7xek: Difference between revisions
Jump to navigation
Jump to search
No edit summary |
No edit summary |
||
(One intermediate revision by the same user not shown) | |||
Line 1: | Line 1: | ||
==SufS with D-cysteine for | ==SufS with D-cysteine for 30 min== | ||
<StructureSection load='7xek' size='340' side='right'caption='[[7xek]], [[Resolution|resolution]] 1.88Å' scene=''> | <StructureSection load='7xek' size='340' side='right'caption='[[7xek]], [[Resolution|resolution]] 1.88Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[7xek]] 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=7XEK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7XEK FirstGlance]. <br> | <table><tr><td colspan='2'>[[7xek]] 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=7XEK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7XEK FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=9YX:(2~{S},4~{S})-2-[2-methyl-3-oxidanyl-5-(phosphonooxymethyl)pyridin-4-yl]-1,3-thiazolidine-4-carboxylic+acid'>9YX</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=PG4:TETRAETHYLENE+GLYCOL'>PG4</scene>, <scene name='pdbligand=PGE:TRIETHYLENE+GLYCOL'>PGE</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]] 1.88Å</td></tr> | ||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=9YX:(2~{S},4~{S})-2-[2-methyl-3-oxidanyl-5-(phosphonooxymethyl)pyridin-4-yl]-1,3-thiazolidine-4-carboxylic+acid'>9YX</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=PG4:TETRAETHYLENE+GLYCOL'>PG4</scene>, <scene name='pdbligand=PGE:TRIETHYLENE+GLYCOL'>PGE</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=7xek FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7xek OCA], [https://pdbe.org/7xek PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7xek RCSB], [https://www.ebi.ac.uk/pdbsum/7xek PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7xek 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=7xek FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7xek OCA], [https://pdbe.org/7xek PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7xek RCSB], [https://www.ebi.ac.uk/pdbsum/7xek PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7xek ProSAT]</span></td></tr> | ||
</table> | </table> |
Latest revision as of 14:48, 30 October 2024
SufS with D-cysteine for 30 minSufS with D-cysteine for 30 min
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
|
|