› 1hqs

X-ray diffraction
1.55Å resolution

CRYSTAL STRUCTURE OF ISOCITRATE DEHYDROGENASE FROM BACILLUS SUBTILIS

Released:
DOI: 10.2210/pdb1hqs/pdb
PDB entry 1hqs coloured by chain, front view.
PDB entry 1hqs coloured by chain, side view.
PDB entry 1hqs coloured by chain, top view.
Source organism: Bacillus subtilis
Primary publication:
Crystal structure of Bacillus subtilis isocitrate dehydrogenase at 1.55 A. Insights into the nature of substrate specificity exhibited by Escherichia coli isocitrate dehydrogenase kinase/phosphatase.
Singh SK, Matsuno K, LaPorte DC, Banaszak LJ
J Biol Chem 276 26154-63 (2001)
PMID: 11290745

Function and Biology Details

Reaction catalysed: 
(1a) isocitrate + NADP(+) = 2-oxalosuccinate + NADPH
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-153838 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Isocitrate dehydrogenase [NADP] Chains: A, B
Molecule details ›
Chains: A, B
Length: 423 amino acids
Theoretical weight: 46.54 KDa
Source organism: Bacillus subtilis
Expression system: Escherichia coli
UniProt:
  • Canonical: P39126 (Residues: 1-423; Coverage: 100%)
Gene names: BSU29130, citC, icd
Sequence domains: Isocitrate/isopropylmalate dehydrogenase
Structure domains: Isopropylmalate Dehydrogenase

Ligands and Environments

3 bound ligands:
Ligand CIT 2 x CIT
Ligand PGO 5 x PGO
Ligand PGR 2 x PGR
1 modified residue:
Ligand CME 2 x CME

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-ID
Spacegroup: P21
Unit cell:
a: 73.69Å b: 73.29Å c: 80.9Å
α: 90° β: 109.48° γ: 90°
R-values:
R R work R free
0.202 0.202 0.249
Expression system: Escherichia coli

Quick links

Citations

1 review citation

Exploring the diversity of protein modifications: special bacterial phosphorylation systems.
Mijakovic et al. (2016)
32 other articles

8 mentions without citation

Lysine acetylation is a highly abundant and evolutionarily conserved modification in Escherichia coli.
Zhang et al. (2009)
7 more