2OHX

REFINED CRYSTAL STRUCTURE OF LIVER ALCOHOL DEHYDROGENASE-NADH COMPLEX AT 1.8 ANGSTROMS RESOLUTION

Summary for 2OHX

• Entry DOI: 10.2210/pdb2ohx/pdb
• Descriptor: ALCOHOL DEHYDROGENASE, ZINC ION, NICOTINAMIDE-ADENINE-DINUCLEOTIDE, ... (5 entities in total)
• Functional Keywords: oxidoreductase(nad(a)-choh(d))
• Biological source: Equus caballus (horse)
• Cellular location: Cytoplasm: P00327
• Total number of polymer chains: 2
• Total formula weight: 81451.30

Authors

Al-Karadaghi, S.,Cedergren-Zeppezauer, E.S. (deposition date: 1993-08-24, release date: 1993-10-31, Last modification date: 2024-02-21)

Primary citation

Al-Karadaghi, S.,Cedergren-Zeppezauer, E.S.,Hovmoller, S.
Refined crystal structure of liver alcohol dehydrogenase-NADH complex at 1.8 A resolution.
Acta Crystallogr.,Sect.D, 50:793-807, 1994

PubMed Abstract: The crystal structure of the ternary complex of horse liver alcohol dehydrogenase (LADH) with the coenzyme NADH and inhibitor dimethyl sulfoxide (DMSO) has been refined by simulated annealing with molecular dynamics and restrained positional refinement using the program X-PLOR. The two subunits of the enzyme were refined independently. The space group was P1 with cell dimensions a = 51.8, b = 44.5, c = 94.6 A, alpha = 104.8, beta = 102.3 and gamma = 70.6 degrees. The resulting crystallographic R factor is 17.3% for 62 440 unique reflections in the resolution range 10.0-1.8 A. A total of 472 ordered solvent molecules were localized in the structure. An analysis of secondary-structure elements, solvent content and NADH binding is presented.

PubMed: 15299346
DOI: 10.1107/S0907444994005263

Experimental method

X-RAY DIFFRACTION (1.8 Å)