1v5z: Difference between revisions
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<StructureSection load='1v5z' size='340' side='right'caption='[[1v5z]], [[Resolution|resolution]] 2.00Å' scene=''> | <StructureSection load='1v5z' size='340' side='right'caption='[[1v5z]], [[Resolution|resolution]] 2.00Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1v5z]] is a 2 chain structure with sequence from [ | <table><tr><td colspan='2'>[[1v5z]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Aliivibrio_fischeri Aliivibrio fischeri]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1V5Z OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1V5Z FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2Å</td></tr> | ||
<tr id=' | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=2HC:(2E)-3-(2-HYDROXYPHENYL)ACRYLIC+ACID'>2HC</scene>, <scene name='pdbligand=FMN:FLAVIN+MONONUCLEOTIDE'>FMN</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=1v5z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1v5z OCA], [https://pdbe.org/1v5z PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1v5z RCSB], [https://www.ebi.ac.uk/pdbsum/1v5z PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1v5z ProSAT]</span></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | |||
</table> | </table> | ||
== Function == | == Function == | ||
[ | [https://www.uniprot.org/uniprot/FRA1_ALIFS FRA1_ALIFS] Involved in bioluminescence. It is a good supplier of reduced flavin mononucleotide (FMNH2) to the bioluminescence reaction. Major FMN reductase. It is capable of using both NADH and NADPH as electron donors. As electron acceptor, FMN is the most effective, FAD is considerably effective, and riboflavin is the least effective. | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Aliivibrio fischeri]] | |||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Kobori | [[Category: Kobori T]] | ||
[[Category: Koike | [[Category: Koike H]] | ||
[[Category: Saigo | [[Category: Saigo K]] | ||
[[Category: Sasaki | [[Category: Sasaki H]] | ||
[[Category: Tanokura | [[Category: Tanokura M]] | ||
[[Category: Zenno | [[Category: Zenno S]] | ||
Latest revision as of 23:58, 27 December 2023
Binding of coumarins to NAD(P)H:FMN oxidoreductase
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