6mgg: Difference between revisions

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New page: '''Unreleased structure''' The entry 6mgg is ON HOLD Authors: Osipiuk, J., Maltseva, N., Jedrzejczak, R., Satchell, K.J.F., Joachimiak, A., Center for Structural Genomics of Infectious ...
 
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'''Unreleased structure'''


The entry 6mgg is ON HOLD
==Succinyl-CoA synthase from Francisella tularensis, phosphorylated, in complex with CoA==
<StructureSection load='6mgg' size='340' side='right'caption='[[6mgg]], [[Resolution|resolution]] 1.78&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6mgg]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Francisella_tularensis_subsp._tularensis_SCHU_S4 Francisella tularensis subsp. tularensis SCHU S4]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6MGG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6MGG 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]] 1.78&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=COA:COENZYME+A'>COA</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NEP:N1-PHOSPHONOHISTIDINE'>NEP</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=6mgg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6mgg OCA], [https://pdbe.org/6mgg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6mgg RCSB], [https://www.ebi.ac.uk/pdbsum/6mgg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6mgg ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q5NHF4_FRATT Q5NHF4_FRATT] Succinyl-CoA synthetase functions in the citric acid cycle (TCA), coupling the hydrolysis of succinyl-CoA to the synthesis of either ATP or GTP and thus represents the only step of substrate-level phosphorylation in the TCA. The alpha subunit of the enzyme binds the substrates coenzyme A and phosphate, while succinate binding and nucleotide specificity is provided by the beta subunit.[HAMAP-Rule:MF_01988][RuleBase:RU000699]


Authors: Osipiuk, J., Maltseva, N., Jedrzejczak, R., Satchell, K.J.F., Joachimiak, A., Center for Structural Genomics of Infectious Diseases (CSGID)
==See Also==
 
*[[Succinyl-CoA synthetase 3D structures|Succinyl-CoA synthetase 3D structures]]
Description: Succinyl-CoA synthase from Francisella tularensis
__TOC__
[[Category: Unreleased Structures]]
</StructureSection>
[[Category: Satchell, K.J.F]]
[[Category: Francisella tularensis subsp. tularensis SCHU S4]]
[[Category: Maltseva, N]]
[[Category: Large Structures]]
[[Category: Joachimiak, A]]
[[Category: Jedrzejczak R]]
[[Category: Jedrzejczak, R]]
[[Category: Joachimiak A]]
[[Category: Osipiuk, J]]
[[Category: Maltseva N]]
[[Category: Center For Structural Genomics Of Infectious Diseases (Csgid)]]
[[Category: Osipiuk J]]
[[Category: Satchell KJF]]

Latest revision as of 06:31, 11 October 2023

Succinyl-CoA synthase from Francisella tularensis, phosphorylated, in complex with CoA

6mgg, resolution 1.78Å

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