› 3vph

X-ray diffraction
2Å resolution

L-lactate dehydrogenase from Thermus caldophilus GK24 complexed with oxamate, NADH and FBP

Released:
DOI: 10.2210/pdb3vph/pdb
PDB entry 3vph coloured by chain, front view.
PDB entry 3vph coloured by chain, side view.
PDB entry 3vph coloured by chain, top view.
Source organism: Thermus caldophilus
Primary publication:
The core of allosteric motion in Thermus caldophilus L-lactate dehydrogenase.
Ikehara Y, Arai K, Furukawa N, Ohno T, Miyake T, Fushinobu S, Nakajima M, Miyanaga A, Taguchi H
J Biol Chem 289 31550-64 (2014)
PMID: 25258319

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-138887 (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: 32.82 KDa
Source organism: Thermus caldophilus
Expression system: Escherichia coli
UniProt:
  • Canonical: P06150 (Residues: 1-310; Coverage: 100%)
Gene name: ldh
Sequence domains:
Structure domains:

Ligands and Environments


Cofactor: Ligand NAD 3 x NAD
3 bound ligands:
Ligand OXM 4 x OXM
Ligand FBP 2 x FBP
Ligand GOL 4 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PHOTON FACTORY BEAMLINE BL-6A
Spacegroup: C2
Unit cell:
a: 146.738Å b: 67.843Å c: 147.343Å
α: 90° β: 94.02° γ: 90°
R-values:
R R work R free
0.209 0.209 0.246
Expression system: Escherichia coli

Quick links

Citations

3 citation in other articles

Mechanistic insights into the allosteric regulation of bacterial ADP-glucose pyrophosphorylases.
Comino et al. (2017)
2 more

1 mention without citation

The core of allosteric motion in Thermus caldophilus L-lactate dehydrogenase.
Ikehara et al. (2014)