3unv: Difference between revisions
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<StructureSection load='3unv' size='340' side='right'caption='[[3unv]], [[Resolution|resolution]] 1.54Å' scene=''> | <StructureSection load='3unv' size='340' side='right'caption='[[3unv]], [[Resolution|resolution]] 1.54Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3unv]] is a 2 chain structure with sequence from [ | <table><tr><td colspan='2'>[[3unv]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/"bacillus_milletiae"_kawakami_and_yoshida_1920 "bacillus milletiae" kawakami and yoshida 1920]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3UNV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3UNV FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PHE:PHENYLALANINE'>PHE</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=SFE:(3S)-3-AMINO-3-PHENYLPROPANOIC+ACID'>SFE</scene></td></tr> | </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=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PHE:PHENYLALANINE'>PHE</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=SFE:(3S)-3-AMINO-3-PHENYLPROPANOIC+ACID'>SFE</scene></td></tr> | ||
<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=KWS:{2-[(1R,2R)-1-AMINO-2-HYDROXYPROPYL]-4-METHYLIDENE-5-OXO-4,5-DIHYDRO-1H-IMIDAZOL-1-YL}ACETIC+ACID'>KWS</scene></td></tr> | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=KWS:{2-[(1R,2R)-1-AMINO-2-HYDROXYPROPYL]-4-METHYLIDENE-5-OXO-4,5-DIHYDRO-1H-IMIDAZOL-1-YL}ACETIC+ACID'>KWS</scene></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=3unv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3unv OCA], [https://pdbe.org/3unv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3unv RCSB], [https://www.ebi.ac.uk/pdbsum/3unv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3unv ProSAT]</span></td></tr> | ||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
Revision as of 10:51, 20 July 2022
Pantoea agglomerans Phenylalanine AminomutasePantoea agglomerans Phenylalanine Aminomutase
Structural highlights
Publication Abstract from PubMedThe structure of the title aminomutase was solved. The steric bulk of Phe 455 (green CPK structure) twists the phenylpropanoate ligand (green stick) by approximately 15 degrees about the C(beta) axis, which precludes a stronger bidentate salt bridge with Arg 323 (magenta structure). Instead, a weaker monodentate bridge may partially explain the different configuration of the product, relative to that obtained with an isoenzyme that forms a bidentate intermediate. Insights into the Mechanistic Pathway of the Pantoea agglomerans Phenylalanine Aminomutase.,Strom S, Wanninayake U, Ratnayake ND, Walker KD, Geiger JH Angew Chem Int Ed Engl. 2012 Feb 8. doi: 10.1002/anie.201108525. PMID:22319000[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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