2g5w
From Proteopedia
(Difference between revisions)
m (Protected "2g5w" [edit=sysop:move=sysop]) |
|||
Line 1: | Line 1: | ||
- | + | ==X-ray crystal structure of Arabidopsis thaliana 12-oxophytodienoate reductase isoform 3 (AtOPR3) in complex with 8-iso prostaglandin A1 and its cofactor, flavin mononucleotide.== | |
- | + | <StructureSection load='2g5w' size='340' side='right' caption='[[2g5w]], [[Resolution|resolution]] 2.58Å' scene=''> | |
- | + | == Structural highlights == | |
- | + | <table><tr><td colspan='2'>[[2g5w]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2G5W OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2G5W FirstGlance]. <br> | |
- | + | </td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=8PG:(8S,12S)-15S-HYDROXY-9-OXOPROSTA-10Z,13E-DIEN-1-OIC+ACID'>8PG</scene>, <scene name='pdbligand=FMN:FLAVIN+MONONUCLEOTIDE'>FMN</scene><br> | |
- | + | <tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1q45|1q45]]</td></tr> | |
- | + | <tr><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">At2g06050 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=3702 Arabidopsis thaliana])</td></tr> | |
- | == | + | <tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/12-oxophytodienoate_reductase 12-oxophytodienoate reductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.3.1.42 1.3.1.42] </span></td></tr> |
- | [[2g5w]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2G5W OCA]. | + | <tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2g5w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2g5w OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2g5w RCSB], [http://www.ebi.ac.uk/pdbsum/2g5w PDBsum]</span></td></tr> |
+ | <table> | ||
+ | == 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/g5/2g5w_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/chain_selection.php?pdb_ID=2ata ConSurf]. | ||
+ | <div style="clear:both"></div> | ||
+ | __TOC__ | ||
+ | </StructureSection> | ||
[[Category: 12-oxophytodienoate reductase]] | [[Category: 12-oxophytodienoate reductase]] | ||
[[Category: Arabidopsis thaliana]] | [[Category: Arabidopsis thaliana]] |
Revision as of 05:28, 29 September 2014
X-ray crystal structure of Arabidopsis thaliana 12-oxophytodienoate reductase isoform 3 (AtOPR3) in complex with 8-iso prostaglandin A1 and its cofactor, flavin mononucleotide.
|
Categories: 12-oxophytodienoate reductase | Arabidopsis thaliana | Bingman, C A. | CESG, Center for Eukaryotic Structural Genomics. | Fox, B G. | Han, B W. | Malone, T E. | Phillips, G N. | Wesenberg, G E. | At2g06050 | Center for eukaryotic structural genomic | Cesg | Flavoenzyme | Flavoprotein | Old yellow enzyme | Opr isoform 3 | Oxidoreductase | Protein structure initiative | Psi | Secondary messenger | Structural genomics functional follow-up study | Xenobiotic reductase