Brand  (β version)

color scheme of protein:

hetatm:

x
information
centroid:
interaction residue:

chain:

Ligands
Code Name Link
CD Cadmium ion
FBP Beta-fructose-1,6-diphosphate
NAD Nicotinamide-adenine-dinucleotide
OXM Oxamic acid
Code : 1A5Z
Header : OXIDOREDUCTASE
Title : LACTATE DEHYDROGENASE FROM THERMOTOGA MARITIMA (TMLDH)
Release Data : 1999-03-23
Compound :
mol_id molecule chains
1 L-LACTATE DEHYDROGENASE A
ec: 1.1.1.27
Source :
mol_id organism_scientific expression_system
1 Thermotoga maritima  (taxid:2336) Escherichia coli  (taxid:562)
expression_system_vector_type: BACTERIUM
Authors : Auerbach, G., Ostendorp, R., Prade, L., Korndoerfer, I., Dams, T., Huber, R., Jaenicke, R.
Keywords : OXIDOREDUCTASE, GLYCOLYSIS, HYPERTHERMOPHILES, THERMOTOGA MARITIMA, PROTEIN STABILITY
Exp. method : X-RAY DIFFRACTION ( 2.1 Å )
Citation :

Lactate dehydrogenase from the hyperthermophilic bacterium thermotoga maritima: the crystal structure at 2.1 A resolution reveals strategies for intrinsic protein stabilization.

Auerbach, G.,Ostendorp, R.,Prade, L.  et al.
(1998)  Structure  6 : 769 - 781

PubMed: 9655830
DOI: 10.1016/S0969-2126(98)00078-1

Extremely Thermostable L(+)-Lactate Dehydrogenase from Thermotoga Maritima: Cloning, Characterization, and Crystallization of the Recombinant Enzyme in its Tetrameric and Octameric State

Ostendorp, R.,Auerbach, G.,Jaenicke, R.
(1996)  Protein Sci.  5 : 862

Chain : A
UniProt : P16115 (LDH_THEMA)
Reaction : (S)-lactate + NAD(+) = pyruvate + NADH.