› 9ldb

X-ray diffraction
2.2Å resolution

DESIGN AND SYNTHESIS OF NEW ENZYMES BASED ON THE LACTATE DEHYDROGENASE FRAMEWORK

Released:
DOI: 10.2210/pdb9ldb/pdb
PDB entry 9ldb coloured by chain, front view.
PDB entry 9ldb coloured by chain, side view.
PDB entry 9ldb coloured by chain, top view.
Source organism: Sus scrofa
Primary publication:
Design and synthesis of new enzymes based on the lactate dehydrogenase framework.
Dunn CR, Wilks HM, Halsall DJ, Atkinson T, Clarke AR, Muirhead H, Holbrook JJ
Philos Trans R Soc Lond B Biol Sci 332 177-84 (1991)
PMID: 1678537

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-132413 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
L-lactate dehydrogenase A chain Chains: A, B
Molecule details ›
Chains: A, B
Length: 332 amino acids
Theoretical weight: 36.56 KDa
Source organism: Sus scrofa
Expression system: Not provided
UniProt:
  • Canonical: P00339 (Residues: 2-332; Coverage: 100%)
Gene name: LDHA
Sequence domains:
Structure domains:

Ligands and Environments


Cofactor: Ligand NAD 2 x NAD
2 bound ligands:
Ligand SO4 3 x SO4
Ligand OXM 1 x OXM
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P21212
Unit cell:
a: 60.3Å b: 136.39Å c: 86.05Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.22 not available not available
Expression system: Not provided

Quick links

Citations

6 review citations

Protein adaptations to temperature and pressure: complementary roles of adaptive changes in amino acid sequence and internal milieu.
Somero GN. (2003)
5 more

1 mention without citation

Mechanistic Analysis of Fluorescence Quenching of Reduced Nicotinamide Adenine Dinucleotide by Oxamate in Lactate Dehydrogenase Ternary Complexes.
Peng et al. (2017)