› 4okn

X-ray diffraction
2.1Å resolution

Crystal structure of human muscle L-lactate dehydrogenase, ternary complex with NADH and oxalate

Released:
DOI: 10.2210/pdb4okn/pdb
PDB entry 4okn coloured by chain, front view.
PDB entry 4okn coloured by chain, side view.
PDB entry 4okn coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structures of lactate dehydrogenase A (LDHA) in apo, ternary and inhibitor-bound forms.
Kolappan S, Shen DL, Mosi R, Sun J, McEachern EJ, Vocadlo DJ, Craig L
Acta Crystallogr D Biol Crystallogr 71 185-95 (2015)
PMID: 25664730

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-132412 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
L-lactate dehydrogenase A chain Chains: A, B, C, D, E, F, G, H
Molecule details ›
Chains: A, B, C, D, E, F, G, H
Length: 337 amino acids
Theoretical weight: 37.43 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P00338 (Residues: 2-332; Coverage: 100%)
Gene names: LDHA, PIG19
Sequence domains:
Structure domains:

Ligands and Environments


Cofactor: Ligand NAI 7 x NAI
3 bound ligands:
Ligand OXL 8 x OXL
Ligand SO4 9 x SO4
Ligand KAN 1 x KAN
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL7-1
Spacegroup: P212121
Unit cell:
a: 65.55Å b: 159.62Å c: 266.16Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.208 0.206 0.245
Expression system: Escherichia coli

Quick links

Citations

5 review citations

MYC, Metabolism, and Cancer.
Stine et al. (2015)
4 more

6 mentions without citation

Small Molecule-Based Enzyme Inhibitors in the Treatment of Primary Hyperoxalurias.
Moya-Garzon et al. (2021)
5 more