6mfz: Difference between revisions
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<StructureSection load='6mfz' size='340' side='right'caption='[[6mfz]], [[Resolution|resolution]] 6.00Å' scene=''> | <StructureSection load='6mfz' size='340' side='right'caption='[[6mfz]], [[Resolution|resolution]] 6.00Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[6mfz]] is a 2 chain structure with sequence from [ | <table><tr><td colspan='2'>[[6mfz]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Brevibacillus_parabrevis Brevibacillus parabrevis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6MFZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6MFZ 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]] 6Å</td></tr> | ||
<tr id=' | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PNS:4-PHOSPHOPANTETHEINE'>PNS</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=6mfz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6mfz OCA], [https://pdbe.org/6mfz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6mfz RCSB], [https://www.ebi.ac.uk/pdbsum/6mfz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6mfz ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[ | [https://www.uniprot.org/uniprot/LGRA_BREPA LGRA_BREPA] Activates valine (or leucine, but much less frequently), and then glycine and catalyzes the formation of the peptide bond in the first step of peptide synthesis. This enzyme may also play a role in N-formylation of the first amino acid residue in the synthesized dipeptide. | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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</div> | </div> | ||
<div class="pdbe-citations 6mfz" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 6mfz" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[Linear gramicidin synthase|Linear gramicidin synthase]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Brevibacillus parabrevis]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Eivaskhani | [[Category: Eivaskhani M]] | ||
[[Category: Harb | [[Category: Harb I]] | ||
[[Category: Reimer | [[Category: Reimer JM]] | ||
[[Category: Schmeing | [[Category: Schmeing TM]] | ||
Latest revision as of 06:30, 11 October 2023
Crystal structure of dimodular LgrA in a condensation state
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