7xep: Difference between revisions
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[7xep]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_subtilis_subsp._subtilis_str._168 Bacillus subtilis subsp. subtilis str. 168]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7XEP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7XEP FirstGlance]. <br> | <table><tr><td colspan='2'>[[7xep]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_subtilis_subsp._subtilis_str._168 Bacillus subtilis subsp. subtilis str. 168]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7XEP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7XEP FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=EIL:[6-methyl-4-[[(5-methyl-2-oxidanylidene-furan-3-ylidene)amino]methyl]-5-oxidanyl-pyridin-3-yl]methyl+dihydrogen+phosphate'>EIL</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</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]] 1.78Å</td></tr> | ||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=EIL:[6-methyl-4-[[(5-methyl-2-oxidanylidene-furan-3-ylidene)amino]methyl]-5-oxidanyl-pyridin-3-yl]methyl+dihydrogen+phosphate'>EIL</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</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=7xep FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7xep OCA], [https://pdbe.org/7xep PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7xep RCSB], [https://www.ebi.ac.uk/pdbsum/7xep PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7xep 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=7xep FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7xep OCA], [https://pdbe.org/7xep PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7xep RCSB], [https://www.ebi.ac.uk/pdbsum/7xep PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7xep ProSAT]</span></td></tr> | ||
</table> | </table> |
Latest revision as of 20:52, 29 November 2023
SufS with L-propargylglycineSufS with L-propargylglycine
Structural highlights
FunctionSUFS_BACSU Enzyme able to deliver sulfur to partners involved in Fe-S cluster assembly. Catalyzes the removal of elemental sulfur atoms from L-cysteine to produce L-alanine. Activity is stimulated 40-to 100-fold by SufU, which acts as a second substrate for this enzyme following release of Ala, and generating SufU.S. A mixture of SufS, SufU, Fra and L-cysteine is able to reconstitute Fe-S clusters on apo-aconitase (citB), reconstituting aconitase activity.[1] [2] [3] References
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