› 1bmd

X-ray diffraction
1.9Å resolution

DETERMINANTS OF PROTEIN THERMOSTABILITY OBSERVED IN THE 1.9 ANGSTROMS CRYSTAL STRUCTURE OF MALATE DEHYDROGENASE FROM THE THERMOPHILIC BACTERIUM THERMUS FLAVUS

Released:
DOI: 10.2210/pdb1bmd/pdb
PDB entry 1bmd coloured by chain, front view.
PDB entry 1bmd coloured by chain, side view.
PDB entry 1bmd 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: 35.45 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 NAD 2 x NAD
No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P212121
Unit cell:
a: 71.51Å b: 87.59Å c: 118.98Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.154 0.154 not available
Expression system: Not provided

Quick links

Citations

8 review citations

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

7 mentions without citation

Building collagen IV smart scaffolds on the outside of cells.
Brown et al. (2017)
6 more