› 4a73

X-ray diffraction
3Å resolution

SINGLE POINT MUTANT OF THERMUS THERMOPHILUS LACTATE DEHYDROGENASE

Released:
DOI: 10.2210/pdb4a73/pdb
PDB entry 4a73 coloured by chain, front view.
PDB entry 4a73 coloured by chain, side view.
PDB entry 4a73 coloured by chain, top view.
Source organism: Thermus thermophilus HB8
Primary publication:
Sampling the conformational energy landscape of a hyperthermophilic protein by engineering key substitutions.
Colletier JP, Aleksandrov A, Coquelle N, Mraihi S, Mendoza-Barberá E, Field M, Madern D
Mol Biol Evol 29 1683-94 (2012)
PMID: 22319152

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-178009 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
L-lactate dehydrogenase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 310 amino acids
Theoretical weight: 32.74 KDa
Source organism: Thermus thermophilus HB8
Expression system: Escherichia coli DH5[alpha]
UniProt:
  • Canonical: Q5SJA1 (Residues: 1-310; Coverage: 100%)
Gene names: TTHA1113, ldh
Sequence domains:
Structure domains:

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-1
Spacegroup: P61
Unit cell:
a: 158.04Å b: 158.04Å c: 142.11Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.173 0.17 0.235
Expression system: Escherichia coli DH5[alpha]

Quick links

Citations

4 review citations

Stabilizing biocatalysts.
Bommarius et al. (2013)
3 more

1 mention without citation

The core of allosteric motion in Thermus caldophilus L-lactate dehydrogenase.
Ikehara et al. (2014)