› 2hjr

X-ray diffraction
2.2Å resolution

Function and Biology Details

Reaction catalysed: 
(S)-lactate + NAD(+) = pyruvate + NADH
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assemblies composition:
homo dimer (preferred)
homo tetramer
Assembly name:
PDBe Complex ID:
PDB-CPX-176954 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
L-lactate dehydrogenase Chains: A, B, C, D, E, F, G, H, I, J, K, L
Molecule details ›
Chains: A, B, C, D, E, F, G, H, I, J, K, L
Length: 328 amino acids
Theoretical weight: 35.11 KDa
Source organism: Cryptosporidium parvum
Expression system: Escherichia coli
UniProt:
  • Canonical: Q5CYZ3 (Residues: 1-328; Coverage: 100%)
Gene name: cgd7_470
Sequence domains:
Structure domains:

Ligands and Environments

2 bound ligands:
Ligand CIT 12 x CIT
Ligand APR 12 x APR
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU
Spacegroup: P32
Unit cell:
a: 171.887Å b: 171.887Å c: 135.606Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.2 0.198 0.247
Expression system: Escherichia coli

Quick links

Citations

34 review citations

Structure-based insights into the catalytic power and conformational dexterity of peroxiredoxins.
Hall et al. (2011)
33 more

4 mentions without citation

An atomic-resolution view of neofunctionalization in the evolution of apicomplexan lactate dehydrogenases.
Boucher et al. (2014)
3 more