› 2v65

X-ray diffraction
2.35Å resolution

Apo LDH from the psychrophile C. gunnari

Released:
DOI: 10.2210/pdb2v65/pdb
PDB entry 2v65 coloured by chain, front view.
PDB entry 2v65 coloured by chain, side view.
PDB entry 2v65 coloured by chain, top view.
Source organism: Champsocephalus gunnari
Primary publication:
Activity, stability and structural studies of lactate dehydrogenases adapted to extreme thermal environments.
Coquelle N, Fioravanti E, Weik M, Vellieux F, Madern D
J Mol Biol 374 547-62 (2007)
PMID: 17936781

Function and Biology Details

Reaction catalysed: 
(S)-lactate + NAD(+) = pyruvate + NADH
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-131667 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
L-lactate dehydrogenase A chain Chains: A, B
Molecule details ›
Chains: A, B
Length: 331 amino acids
Theoretical weight: 36.2 KDa
Source organism: Champsocephalus gunnari
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: O93541 (Residues: 1-331; Coverage: 100%)
Gene name: ldha
Sequence domains:
Structure domains:

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE BM30A
Spacegroup: C222
Unit cell:
a: 113.79Å b: 113.79Å c: 109.9Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.228 0.228 0.241
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

4 review citations

Optimization to low temperature activity in psychrophilic enzymes.
Struvay et al. (2012)
3 more

5 mentions without citation

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