1xt6: Difference between revisions
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<StructureSection load='1xt6' size='340' side='right'caption='[[1xt6]], [[Resolution|resolution]] 1.80Å' scene=''> | <StructureSection load='1xt6' size='340' side='right'caption='[[1xt6]], [[Resolution|resolution]] 1.80Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1xt6]] is a 1 chain structure with sequence from [ | <table><tr><td colspan='2'>[[1xt6]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Desvh Desvh]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XT6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1XT6 FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><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" id="ligandDat"><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'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1xt6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1xt6 OCA], [https://pdbe.org/1xt6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1xt6 RCSB], [https://www.ebi.ac.uk/pdbsum/1xt6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1xt6 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[[ | [[https://www.uniprot.org/uniprot/FLAV_DESVH FLAV_DESVH]] Low-potential electron donor to a number of redox enzymes. | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
Revision as of 19:44, 20 October 2021
S35C Flavodoxin Mutant in the semiquinone stateS35C Flavodoxin Mutant in the semiquinone state
Structural highlights
Function[FLAV_DESVH] Low-potential electron donor to a number of redox enzymes. Evolutionary 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 crystallographic structure of an engineered flavodoxin mutant from Desulfovibrio vulgaris has been analysed. Site-directed mutagenesis was used to substitute serine 35 with a cysteine to provide a possible covalent linkage. The crystal structure of the semiquinone form of this mutant is similar to the corresponding oxidation state of the wild-type flavodoxin. Analysis of the structural changes reveals the interaction between N(5)H of the flavin and the carbonyl O atom of Gly61 to be critical for modulation of the electrochemical properties of the protein. Structure of S35C flavodoxin mutant from Desulfovibrio vulgaris in the semiquinone state.,Artali R, Marchini N, Meneghetti F, Cavazzini D, Cassetta A, Sassone C Acta Crystallogr D Biol Crystallogr. 2005 Apr;61(Pt 4):481-4. Epub 2005, Mar 24. PMID:15805604[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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