1teh
From Proteopedia
| Line 20: | Line 20: | ||
[[Category: nad+ dependent alcohol dehydrogenase glutathione dependent formaldehyde dehydrogenase]] | [[Category: nad+ dependent alcohol dehydrogenase glutathione dependent formaldehyde dehydrogenase]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 16:05:07 2007'' |
Revision as of 14:00, 30 October 2007
|
STRUCTURE OF HUMAN LIVER CHICHI ALCOHOL DEHYDROGENASE (A GLUTATHIONE-DEPENDENT FORMALDEHYDE DEHYDROGENASE)
Overview
The crystal structure of the human class III chi chi alcohol dehydrogenase, (ADH) in a binary complex with NAD+(gamma) was solved to 2.7 A resolution, by molecular replacement with human class I beta1 beta1 ADH. chi chi ADH, catalyzes the oxidation of long-chain alcohols such as omega-hydroxy fatty, acids as well as S-hydroxymethyl-glutathione, a spontaneous adduct between, formaldehyde and glutathione. There are two subunits per asymmetric unit, in the chi chi ADH structure. Both subunits display a semi-open, conformation of the catalytic domain. This conformation is half-way, between the open and closed conformations described for the horse EE ADH, enzyme. The semi-open conformation and key changes in elements of, secondary structure provide a structural basis for the ability of chi ... [(full description)]
About this Structure
1TEH is a [Single protein] structure of sequence from [Homo sapiens] with ZN and NAD as [ligands]. Structure known Active Sites: ZN1, ZN2, ZN3, ZN4 and ZNS. Full crystallographic information is available from [OCA].
Reference
Structure of human chi chi alcohol dehydrogenase: a glutathione-dependent formaldehyde dehydrogenase., Yang ZN, Bosron WF, Hurley TD, J Mol Biol. 1997 Jan 24;265(3):330-43. PMID:9018047
Page seeded by OCA on Tue Oct 30 16:05:07 2007
