6q2d: Difference between revisions

From Proteopedia
Jump to navigationJump to search
← Older edit
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,328,572 edits
No edit summary
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,328,572 edits
No edit summary
 
(One intermediate revision by the same user not shown)
Line 3: Line 3:
<StructureSection load='6q2d' size='340' side='right'caption='[[6q2d]], [[Resolution|resolution]] 3.45&Aring;' scene=''>
<StructureSection load='6q2d' size='340' side='right'caption='[[6q2d]], [[Resolution|resolution]] 3.45&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[6q2d]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_35061 Atcc 35061]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6Q2D OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6Q2D FirstGlance]. <br>
<table><tr><td colspan='2'>[[6q2d]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Methanobrevibacter_smithii Methanobrevibacter smithii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6Q2D OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6Q2D FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SF4:IRON/SULFUR+CLUSTER'>SF4</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]] 3.45&#8491;</td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Msm_1358 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2173 ATCC 35061]), fusA, BK798_06620 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2173 ATCC 35061])</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=6q2d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6q2d OCA], [https://pdbe.org/6q2d PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6q2d RCSB], [https://www.ebi.ac.uk/pdbsum/6q2d PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6q2d ProSAT]</span></td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/2-(3-amino-3-carboxypropyl)histidine_synthase 2-(3-amino-3-carboxypropyl)histidine synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.5.1.108 2.5.1.108] </span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6q2d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6q2d OCA], [http://pdbe.org/6q2d PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6q2d RCSB], [http://www.ebi.ac.uk/pdbsum/6q2d PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6q2d ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/A5UMY5_METS3 A5UMY5_METS3]] Catalyzes the first step of diphthamide biosynthesis, i.e. the transfer of the 3-amino-3-carboxypropyl group from S-adenosyl-L-methionine (SAM) to the C2 position of the imidazole ring of the target histidine residue in translation elongation factor 2 (EF-2).[PIRNR:PIRNR004967] [[http://www.uniprot.org/uniprot/A0A2H4U7K7_METSM A0A2H4U7K7_METSM]] Catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post-translocational (POST) state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E sites, respectively. Catalyzes the coordinated movement of the two tRNA molecules, the mRNA and conformational changes in the ribosome.[HAMAP-Rule:MF_00054][SAAS:SAAS00384500]  
[https://www.uniprot.org/uniprot/A5UMY5_METS3 A5UMY5_METS3] Catalyzes the first step of diphthamide biosynthesis, i.e. the transfer of the 3-amino-3-carboxypropyl group from S-adenosyl-L-methionine (SAM) to the C2 position of the imidazole ring of the target histidine residue in translation elongation factor 2 (EF-2).[PIRNR:PIRNR004967]
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
Line 20: Line 18:
</div>
</div>
<div class="pdbe-citations 6q2d" style="background-color:#fffaf0;"></div>
<div class="pdbe-citations 6q2d" style="background-color:#fffaf0;"></div>
==See Also==
*[[Elongation factor 3D structures|Elongation factor 3D structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Atcc 35061]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Dong, M]]
[[Category: Methanobrevibacter smithii]]
[[Category: Ealick, S E]]
[[Category: Dong M]]
[[Category: Fenwick, M K]]
[[Category: Ealick SE]]
[[Category: Lin, H]]
[[Category: Fenwick MK]]
[[Category: Enzyme]]
[[Category: Lin H]]
[[Category: Iron sulfur cluster]]
[[Category: Radical]]
[[Category: S-adenosylmethionine]]
[[Category: Transferase]]
Retrieved from "https://proteopedia.org/6q2d"