1v5z
From Proteopedia
(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 [http://en.wikipedia.org/wiki/ | + | <table><tr><td colspan='2'>[[1v5z]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/"achromobacter_fischeri"_(beijerinck_1889)_bergey_et_al._1930 "achromobacter fischeri" (beijerinck 1889) bergey et al. 1930]. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1V5Z FirstGlance]. <br> |
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=2HC:(2E)-3-(2-HYDROXYPHENYL)ACRYLIC+ACID'>2HC</scene>, <scene name='pdbligand=FMN:FLAVIN+MONONUCLEOTIDE'>FMN</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=2HC:(2E)-3-(2-HYDROXYPHENYL)ACRYLIC+ACID'>2HC</scene>, <scene name='pdbligand=FMN:FLAVIN+MONONUCLEOTIDE'>FMN</scene></td></tr> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1vfr|1vfr]], [[1v5y|1v5y]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1vfr|1vfr]], [[1v5y|1v5y]]</td></tr> | ||
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">FRaseI ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=668 | + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">FRaseI ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=668 "Achromobacter fischeri" (Beijerinck 1889) Bergey et al. 1930])</td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1v5z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1v5z OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1v5z RCSB], [http://www.ebi.ac.uk/pdbsum/1v5z PDBsum]</span></td></tr> | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1v5z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1v5z OCA], [http://pdbe.org/1v5z PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1v5z RCSB], [http://www.ebi.ac.uk/pdbsum/1v5z PDBsum]</span></td></tr> |
</table> | </table> | ||
== Function == | == Function == | ||
| - | [[http://www.uniprot.org/uniprot/ | + | [[http://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: Kobori, T]] | [[Category: Kobori, T]] | ||
[[Category: Koike, H]] | [[Category: Koike, H]] | ||
Revision as of 13:38, 10 September 2015
Binding of coumarins to NAD(P)H:FMN oxidoreductase
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