2ohx
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(New page: 200px<br /><applet load="2ohx" size="450" color="white" frame="true" align="right" spinBox="true" caption="2ohx, resolution 1.8Å" /> '''REFINED CRYSTAL STRUC...)
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Revision as of 11:04, 21 November 2007
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REFINED CRYSTAL STRUCTURE OF LIVER ALCOHOL DEHYDROGENASE-NADH COMPLEX AT 1.8 ANGSTROMS RESOLUTION
Overview
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.
About this Structure
2OHX is a Single protein structure of sequence from Equus caballus with ZN, NAD and DMS as ligands. Active as Alcohol dehydrogenase, with EC number 1.1.1.1 Full crystallographic information is available from OCA.
Reference
Refined crystal structure of liver alcohol dehydrogenase-NADH complex at 1.8 A resolution., Al-Karadaghi S, Cedergren-Zeppezauer ES, Hovmoller S, Acta Crystallogr D Biol Crystallogr. 1994 Nov 1;50(Pt 6):793-807. PMID:15299346
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