1agn

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spinqualitylabelsall models 1agn, resolution 3.Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

X-RAY STRUCTURE OF HUMAN SIGMA ALCOHOL DEHYDROGENASE

Overview

The structural determinants of substrate recognition in the human class, IV, or sigmasigma, alcohol dehydrogenase (ADH) isoenzyme were examined, through x-ray crystallography and site-directed mutagenesis. The crystal, structure of sigmasigma ADH complexed with NAD+ and acetate was solved to, 3-A resolution. The human beta1beta1 and sigmasigma ADH isoenzymes share, 69% sequence identity and exhibit dramatically different kinetic, properties. Differences in the amino acids at positions 57, 116, 141, 309, and 317 create a different topology within the sigmasigma, substrate-binding pocket, relative to the beta1beta1 isoenzyme. The, nicotinamide ring of the NAD(H) molecule, in the sigmasigma structure, appears to be twisted relative to its position in the beta1beta1, isoenzyme. In conjunction ... [(full description)]

About this Structure

1AGN is a [Single protein] structure of sequence from [Homo sapiens] with ZN, ACT and NAD as [ligands]. The following page contains interesting information on the relation of 1AGN with [Alcohol Dehydrogenase]. Active as [[1]], with EC number [1.1.1.1]. Full crystallographic information is available from [OCA].

Reference

X-ray structure of human class IV sigmasigma alcohol dehydrogenase. Structural basis for substrate specificity., Xie P, Parsons SH, Speckhard DC, Bosron WF, Hurley TD, J Biol Chem. 1997 Jul 25;272(30):18558-63. PMID:9228021

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