6mel
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Succinyl-CoA synthase from Campylobacter jejuni== | |
| - | + | <StructureSection load='6mel' size='340' side='right' caption='[[6mel]], [[Resolution|resolution]] 2.06Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[6mel]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6MEL OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6MEL FirstGlance]. <br> | |
| - | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CIT:CITRIC+ACID'>CIT</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene></td></tr> | |
| - | [[Category: | + | <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> |
| - | [[Category: | + | <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=6mel FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6mel OCA], [http://pdbe.org/6mel PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6mel RCSB], [http://www.ebi.ac.uk/pdbsum/6mel PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6mel ProSAT]</span></td></tr> |
| + | </table> | ||
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/SUCC_CAMJR SUCC_CAMJR]] 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. | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Structural genomic]] | ||
| + | [[Category: Jedrzejczak, R]] | ||
| + | [[Category: Joachimiak, A]] | ||
[[Category: Maltseva, N]] | [[Category: Maltseva, N]] | ||
| - | [[Category: Joachimiak, A]] | ||
| - | [[Category: Jedrzejczak, R]] | ||
[[Category: Osipiuk, J]] | [[Category: Osipiuk, J]] | ||
| - | [[Category: | + | [[Category: Satchell, K J.F]] |
| + | [[Category: Cpx_90676_90715]] | ||
| + | [[Category: Csgid]] | ||
| + | [[Category: Idp90676]] | ||
| + | [[Category: Idp90715]] | ||
| + | [[Category: Ligase]] | ||
| + | [[Category: Succinyl-coa synthase]] | ||
Revision as of 20:00, 19 September 2018
Succinyl-CoA synthase from Campylobacter jejuni
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