4xx0: Difference between revisions
Jump to navigation
Jump to search
No edit summary |
No edit summary |
||
| Line 4: | Line 4: | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4xx0]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4XX0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4XX0 FirstGlance]. <br> | <table><tr><td colspan='2'>[[4xx0]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4XX0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4XX0 FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CME:S,S-(2-HYDROXYETHYL)THIOCYSTEINE'>CME</scene>, <scene name='pdbligand=COA:COENZYME+A'>COA</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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]] 2.1Å</td></tr> | ||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CME:S,S-(2-HYDROXYETHYL)THIOCYSTEINE'>CME</scene>, <scene name='pdbligand=COA:COENZYME+A'>COA</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=4xx0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4xx0 OCA], [https://pdbe.org/4xx0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4xx0 RCSB], [https://www.ebi.ac.uk/pdbsum/4xx0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4xx0 ProSAT]</span></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=4xx0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4xx0 OCA], [https://pdbe.org/4xx0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4xx0 RCSB], [https://www.ebi.ac.uk/pdbsum/4xx0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4xx0 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
Latest revision as of 03:55, 28 December 2023
CoA bound to pig GTP-specific succinyl-CoA synthetaseCoA bound to pig GTP-specific succinyl-CoA synthetase
Structural highlights
FunctionSUCA_PIG Catalyzes the ATP- or GTP-dependent ligation of succinate and CoA to form succinyl-CoA. The nature of the beta subunit determines the nucleotide specificity (By similarity). Publication Abstract from PubMedPig GTP-specific succinyl-CoA synthetase is an alphabeta-heterodimer. The crystal structure of the complex with the substrate CoA was determined at 2.1 A resolution. The structure shows CoA bound to the amino-terminal domain of the alpha-subunit, with the free thiol extending from the adenine portion into the site where the catalytic histidine residue resides. Structure of GTP-specific succinyl-CoA synthetase in complex with CoA.,Huang J, Malhi M, Deneke J, Fraser ME Acta Crystallogr F Struct Biol Commun. 2015 Aug 1;71(Pt 8):1067-71. doi:, 10.1107/S2053230X15011188. Epub 2015 Jul 29. PMID:26249701[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
|
| ||||||||||||||||||