› 3zzn

X-ray diffraction
2.9Å resolution

5-Mutant (R79W, R151A, E279A, E299A,E313A) Lactate-Dehydrogenase from Thermus thermophillus

Released:
DOI: 10.2210/pdb3zzn/pdb
PDB entry 3zzn coloured by chain, front view.
PDB entry 3zzn coloured by chain, side view.
PDB entry 3zzn 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: 32.6 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

1 bound ligand:
Ligand ADP 2 x ADP
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-4
Spacegroup: C2
Unit cell:
a: 157.123Å b: 59.597Å c: 153.076Å
α: 90° β: 93.37° γ: 90°
R-values:
R R work R free
0.192 0.188 0.251
Expression system: Escherichia coli DH5[alpha]

Quick links

Citations

4 review citations

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