5opd: Difference between revisions

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New page: '''Unreleased structure''' The entry 5opd is ON HOLD Authors: Garcia-Pino, A. Description: Structure of phosphorylated EF-Tu in complex with GTP Category: Unreleased Structures [[C...
 
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'''Unreleased structure'''


The entry 5opd is ON HOLD
==Structure of phosphorylated EF-Tu in complex with GTP==
<StructureSection load='5opd' size='340' side='right'caption='[[5opd]], [[Resolution|resolution]] 2.75&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5opd]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_HS Escherichia coli HS]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5OPD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5OPD FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.75&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=GTP:GUANOSINE-5-TRIPHOSPHATE'>GTP</scene>, <scene name='pdbligand=IOD:IODIDE+ION'>IOD</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=TPO:PHOSPHOTHREONINE'>TPO</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=5opd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5opd OCA], [https://pdbe.org/5opd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5opd RCSB], [https://www.ebi.ac.uk/pdbsum/5opd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5opd ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/EFTU1_ECOLI EFTU1_ECOLI] This protein promotes the GTP-dependent binding of aminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis.[HAMAP-Rule:MF_00118]  May play an important regulatory role in cell growth and in the bacterial response to nutrient deprivation.[HAMAP-Rule:MF_00118]


Authors: Garcia-Pino, A.
==See Also==
 
*[[Elongation factor 3D structures|Elongation factor 3D structures]]
Description: Structure of phosphorylated EF-Tu in complex with GTP
__TOC__
[[Category: Unreleased Structures]]
</StructureSection>
[[Category: Garcia-Pino, A]]
[[Category: Escherichia coli HS]]
[[Category: Large Structures]]
[[Category: Garcia-Pino A]]

Latest revision as of 16:57, 13 December 2023

Structure of phosphorylated EF-Tu in complex with GTP

5opd, resolution 2.75Å

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