1euc: Difference between revisions

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<StructureSection load='1euc' size='340' side='right'caption='[[1euc]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
<StructureSection load='1euc' size='340' side='right'caption='[[1euc]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1euc]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Pig Pig]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EUC OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1EUC FirstGlance]. <br>
<table><tr><td colspan='2'>[[1euc]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Pig Pig]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EUC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1EUC FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=CME:S,S-(2-HYDROXYETHYL)THIOCYSTEINE'>CME</scene></td></tr>
<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=CME:S,S-(2-HYDROXYETHYL)THIOCYSTEINE'>CME</scene></td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1eud|1eud]], [[2scu|2scu]], [[1cqi|1cqi]], [[1cqj|1cqj]]</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1eud|1eud]], [[2scu|2scu]], [[1cqi|1cqi]], [[1cqj|1cqj]]</div></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_(GDP-forming) Succinate--CoA ligase (GDP-forming)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.2.1.4 6.2.1.4] </span></td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Succinate--CoA_ligase_(GDP-forming) Succinate--CoA ligase (GDP-forming)], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.2.1.4 6.2.1.4] </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=1euc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1euc OCA], [http://pdbe.org/1euc PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1euc RCSB], [http://www.ebi.ac.uk/pdbsum/1euc PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1euc 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=1euc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1euc OCA], [https://pdbe.org/1euc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1euc RCSB], [https://www.ebi.ac.uk/pdbsum/1euc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1euc ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/SUCA_PIG SUCA_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). [[http://www.uniprot.org/uniprot/SUCB2_PIG SUCB2_PIG]] Catalyzes the GTP-dependent ligation of succinate and CoA to form succinyl-CoA (By similarity).  
[[https://www.uniprot.org/uniprot/SUCA_PIG SUCA_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). [[https://www.uniprot.org/uniprot/SUCB2_PIG SUCB2_PIG]] Catalyzes the GTP-dependent ligation of succinate and CoA to form succinyl-CoA (By similarity).  
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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==See Also==
==See Also==
*[[Succinyl-CoA synthetase|Succinyl-CoA synthetase]]
*[[Succinyl-CoA synthetase 3D structures|Succinyl-CoA synthetase 3D structures]]
== References ==
== References ==
<references/>
<references/>

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