X-ray diffraction
2.9Å resolution

Structural characterisation of the NADH binary complex of human lactate dehydrogenase M isozyme

Source organism: Homo sapiens
Primary publication:
Structural characterization of the apo form and NADH binary complex of human lactate dehydrogenase.
OpenAccess logo Acta Crystallogr. D Biol. Crystallogr. 70 1484-90 (2014)
PMID: 24816116

Function and Biology Details

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Entry contents:
1 distinct polypeptide molecule
L-lactate dehydrogenase A chain Chains: A, H
Molecule details ›
Chains: A, H
Length: 339 amino acids
Theoretical weight: 37.67 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
  • Canonical: P00338 (Residues: 2-332; Coverage: 100%)
Gene names: LDHA, PIG19
Sequence domains:
Structure domains:

Ligands and Environments

Cofactor: Ligand NAI 2 x NAI
No bound ligands

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I04-1
Spacegroup: P4122
Unit cell:
a: 84.317Å b: 84.317Å c: 276.691Å
α: 90° β: 90° γ: 90°
R R work R free
0.188 0.185 0.246
Expression system: Escherichia coli