1uxh

X-ray diffraction
2.1Å resolution

Large improvement in the thermal stability of a tetrameric malate dehydrogenase by single point mutations at the dimer-dimer interface

Released:

Function and Biology Details

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-160336 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Malate dehydrogenase Chains: A, B
Molecule details ›
Chains: A, B
Length: 309 amino acids
Theoretical weight: 32.75 KDa
Source organism: Chloroflexus aurantiacus
Expression system: Escherichia coli
UniProt:
  • Canonical: P80040 (Residues: 1-309; Coverage: 100%)
Gene names: Caur_0900, mdh
Sequence domains:
Structure domains:

Ligands and Environments


Cofactor: Ligand NAD 2 x NAD
1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE BM1A
Spacegroup: P43212
Unit cell:
a: 149.79Å b: 149.79Å c: 111.264Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.235 0.235 0.262
Expression system: Escherichia coli