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1pu7
From Proteopedia
(Difference between revisions)
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<StructureSection load='1pu7' size='340' side='right'caption='[[1pu7]], [[Resolution|resolution]] 1.93Å' scene=''> | <StructureSection load='1pu7' size='340' side='right'caption='[[1pu7]], [[Resolution|resolution]] 1.93Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[1pu7]] is a 2 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[1pu7]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_43504 Atcc 43504]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PU7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1PU7 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=39A:6-AMINO-3,9-DIMETHYL-9H-PURIN-3-IUM'>39A</scene>, <scene name='pdbligand=BME:BETA-MERCAPTOETHANOL'>BME</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=39A:6-AMINO-3,9-DIMETHYL-9H-PURIN-3-IUM'>39A</scene>, <scene name='pdbligand=BME:BETA-MERCAPTOETHANOL'>BME</scene></td></tr> |
<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=KCX:LYSINE+NZ-CARBOXYLIC+ACID'>KCX</scene></td></tr> | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=KCX:LYSINE+NZ-CARBOXYLIC+ACID'>KCX</scene></td></tr> | ||
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1pu6|1pu6]], [[1pu8|1pu8]]</td></tr> | + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1pu6|1pu6]], [[1pu8|1pu8]]</div></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=1pu7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1pu7 OCA], [https://pdbe.org/1pu7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1pu7 RCSB], [https://www.ebi.ac.uk/pdbsum/1pu7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1pu7 ProSAT]</span></td></tr> |
</table> | </table> | ||
== Function == | == Function == | ||
| - | [[ | + | [[https://www.uniprot.org/uniprot/O25323_HELPY O25323_HELPY]] DNA repair enzyme that has both DNA N-glycosylase activity and AP-lyase activity (By similarity).[PIRNR:PIRNR001435] |
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
Revision as of 09:34, 8 September 2021
Crystal structure of H.pylori 3-methyladenine DNA glycosylase (MagIII) bound to 3,9-dimethyladenine
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