› 1a5z

X-ray diffraction
2.1Å resolution

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-147627 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
L-lactate dehydrogenase Chain: A
Molecule details ›
Chain: A
Length: 319 amino acids
Theoretical weight: 35.03 KDa
Source organism: Thermotoga maritima
Expression system: Escherichia coli
UniProt:
  • Canonical: P16115 (Residues: 1-319; Coverage: 100%)
Gene names: TM_1867, ldh
Sequence domains:
Structure domains:

Ligands and Environments


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

Experiments and Validation Details

Entry percentile scores
X-ray source: MPG/DESY, HAMBURG BEAMLINE BW6
Spacegroup: I4122
Unit cell:
a: 105.48Å b: 105.48Å c: 187.7Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.2 0.2 0.286
Expression system: Escherichia coli

Quick links

Citations

5 review citations

Hyperthermophilic enzymes: sources, uses, and molecular mechanisms for thermostability.
Vieille et al. (2001)
4 more

9 mentions without citation

PDBsum new things.
Laskowski RA. (2009)
8 more