› 4aoy

X-ray diffraction
2.35Å resolution

Open CtIDH. The complex structures of Isocitrate dehydrogenase from Clostridium thermocellum and Desulfotalea psychrophila, support a new active site locking mechanism

Released:
DOI: 10.2210/pdb4aoy/pdb
PDB entry 4aoy coloured by chain, front view.
PDB entry 4aoy coloured by chain, side view.
PDB entry 4aoy coloured by chain, top view.
Source organism: Acetivibrio thermocellus
Primary publication:
The complex structures of isocitrate dehydrogenase from Clostridium thermocellum and Desulfotalea psychrophila suggest a new active site locking mechanism.
Leiros HK, Fedøy AE, Leiros I, Steen IH
FEBS Open Bio 2 159-72 (2012)
PMID: 23650595

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-164287 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
ISOCITRATE DEHYDROGENASE [NADP] Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 402 amino acids
Theoretical weight: 45.84 KDa
Source organism: Acetivibrio thermocellus
Structure domains: Isopropylmalate Dehydrogenase

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID29
Spacegroup: P21
Unit cell:
a: 56.13Å b: 106.84Å c: 154.5Å
α: 90° β: 93.63° γ: 90°
R-values:
R R work R free
0.211 0.21 0.258

Quick links

Citations

2 citation in other articles

Novel type II and monomeric NAD+ specific isocitrate dehydrogenases: phylogenetic affinity, enzymatic characterization, and evolutionary implication.
Wang et al. (2015)
1 more

1 mention without citation

The complex structures of isocitrate dehydrogenase from Clostridium thermocellum and Desulfotalea psychrophila suggest a new active site locking mechanism.
Leiros et al. (2012)