6rji
From Proteopedia
(Difference between revisions)
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<StructureSection load='6rji' size='340' side='right'caption='[[6rji]], [[Resolution|resolution]] 1.48Å' scene=''> | <StructureSection load='6rji' size='340' side='right'caption='[[6rji]], [[Resolution|resolution]] 1.48Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[6rji]] is a 1 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[6rji]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Staa8 Staa8]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6RJI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6RJI FirstGlance]. <br> |
| - | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">efp, SAOUHSC_01625 ([ | + | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">efp, SAOUHSC_01625 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=93061 STAA8])</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=6rji FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6rji OCA], [https://pdbe.org/6rji PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6rji RCSB], [https://www.ebi.ac.uk/pdbsum/6rji PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6rji ProSAT]</span></td></tr> |
</table> | </table> | ||
== Function == | == Function == | ||
| - | [[ | + | [[https://www.uniprot.org/uniprot/EFP_STAA8 EFP_STAA8]] Involved in peptide bond synthesis. Stimulates efficient translation and peptide-bond synthesis on native or reconstituted 70S ribosomes in vitro. Probably functions indirectly by altering the affinity of the ribosome for aminoacyl-tRNA, thus increasing their reactivity as acceptors for peptidyl transferase. |
<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 6rji" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 6rji" style="background-color:#fffaf0;"></div> | ||
| + | |||
| + | ==See Also== | ||
| + | *[[Elongation factor 3D structures|Elongation factor 3D structures]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
Revision as of 15:25, 8 June 2021
X-ray structure of the elongation factor P of S. aureus
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