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3bnu
From Proteopedia
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| - | [[Image:3bnu.jpg|left|200px]] | ||
| - | + | ==Crystal structure of polyamine oxidase FMS1 from Saccharomyces cerevisiae in complex with bis-(3S,3'S)-methylated spermine== | |
| - | + | <StructureSection load='3bnu' size='340' side='right'caption='[[3bnu]], [[Resolution|resolution]] 2.20Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[3bnu]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_18824 Atcc 18824]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3BNU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3BNU FirstGlance]. <br> | |
| - | | | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=SPZ:(3S,3S)-N~1~,N~1~-BUTANE-1,4-DIYLDIBUTANE-1,3-DIAMINE'>SPZ</scene></td></tr> |
| - | + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3bnm|3bnm]]</div></td></tr> | |
| - | + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">FMS1, YMR020W, YM9711.09 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 ATCC 18824])</td></tr> | |
| - | + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Oxidoreductase Oxidoreductase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.5.3.13, 1.5.3.14, 1.5.3.15, 1.5.3.16 and 1.5.3.17 1.5.3.13, 1.5.3.14, 1.5.3.15, 1.5.3.16 and 1.5.3.17] </span></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=3bnu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3bnu OCA], [https://pdbe.org/3bnu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3bnu RCSB], [https://www.ebi.ac.uk/pdbsum/3bnu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3bnu ProSAT]</span></td></tr> | |
| - | + | </table> | |
| + | == Function == | ||
| + | [[https://www.uniprot.org/uniprot/FMS1_YEAST FMS1_YEAST]] Involved in the production of beta-alanine, a precursor of pantothenic acid. Multicopy suppressor of fenpropimorph resistance.<ref>PMID:12670477</ref> <ref>PMID:14617780</ref> | ||
| + | == Evolutionary Conservation == | ||
| + | [[Image:Consurf_key_small.gif|200px|right]] | ||
| + | Check<jmol> | ||
| + | <jmolCheckbox> | ||
| + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/bn/3bnu_consurf.spt"</scriptWhenChecked> | ||
| + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
| + | <text>to colour the structure by Evolutionary Conservation</text> | ||
| + | </jmolCheckbox> | ||
| + | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3bnu ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| - | + | ==See Also== | |
| - | + | *[[Polyamine oxidase|Polyamine oxidase]] | |
| - | + | == References == | |
| - | == | + | <references/> |
| - | + | __TOC__ | |
| + | </StructureSection> | ||
| + | [[Category: Atcc 18824]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Oxidoreductase]] | ||
| + | [[Category: Hao, Q]] | ||
| + | [[Category: Huang, Q]] | ||
| + | [[Category: Fad]] | ||
| + | [[Category: Flavoprotein]] | ||
| + | [[Category: Fms1]] | ||
[[Category: Polyamine oxidase]] | [[Category: Polyamine oxidase]] | ||
| - | [[Category: | + | [[Category: Stereospecificity]] |
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Current revision
Crystal structure of polyamine oxidase FMS1 from Saccharomyces cerevisiae in complex with bis-(3S,3'S)-methylated spermine
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