2x3n: Difference between revisions
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<StructureSection load='2x3n' size='340' side='right'caption='[[2x3n]], [[Resolution|resolution]] 1.75Å' scene=''> | <StructureSection load='2x3n' size='340' side='right'caption='[[2x3n]], [[Resolution|resolution]] 1.75Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2x3n]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[2x3n]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_aeruginosa Pseudomonas aeruginosa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2X3N OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2X3N 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></td></tr> | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.75Å</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></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=2x3n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2x3n OCA], [https://pdbe.org/2x3n PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2x3n RCSB], [https://www.ebi.ac.uk/pdbsum/2x3n PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2x3n ProSAT]</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=2x3n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2x3n OCA], [https://pdbe.org/2x3n PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2x3n RCSB], [https://www.ebi.ac.uk/pdbsum/2x3n PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2x3n ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/Q9HWJ1_PSEAE Q9HWJ1_PSEAE] | |||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Carter | [[Category: Pseudomonas aeruginosa]] | ||
[[Category: Johnson | [[Category: Carter LG]] | ||
[[Category: Liu | [[Category: Johnson KA]] | ||
[[Category: Mcmahon | [[Category: Liu H]] | ||
[[Category: Naismith | [[Category: Mcmahon SA]] | ||
[[Category: Oke | [[Category: Naismith JH]] | ||
[[Category: White | [[Category: Oke M]] | ||
[[Category: White MF]] | |||
Latest revision as of 13:20, 9 May 2024
Crystal structure of pqsL, a probable FAD-dependent monooxygenase from Pseudomonas aeruginosaCrystal structure of pqsL, a probable FAD-dependent monooxygenase from Pseudomonas aeruginosa
Structural highlights
FunctionEvolutionary Conservation![]() Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe Scottish Structural Proteomics Facility was funded to develop a laboratory scale approach to high throughput structure determination. The effort was successful in that over 40 structures were determined. These structures and the methods harnessed to obtain them are reported here. This report reflects on the value of automation but also on the continued requirement for a high degree of scientific and technical expertise. The efficiency of the process poses challenges to the current paradigm of structural analysis and publication. In the 5 year period we published ten peer-reviewed papers reporting structural data arising from the pipeline. Nevertheless, the number of structures solved exceeded our ability to analyse and publish each new finding. By reporting the experimental details and depositing the structures we hope to maximize the impact of the project by allowing others to follow up the relevant biology. The Scottish Structural Proteomics Facility: targets, methods and outputs.,Oke M, Carter LG, Johnson KA, Liu H, McMahon SA, Yan X, Kerou M, Weikart ND, Kadi N, Sheikh MA, Schmelz S, Dorward M, Zawadzki M, Cozens C, Falconer H, Powers H, Overton IM, van Niekerk CA, Peng X, Patel P, Garrett RA, Prangishvili D, Botting CH, Coote PJ, Dryden DT, Barton GJ, Schwarz-Linek U, Challis GL, Taylor GL, White MF, Naismith JH J Struct Funct Genomics. 2010 Jun;11(2):167-80. Epub 2010 Apr 24. PMID:20419351[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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