› 2uxr

X-ray diffraction
2.3Å resolution

Complex with isocitrate and the protein isocitrate dehydrogenase from the psychrophilic bacterium Desulfotalea psychrophila

Released:
DOI: 10.2210/pdb2uxr/pdb
PDB entry 2uxr coloured by chain, front view.
PDB entry 2uxr coloured by chain, side view.
PDB entry 2uxr coloured by chain, top view.
Source organism: Desulfotalea psychrophila
Primary publication:
Structural and functional properties of isocitrate dehydrogenase from the psychrophilic bacterium Desulfotalea psychrophila reveal a cold-active enzyme with an unusual high thermal stability.
Fedøy AE, Yang N, Martinez A, Leiros HK, Steen IH
J Mol Biol 372 130-49 (2007)
PMID: 17632124

Function and Biology Details

Reaction catalysed: 
(1a) isocitrate + NADP(+) = 2-oxalosuccinate + NADPH
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-179398 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Isocitrate dehydrogenase [NADP] Chains: A, B
Molecule details ›
Chains: A, B
Length: 402 amino acids
Theoretical weight: 45.65 KDa
Source organism: Desulfotalea psychrophila
Expression system: Escherichia coli
UniProt:
  • Canonical: Q6AQ66 (Residues: 1-402; Coverage: 100%)
Gene name: DP0778
Sequence domains: Isocitrate/isopropylmalate dehydrogenase
Structure domains: Isopropylmalate Dehydrogenase

Ligands and Environments

3 bound ligands:
Ligand ICT 3 x ICT
Ligand MG 3 x MG
Ligand GOL 1 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-2
Spacegroup: C2221
Unit cell:
a: 58.56Å b: 121.74Å c: 273.77Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.199 0.195 0.259
Expression system: Escherichia coli

Quick links

Citations

8 review citations

Psychrophilic enzymes: from folding to function and biotechnology.
Feller G. (2013)
7 more

3 mentions without citation

Discovery, Molecular Mechanisms, and Industrial Applications of Cold-Active Enzymes.
Santiago et al. (2016)
2 more