6pfn

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<StructureSection load='6pfn' size='340' side='right'caption='[[6pfn]], [[Resolution|resolution]] 1.76&Aring;' scene=''>
<StructureSection load='6pfn' size='340' side='right'caption='[[6pfn]], [[Resolution|resolution]] 1.76&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[6pfn]] 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=6PFN OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6PFN FirstGlance]. <br>
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<table><tr><td colspan='2'>[[6pfn]] 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=6PFN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6PFN FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=COA:COENZYME+A'>COA</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.76&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[6mgg|6mgg]]</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=COA:COENZYME+A'>COA</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene></td></tr>
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<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>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6pfn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6pfn OCA], [https://pdbe.org/6pfn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6pfn RCSB], [https://www.ebi.ac.uk/pdbsum/6pfn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6pfn ProSAT]</span></td></tr>
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<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>
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<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=6pfn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6pfn OCA], [http://pdbe.org/6pfn PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6pfn RCSB], [http://www.ebi.ac.uk/pdbsum/6pfn PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6pfn ProSAT]</span></td></tr>
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</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/A0A454XSD0_FRATT A0A454XSD0_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.
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[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]
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==See Also==
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*[[Succinyl-CoA synthetase 3D structures|Succinyl-CoA synthetase 3D structures]]
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__TOC__
</StructureSection>
</StructureSection>
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[[Category: Fratt]]
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[[Category: Francisella tularensis subsp. tularensis SCHU S4]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Structural genomic]]
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[[Category: Jedrzejczak R]]
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[[Category: Jedrzejczak, R]]
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[[Category: Joachimiak A]]
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[[Category: Joachimiak, A]]
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[[Category: Maltseva N]]
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[[Category: Maltseva, N]]
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[[Category: Osipiuk J]]
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[[Category: Osipiuk, J]]
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[[Category: Satchell KJF]]
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[[Category: Satchell, K J.F]]
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[[Category: Cpx_02187_02692]]
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[[Category: Csgid]]
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[[Category: Idp02187]]
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[[Category: Idp02692]]
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[[Category: Ligase]]
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[[Category: Succinyl-coa synthase]]
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Current revision

Succinyl-CoA synthase from Francisella tularensis

PDB ID 6pfn

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