1hf3: Difference between revisions
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<StructureSection load='1hf3' size='340' side='right'caption='[[1hf3]], [[Resolution|resolution]] 1.95Å' scene=''> | <StructureSection load='1hf3' size='340' side='right'caption='[[1hf3]], [[Resolution|resolution]] 1.95Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1hf3]] is a 2 chain structure with sequence from [ | <table><tr><td colspan='2'>[[1hf3]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Equus_caballus Equus caballus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HF3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1HF3 FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CD:CADMIUM+ION'>CD</scene>, <scene name='pdbligand=MRD:(4R)-2-METHYLPENTANE-2,4-DIOL'>MRD</scene>, <scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CD:CADMIUM+ION'>CD</scene>, <scene name='pdbligand=MRD:(4R)-2-METHYLPENTANE-2,4-DIOL'>MRD</scene>, <scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene></td></tr> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1het|1het]], [[1heu|1heu]], [[1a71|1a71]], [[1a72|1a72]], [[1axe|1axe]], [[1axg|1axg]], [[1bto|1bto]], [[1lde|1lde]], [[1ldy|1ldy]], [[1qlh|1qlh]], [[1qlj|1qlj]], [[3bto|3bto]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1het|1het]], [[1heu|1heu]], [[1a71|1a71]], [[1a72|1a72]], [[1axe|1axe]], [[1axg|1axg]], [[1bto|1bto]], [[1lde|1lde]], [[1ldy|1ldy]], [[1qlh|1qlh]], [[1qlj|1qlj]], [[3bto|3bto]]</div></td></tr> | ||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Alcohol_dehydrogenase Alcohol dehydrogenase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.1 1.1.1.1] </span></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1hf3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hf3 OCA], [https://pdbe.org/1hf3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1hf3 RCSB], [https://www.ebi.ac.uk/pdbsum/1hf3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1hf3 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
Revision as of 08:49, 28 April 2021
ATOMIC X-RAY STRUCTURE OF LIVER ALCOHOL DEHYDROGENASE CONTAINING Cadmium and a hydroxide adduct to NADHATOMIC X-RAY STRUCTURE OF LIVER ALCOHOL DEHYDROGENASE CONTAINING Cadmium and a hydroxide adduct to NADH
Structural highlights
Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedAtomic (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. 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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