1heu: Difference between revisions
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[[Image:1heu.jpg|left|200px]]<br /><applet load="1heu" size=" | [[Image:1heu.jpg|left|200px]]<br /><applet load="1heu" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="1heu, resolution 1.15Å" /> | caption="1heu, resolution 1.15Å" /> | ||
'''ATOMIC X-RAY STRUCTURE OF LIVER ALCOHOL DEHYDROGENASE CONTAINING CADMIUM AND A HYDROXIDE ADDUCT TO NADH'''<br /> | '''ATOMIC X-RAY STRUCTURE OF LIVER ALCOHOL DEHYDROGENASE CONTAINING CADMIUM AND A HYDROXIDE ADDUCT TO NADH'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
1HEU is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Equus_caballus Equus caballus] with CD, NAD and MRD as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Alcohol_dehydrogenase Alcohol dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.1 1.1.1.1] Known structural/functional Sites: <scene name='pdbsite=AC1:Cd Binding Site For Chain A'>AC1</scene>, <scene name='pdbsite=AC2:Cd Binding Site For Chain A'>AC2</scene>, <scene name='pdbsite=AC3:Cd Binding Site For Chain B'>AC3</scene>, <scene name='pdbsite=AC4:Cd Binding Site For Chain B'>AC4</scene>, <scene name='pdbsite=AC5:Nad Binding Site For Chain A'>AC5</scene> and <scene name='pdbsite=AC6:Nad Binding Site For Chain B'>AC6</scene>. Full crystallographic information is available from [http:// | 1HEU is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Equus_caballus Equus caballus] with <scene name='pdbligand=CD:'>CD</scene>, <scene name='pdbligand=NAD:'>NAD</scene> and <scene name='pdbligand=MRD:'>MRD</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Alcohol_dehydrogenase Alcohol dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.1 1.1.1.1] Known structural/functional Sites: <scene name='pdbsite=AC1:Cd+Binding+Site+For+Chain+A'>AC1</scene>, <scene name='pdbsite=AC2:Cd+Binding+Site+For+Chain+A'>AC2</scene>, <scene name='pdbsite=AC3:Cd+Binding+Site+For+Chain+B'>AC3</scene>, <scene name='pdbsite=AC4:Cd+Binding+Site+For+Chain+B'>AC4</scene>, <scene name='pdbsite=AC5:Nad+Binding+Site+For+Chain+A'>AC5</scene> and <scene name='pdbsite=AC6:Nad+Binding+Site+For+Chain+B'>AC6</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HEU OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: oxidoreductase(nad(a)-choh(d))]] | [[Category: oxidoreductase(nad(a)-choh(d))]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb 3 09:48:54 2008'' | ||
Revision as of 10:48, 3 February 2008
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ATOMIC X-RAY STRUCTURE OF LIVER ALCOHOL DEHYDROGENASE CONTAINING CADMIUM AND A HYDROXIDE ADDUCT TO NADH
OverviewOverview
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 StructureAbout this Structure
1HEU 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.
ReferenceReference
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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