLINE BL19U1
Spacegroup: P42212
Unit cell:
a: 135.92Å b: 135.92Å c: 66.35Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.182 0.181 0.197
Expression system: Escherichia coli K-12