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5u7f
From Proteopedia
(Difference between revisions)
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==Co-bound dihydroneopterin triphosphate pyrophosphohydrolase from E. coli== | ==Co-bound dihydroneopterin triphosphate pyrophosphohydrolase from E. coli== | ||
| - | <StructureSection load='5u7f' size='340' side='right' caption='[[5u7f]], [[Resolution|resolution]] 1.79Å' scene=''> | + | <StructureSection load='5u7f' size='340' side='right'caption='[[5u7f]], [[Resolution|resolution]] 1.79Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[5u7f]] is a 1 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[5u7f]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Eco57 Eco57]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5U7F OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5U7F FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CO:COBALT+(II)+ION'>CO</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CO:COBALT+(II)+ION'>CO</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5u7e|5u7e]], [[5u7h|5u7h]]</td></tr> | + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[5u7e|5u7e]], [[5u7h|5u7h]]</div></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">nudB, Z2917, ECs2575 ([ | + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">nudB, Z2917, ECs2575 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83334 ECO57])</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/Dihydroneopterin_triphosphate_diphosphatase Dihydroneopterin triphosphate diphosphatase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.1.67 3.6.1.67] </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=5u7f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5u7f OCA], [https://pdbe.org/5u7f PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5u7f RCSB], [https://www.ebi.ac.uk/pdbsum/5u7f PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5u7f ProSAT]</span></td></tr> |
</table> | </table> | ||
== Function == | == Function == | ||
| - | [[ | + | [[https://www.uniprot.org/uniprot/NUDB_ECO57 NUDB_ECO57]] Catalyzes the hydrolysis of dihydroneopterin triphosphate to dihydroneopterin monophosphate and pyrophosphate. Required for efficient folate biosynthesis. Can also hydrolyze nucleoside triphosphates with a preference for dATP.[UniProtKB:P0AFC0] |
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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[[Category: Dihydroneopterin triphosphate diphosphatase]] | [[Category: Dihydroneopterin triphosphate diphosphatase]] | ||
[[Category: Eco57]] | [[Category: Eco57]] | ||
| + | [[Category: Large Structures]] | ||
[[Category: Hill, S E]] | [[Category: Hill, S E]] | ||
[[Category: Lieberman, R L]] | [[Category: Lieberman, R L]] | ||
Revision as of 07:06, 16 March 2022
Co-bound dihydroneopterin triphosphate pyrophosphohydrolase from E. coli
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