› 1lld

X-ray diffraction
2Å resolution

MOLECULAR BASIS OF ALLOSTERIC ACTIVATION OF BACTERIAL L-LACTATE DEHYDROGENASE

Released:
DOI: 10.2210/pdb1lld/pdb
PDB entry 1lld coloured by chain, front view.
PDB entry 1lld coloured by chain, side view.
PDB entry 1lld coloured by chain, top view.
Source organism: Bifidobacterium longum subsp. longum
Primary publication:
Molecular basis of allosteric activation of bacterial L-lactate dehydrogenase.
Iwata S, Ohta T
J Mol Biol 230 21-7 (1993)
PMID: 8450537

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-123104 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
L-lactate dehydrogenase 2 Chains: A, B
Molecule details ›
Chains: A, B
Length: 319 amino acids
Theoretical weight: 34.13 KDa
Source organism: Bifidobacterium longum subsp. longum
Expression system: Not provided
UniProt:
  • Canonical: E8ME30 (Residues: 2-320; Coverage: 100%)
Gene names: BLLJ_1290, ldh2
Sequence domains:
Structure domains:

Ligands and Environments


Cofactor: Ligand NAD 2 x NAD
No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P21212
Unit cell:
a: 105.8Å b: 131.4Å c: 63.8Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.179 not available not available
Expression system: Not provided

Quick links

Citations

2 review citations

Bifidobacterium carbohydrases-their role in breakdown and synthesis of (potential) prebiotics.
van den Broek et al. (2008)
1 more

6 mentions without citation

Interaction signatures stabilizing the NAD(P)-binding Rossmann fold: a structure network approach.
Bhattacharyya et al. (2012)
5 more