› 1ez4

X-ray diffraction
2.3Å resolution

CRYSTAL STRUCTURE OF NON-ALLOSTERIC L-LACTATE DEHYDROGENASE FROM LACTOBACILLUS PENTOSUS AT 2.3 ANGSTROM RESOLUTION

Released:
DOI: 10.2210/pdb1ez4/pdb
PDB entry 1ez4 coloured by chain, front view.
PDB entry 1ez4 coloured by chain, side view.
PDB entry 1ez4 coloured by chain, top view.
Source organism: Lactiplantibacillus pentosus
Primary publication:
Crystal structure of non-allosteric L-lactate dehydrogenase from Lactobacillus pentosus at 2.3 A resolution: specific interactions at subunit interfaces.
Uchikoba H, Fushinobu S, Wakagi T, Konno M, Taguchi H, Matsuzawa H
Proteins 46 206-14 (2002)
PMID: 11807949

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-157477 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
L-lactate dehydrogenase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 318 amino acids
Theoretical weight: 34.04 KDa
Source organism: Lactiplantibacillus pentosus
Expression system: Escherichia coli
UniProt:
  • Canonical: P56511 (Residues: 3-320; Coverage: 99%)
Gene names: ldh, ldhL
Sequence domains:
Structure domains:

Ligands and Environments


Cofactor: Ligand NAD 4 x NAD
No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PHOTON FACTORY BEAMLINE BL-6A
Spacegroup: P212121
Unit cell:
a: 149.351Å b: 145.544Å c: 111.926Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.205 0.205 0.241
Expression system: Escherichia coli

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Citations

1 review citation

Is allostery an intrinsic property of all dynamic proteins?
Gunasekaran et al. (2004)
10 other articles

2 mentions without citation

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