This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


1pu8

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (09:47, 16 August 2023) (edit) (undo)
 
(2 intermediate revisions not shown.)
Line 1: Line 1:
==Crystal structure of H.pylori 3-methyladenine DNA glycosylase (MagIII) bound to 1,N6-ethenoadenine==
==Crystal structure of H.pylori 3-methyladenine DNA glycosylase (MagIII) bound to 1,N6-ethenoadenine==
-
<StructureSection load='1pu8' size='340' side='right' caption='[[1pu8]], [[Resolution|resolution]] 2.13&Aring;' scene=''>
+
<StructureSection load='1pu8' size='340' side='right'caption='[[1pu8]], [[Resolution|resolution]] 2.13&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
-
<table><tr><td colspan='2'>[[1pu8]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_43504 Atcc 43504]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PU8 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1PU8 FirstGlance]. <br>
+
<table><tr><td colspan='2'>[[1pu8]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Helicobacter_pylori Helicobacter pylori]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PU8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1PU8 FirstGlance]. <br>
-
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BME:BETA-MERCAPTOETHANOL'>BME</scene>, <scene name='pdbligand=EA1:3H-IMIDAZO[2,1-I]PURINE'>EA1</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]] 2.13&#8491;</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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BME:BETA-MERCAPTOETHANOL'>BME</scene>, <scene name='pdbligand=EA1:3H-IMIDAZO[2,1-I]PURINE'>EA1</scene>, <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]], [[1pu7|1pu7]]</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=1pu8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1pu8 OCA], [https://pdbe.org/1pu8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1pu8 RCSB], [https://www.ebi.ac.uk/pdbsum/1pu8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1pu8 ProSAT]</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=1pu8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1pu8 OCA], [http://pdbe.org/1pu8 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1pu8 RCSB], [http://www.ebi.ac.uk/pdbsum/1pu8 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1pu8 ProSAT]</span></td></tr>
+
</table>
</table>
== Function ==
== Function ==
-
[[http://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]
+
[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]]
Line 30: Line 29:
</div>
</div>
<div class="pdbe-citations 1pu8" style="background-color:#fffaf0;"></div>
<div class="pdbe-citations 1pu8" style="background-color:#fffaf0;"></div>
 +
 +
==See Also==
 +
*[[DNA glycosylase 3D structures|DNA glycosylase 3D structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
-
[[Category: Atcc 43504]]
+
[[Category: Helicobacter pylori]]
-
[[Category: Eichman, B F]]
+
[[Category: Large Structures]]
-
[[Category: Ellenberger, T]]
+
[[Category: Eichman BF]]
-
[[Category: Radicella, J P]]
+
[[Category: Ellenberger T]]
-
[[Category: Rourke, E J.O]]
+
[[Category: O'Rourke EJ]]
-
[[Category: 3-methyladenine]]
+
[[Category: Radicella JP]]
-
[[Category: Base excision repair]]
+
-
[[Category: Glycosylase]]
+
-
[[Category: Helix-hairpin-helix]]
+
-
[[Category: Hydrolase]]
+

Current revision

Crystal structure of H.pylori 3-methyladenine DNA glycosylase (MagIII) bound to 1,N6-ethenoadenine

PDB ID 1pu8

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1pu8"
Personal tools