1het
From Proteopedia
Contents |
ATOMIC X-RAY STRUCTURE OF LIVER ALCOHOL DEHYDROGENASE CONTAINING A HYDROXIDE ADDUCT TO NADH
Template:ABSTRACT PUBMED 11134046
About this Structure
1het is a 2 chain structure with sequence from Equus caballus. Full crystallographic information is available from OCA.
See Also
Reference
- Meijers R, Morris RJ, Adolph HW, Merli A, Lamzin VS, Cedergren-Zeppezauer ES. On the enzymatic activation of NADH. J Biol Chem. 2001 Mar 23;276(12):9316-21. Epub 2000 Dec 28. PMID:11134046 doi:10.1074/jbc.M010870200
- Ramaswamy S, Park DH, Plapp BV. Substitutions in a flexible loop of horse liver alcohol dehydrogenase hinder the conformational change and unmask hydrogen transfer. Biochemistry. 1999 Oct 19;38(42):13951-9. PMID:10529241
- Adolph HW, Kiefer M, Cedergren-Zeppezauer E. Electrostatic effects in the kinetics of coenzyme binding to isozymes of alcohol dehydrogenase from horse liver. Biochemistry. 1997 Jul 22;36(29):8743-54. PMID:9220961 doi:10.1021/bi970398k
- Al-Karadaghi S, Cedergren-Zeppezauer ES, Dauter Z, Wilson KS. Refined structure of Cu-substituted alcohol dehydrogenase at 2.1 A resolution. Acta Crystallogr D Biol Crystallogr. 1995 Sep 1;51(Pt 5):805-13. PMID:15299812 doi:10.1107/S090744499500045X
- Al-Karadaghi S, Cedergren-Zeppezauer ES, Hovmoller S. Refined crystal structure of liver alcohol dehydrogenase-NADH complex at 1.8 A resolution. Acta Crystallogr D Biol Crystallogr. 1994 Nov 1;50(Pt 6):793-807. PMID:15299346 doi:http://dx.doi.org/10.1107/S0907444994005263
