› 8imu

X-ray diffraction
1.93Å resolution

Dihydroxyacid dehydratase (DHAD) mutant-V497F

Released:
DOI: 10.2210/pdb8imu/pdb
PDB entry 8imu coloured by chain, front view.
PDB entry 8imu coloured by chain, side view.
PDB entry 8imu coloured by chain, top view.
Source organism: Arabidopsis thaliana
Primary publication:
Structural Bases of Dihydroxy Acid Dehydratase Inhibition and Biodesign for Self-Resistance.
Zang X, Bat-Erdene U, Huang W, Wu Z, Jacobsen SE, Tang Y, Zhou J
Biodes Res 6 0046 (2024)
PMID: 39494391

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)
Assembly name:
PDBe Complex ID:
PDB-CPX-192280 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Dihydroxy-acid dehydratase, chloroplastic Chains: A, B
Molecule details ›
Chains: A, B
Length: 574 amino acids
Theoretical weight: 61.19 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:
Ligand FES 2 x FES
Ligand ACT 2 x ACT
Ligand GOL 2 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRF BEAMLINE BL19U1
Spacegroup: P41212
Unit cell:
a: 135.12Å b: 135.12Å c: 136.44Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.183 0.182 0.208
Expression system: Escherichia coli K-12

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