4a59: Difference between revisions

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 <StructureSection load='4a59' size='340' side='right'caption='[[4a59]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[4a59]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Toxgo Toxgo]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4A59 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4A59 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[4a59]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Toxgo Toxgo]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4A59 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4A59 FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=AMP:ADENOSINE+MONOPHOSPHATE'>AMP</scene></td></tr>
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=AMP:ADENOSINE+MONOPHOSPHATE'>AMP</scene></td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4a5a|4a5a]], [[4a57|4a57]], [[4a5b|4a5b]]</td></tr>
+<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[4a5a|4a5a]], [[4a57|4a57]], [[4a5b|4a5b]]</div></td></tr>
-<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Apyrase Apyrase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.1.5 3.6.1.5] </span></td></tr>
+<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Apyrase Apyrase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.1.5 3.6.1.5] </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=4a59 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4a59 OCA], [http://pdbe.org/4a59 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4a59 RCSB], [http://www.ebi.ac.uk/pdbsum/4a59 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4a59 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=4a59 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4a59 OCA], [https://pdbe.org/4a59 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4a59 RCSB], [https://www.ebi.ac.uk/pdbsum/4a59 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4a59 ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/NTP1_TOXGO NTP1_TOXGO]] May perform an important processing step in the conversion of high energy nucleotides prior to uptake by the parasite and may contribute to intracellular survival and virulence. NTPAse-I has a specific activity 4.5-fold higher than NTPAse-II in hydrolysis of ATP. The primary difference between these isozymes lies in their ability to hydrolyze nucleoside triphosphate versus diphosphate substrates. While NTPAse-II hydrolyzes ATP to ADP and ADP to AMP at almost the same rate, NTPAse-I hydrolyzes ADP to AMP at a much slower rate (0.7% of the rate for ATP).
+[[https://www.uniprot.org/uniprot/NTP1_TOXGO NTP1_TOXGO]] May perform an important processing step in the conversion of high energy nucleotides prior to uptake by the parasite and may contribute to intracellular survival and virulence. NTPAse-I has a specific activity 4.5-fold higher than NTPAse-II in hydrolysis of ATP. The primary difference between these isozymes lies in their ability to hydrolyze nucleoside triphosphate versus diphosphate substrates. While NTPAse-II hydrolyzes ATP to ADP and ADP to AMP at almost the same rate, NTPAse-I hydrolyzes ADP to AMP at a much slower rate (0.7% of the rate for ATP).
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
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 ==See Also==
 *[[Ectonucleoside triphosphate diphosphohydrolase|Ectonucleoside triphosphate diphosphohydrolase]]
+*[[Nucleoside triphosphatase|Nucleoside triphosphatase]]
+*[[Sandbox 30008|Sandbox 30008]]
 == References ==
 <references/>
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 </StructureSection>
 [[Category: Apyrase]]
+[[Category: Large Structures]]
 [[Category: Toxgo]]
 [[Category: Krug, U]]