6mgg: Difference between revisions

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<StructureSection load='6mgg' size='340' side='right'caption='[[6mgg]], [[Resolution|resolution]] 1.78&Aring;' scene=''>
<StructureSection load='6mgg' size='340' side='right'caption='[[6mgg]], [[Resolution|resolution]] 1.78&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[6mgg]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Fratt Fratt]. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6MGG FirstGlance]. <br>
<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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><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></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]] 1.78&#8491;</td></tr>
<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=NEP:N1-PHOSPHONOHISTIDINE'>NEP</scene></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='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">sucD, BZ14_337 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=177416 FRATT]), sucC, FTT_0504c ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=177416 FRATT])</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>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Succinate--CoA_ligase_(ADP-forming) Succinate--CoA ligase (ADP-forming)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.2.1.5 6.2.1.5] </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=6mgg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6mgg OCA], [http://pdbe.org/6mgg PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6mgg RCSB], [http://www.ebi.ac.uk/pdbsum/6mgg PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6mgg ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/A0A0G2RQ73_FRATT A0A0G2RQ73_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] [[http://www.uniprot.org/uniprot/SUCC_FRATT SUCC_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 beta subunit provides nucleotide specificity of the enzyme and binds the substrate succinate, while the binding sites for coenzyme A and phosphate are found in the alpha subunit.
[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]
 
==See Also==
*[[Succinyl-CoA synthetase 3D structures|Succinyl-CoA synthetase 3D structures]]
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Fratt]]
[[Category: Francisella tularensis subsp. tularensis SCHU S4]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Structural genomic]]
[[Category: Jedrzejczak R]]
[[Category: Jedrzejczak, R]]
[[Category: Joachimiak A]]
[[Category: Joachimiak, A]]
[[Category: Maltseva N]]
[[Category: Maltseva, N]]
[[Category: Osipiuk J]]
[[Category: Osipiuk, J]]
[[Category: Satchell KJF]]
[[Category: Satchell, K J.F]]
[[Category: Cpx_02187_02692]]
[[Category: Csgid]]
[[Category: Idp02187]]
[[Category: Idp02692]]
[[Category: Ligase]]
[[Category: Succinyl-coa synthase]]

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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