› 5j34

X-ray diffraction
1.83Å resolution

Isopropylmalate dehydrogenase K232M mutant

Released:
DOI: 10.2210/pdb5j34/pdb
PDB entry 5j34 coloured by chain, front view.
PDB entry 5j34 coloured by chain, side view.
PDB entry 5j34 coloured by chain, top view.
Source organism: Arabidopsis thaliana
Primary publication:
Structure and Mechanism of Isopropylmalate Dehydrogenase from Arabidopsis thaliana: INSIGHTS ON LEUCINE AND ALIPHATIC GLUCOSINOLATE BIOSYNTHESIS.
Lee SG, Nwumeh R, Jez JM
J Biol Chem 291 13421-30 (2016)
PMID: 27137927

Function and Biology Details

Reaction catalysed: 
(1a) (2R,3S)-3-isopropylmalate + NAD(+) = (2S)-2-isopropyl-3-oxosuccinate + NADH
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-161091 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
3-isopropylmalate dehydrogenase 2, chloroplastic Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 405 amino acids
Theoretical weight: 43.42 KDa
Source organism: Arabidopsis thaliana
Expression system: Escherichia coli
UniProt:
  • Canonical: P93832 (Residues: 1-405; Coverage: 100%)
Gene names: At1g80560, IMD2, IMDH, IMDH2, IPMDH2, T21F11.11
Sequence domains: Isocitrate/isopropylmalate dehydrogenase
Structure domains: Isopropylmalate Dehydrogenase

Ligands and Environments

2 bound ligands:
Ligand MG 4 x MG
Ligand SO4 6 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-ID
Spacegroup: P21
Unit cell:
a: 76.803Å b: 76.82Å c: 209.497Å
α: 90° β: 90.22° γ: 90°
R-values:
R R work R free
0.166 0.165 0.186
Expression system: Escherichia coli

Quick links

Citations

2 review citations

Promiscuity, impersonation and accommodation: evolution of plant specialized metabolism.
Leong et al. (2017)
1 more

1 mention without citation

Structure and Mechanism of Isopropylmalate Dehydrogenase from Arabidopsis thaliana: INSIGHTS ON LEUCINE AND ALIPHATIC GLUCOSINOLATE BIOSYNTHESIS.
Lee et al. (2016)