› 1bdm

X-ray diffraction
1.8Å resolution

THE STRUCTURE AT 1.8 ANGSTROMS RESOLUTION OF A SINGLE SITE MUTANT (T189I) OF MALATE DEHYDROGENASE FROM THERMUS FLAVUS WITH INCREASED ENZYMATIC ACTIVITY

Released:
DOI: 10.2210/pdb1bdm/pdb
PDB entry 1bdm coloured by chain, front view.
PDB entry 1bdm coloured by chain, side view.
PDB entry 1bdm coloured by chain, top view.
Source organism: Thermus thermophilus
Primary publication:
Determinants of protein thermostability observed in the 1.9-A crystal structure of malate dehydrogenase from the thermophilic bacterium Thermus flavus.
Kelly CA, Nishiyama M, Ohnishi Y, Beppu T, Birktoft JJ
Biochemistry 32 3913-22 (1993)
PMID: 8471603

Function and Biology Details

Reaction catalysed: 
(S)-malate + NAD(+) = oxaloacetate + NADH
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:
Structure domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-145339 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Malate dehydrogenase Chains: A, B
Molecule details ›
Chains: A, B
Length: 327 amino acids
Theoretical weight: 35.46 KDa
Source organism: Thermus thermophilus
Expression system: Not provided
UniProt:
  • Canonical: P10584 (Residues: 1-327; Coverage: 100%)
Gene name: mdh
Sequence domains:
Structure domains:

Ligands and Environments


Cofactor: Ligand NAX 2 x NAX
No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P212121
Unit cell:
a: 71.75Å b: 88.64Å c: 118.97Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.169 0.169 not available
Expression system: Not provided

Quick links

Citations

9 review citations

Disulfide bonds and the stability of globular proteins.
Betz SF. (1993)
8 more

4 mentions without citation

Comparative Protein Structure Modeling Using MODELLER.
Webb et al. (2016)
3 more