8ozw
From Proteopedia
(Difference between revisions)
| Line 1: | Line 1: | ||
| - | '''Unreleased structure''' | ||
| - | + | ==Imine Reductase from Ajellomyces dermatitidis in complex NADPH4== | |
| + | <StructureSection load='8ozw' size='340' side='right'caption='[[8ozw]], [[Resolution|resolution]] 2.01Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[8ozw]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Blastomyces_dermatitidis Blastomyces dermatitidis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8OZW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8OZW FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.01Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=TXP:1,4,5,6-TETRAHYDRONICOTINAMIDE+ADENINE+DINUCLEOTIDE+PHOSPHATE'>TXP</scene></td></tr> | ||
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=8ozw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8ozw OCA], [https://pdbe.org/8ozw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8ozw RCSB], [https://www.ebi.ac.uk/pdbsum/8ozw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8ozw ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/C5GTJ9_AJEDR C5GTJ9_AJEDR] | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The NADPH-dependent imine reductase from Ajellomyces dermatitidis (AdRedAm) catalyzes the reductive amination of certain ketones with amine donors supplied in an equimolar ratio. The structure of AdRedAm has been determined in three forms. The first form, which belongs to space group P3(1)21 and was refined to 2.01 A resolution, features two molecules (one dimer) in the asymmetric unit in complex with the redox-inactive cofactor NADPH(4). The second form, which belongs to space group C2(1) and was refined to 1.73 A resolution, has nine molecules (four and a half dimers) in the asymmetric unit, each complexed with NADP(+). The third form, which belongs to space group P3(1)21 and was refined to 1.52 A resolution, has one molecule (one half-dimer) in the asymmetric unit. This structure was again complexed with NADP(+) and also with the substrate 2,2-difluoroacetophenone. The different data sets permit the analysis of AdRedAm in different conformational states and also reveal the molecular basis of stereoselectivity in the transformation of fluorinated acetophenone substrates by the enzyme. | ||
| - | + | Structure of the imine reductase from Ajellomyces dermatitidis in three crystal forms.,Sharma M, Cuetos A, Willliams A, Gonzalez-Martinez D, Grogan G Acta Crystallogr F Struct Biol Commun. 2023 Sep 1. doi: , 10.1107/S2053230X23006672. PMID:37581897<ref>PMID:37581897</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| - | [[Category: | + | <div class="pdbe-citations 8ozw" style="background-color:#fffaf0;"></div> |
| - | [[Category: Grogan | + | == References == |
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Blastomyces dermatitidis]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Grogan G]] | ||
| + | [[Category: Sharma M]] | ||
Revision as of 09:17, 30 August 2023
Imine Reductase from Ajellomyces dermatitidis in complex NADPH4
| |||||||||||
