1het

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Image:1het.gif

1het, resolution 1.15Å

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ATOMIC X-RAY STRUCTURE OF LIVER ALCOHOL DEHYDROGENASE CONTAINING A HYDROXIDE ADDUCT TO NADH

Overview

Atomic (1 A) resolution x-ray structures of horse liver alcohol dehydrogenase in complex with NADH revealed the formation of an adduct in the active site between a metal-bound water and NADH. Furthermore, a pronounced distortion of the pyridine ring of NADH was observed. A series of quantum chemical calculations on the water-nicotinamide adduct showed that the puckering of the pyridine ring in the crystal structures can only be reproduced when the water is considered a hydroxide ion. These observations provide fundamental insight into the enzymatic activation of NADH for hydride transfer.

About this Structure

1HET is a Single protein structure of sequence from Equus caballus with , and as ligands. Active as Alcohol dehydrogenase, with EC number 1.1.1.1 Known structural/functional Sites: , , , , and . Full crystallographic information is available from OCA.

Reference

On the enzymatic activation of NADH., Meijers R, Morris RJ, Adolph HW, Merli A, Lamzin VS, Cedergren-Zeppezauer ES, J Biol Chem. 2001 Mar 23;276(12):9316-21. Epub 2000 Dec 28. PMID:11134046

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