› 2v7p

X-ray diffraction
2.1Å resolution

Crystal structure of lactate dehydrogenase from Thermus Thermophilus HB8 (Holo form)

Released:
DOI: 10.2210/pdb2v7p/pdb
PDB entry 2v7p coloured by chain, front view.
PDB entry 2v7p coloured by chain, side view.
PDB entry 2v7p coloured by chain, top view.
Source organism: Thermus thermophilus HB8
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-178009 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
L-lactate dehydrogenase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 310 amino acids
Theoretical weight: 32.83 KDa
Source organism: Thermus thermophilus HB8
Expression system: Escherichia coli DH5[alpha]
UniProt:
  • Canonical: Q5SJA1 (Residues: 1-310; Coverage: 100%)
Gene names: TTHA1113, ldh
Sequence domains:
Structure domains:

Ligands and Environments


Cofactor: Ligand NAD 4 x NAD
1 bound ligand:
Ligand OXM 4 x OXM
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID23-2
Spacegroup: P212121
Unit cell:
a: 151.5Å b: 142.85Å c: 59.57Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.192 0.192 0.204
Expression system: Escherichia coli DH5[alpha]

Quick links

Citations

6 review citations

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

3 mentions without citation

Interface matters: the stiffness route to stability of a thermophilic tetrameric malate dehydrogenase.
Kalimeri et al. (2014)
2 more