› 1llc

X-ray diffraction
3Å resolution

STRUCTURE DETERMINATION OF THE ALLOSTERIC L-LACTATE DEHYDROGENASE FROM LACTOBACILLUS CASEI AT 3.0 ANGSTROMS RESOLUTION

Released:
DOI: 10.2210/pdb1llc/pdb
PDB entry 1llc coloured by chain, front view.
PDB entry 1llc coloured by chain, side view.
PDB entry 1llc coloured by chain, top view.
Source organism: Lacticaseibacillus casei
Primary publication:
STRUCTURE DETERMINATION OF THE ALLOSTERIC L-LACTATE DEHYDROGENASE FROM LACTOBACILLUS-CASEI AT 3A RESOLUTION.
Buehner M, Hecht HJ
Acta Crystallogr., A, Found. Crystallogr. 40 32-32 (1984)

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-132418 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
L-lactate dehydrogenase Chain: A
Molecule details ›
Chain: A
Length: 325 amino acids
Theoretical weight: 35.48 KDa
Source organism: Lacticaseibacillus casei
Expression system: Not provided
UniProt:
  • Canonical: P00343 (Residues: 2-326; Coverage: 100%)
Gene name: ldh
Sequence domains:
Structure domains:

Ligands and Environments

2 bound ligands:
Ligand AFP 1 x AFP
Ligand SO4 1 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: C2
Unit cell:
a: 169.2Å b: 85.38Å c: 180.18Å
α: 90° β: 91.3° γ: 90°
R-values:
R R work R free
0.374 0.374 not available
Expression system: Not provided

Quick links

Citations

1 mention without citation

Evolutionary plasticity of protein families: coupling between sequence and structure variation.
Panchenko et al. (2005)