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1zun
From Proteopedia
(Difference between revisions)
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==Crystal Structure of a GTP-Regulated ATP Sulfurylase Heterodimer from Pseudomonas syringae== | ==Crystal Structure of a GTP-Regulated ATP Sulfurylase Heterodimer from Pseudomonas syringae== | ||
| - | <StructureSection load='1zun' size='340' side='right' caption='[[1zun]], [[Resolution|resolution]] 2.70Å' scene=''> | + | <StructureSection load='1zun' size='340' side='right'caption='[[1zun]], [[Resolution|resolution]] 2.70Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[1zun]] is a 2 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[1zun]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_19310 Atcc 19310] and [https://en.wikipedia.org/wiki/Psesm Psesm]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ZUN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ZUN FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=AGS:PHOSPHOTHIOPHOSPHORIC+ACID-ADENYLATE+ESTER'>AGS</scene>, <scene name='pdbligand=GDP:GUANOSINE-5-DIPHOSPHATE'>GDP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=AGS:PHOSPHOTHIOPHOSPHORIC+ACID-ADENYLATE+ESTER'>AGS</scene>, <scene name='pdbligand=GDP:GUANOSINE-5-DIPHOSPHATE'>GDP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr> |
<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> | ||
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">cysD ([ | + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">cysD ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=317 ATCC 19310]), cysNC ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=223283 PSESM])</td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Sulfate_adenylyltransferase Sulfate adenylyltransferase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.7.4 2.7.7.4] </span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1zun FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1zun OCA], [https://pdbe.org/1zun PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1zun RCSB], [https://www.ebi.ac.uk/pdbsum/1zun PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1zun ProSAT]</span></td></tr> |
</table> | </table> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Atcc 19310]] | [[Category: Atcc 19310]] | ||
| + | [[Category: Large Structures]] | ||
[[Category: Psesm]] | [[Category: Psesm]] | ||
[[Category: Sulfate adenylyltransferase]] | [[Category: Sulfate adenylyltransferase]] | ||
Revision as of 08:17, 27 January 2021
Crystal Structure of a GTP-Regulated ATP Sulfurylase Heterodimer from Pseudomonas syringae
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