3zvm

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (11:14, 20 December 2023) (edit) (undo)
 
(4 intermediate revisions not shown.)
Line 1: Line 1:
-
==THE STRUCTURAL BASIS FOR SUBSTRATE RECOGNITION BY MAMMALIAN POLYNUCLEOTIDE KINASE 3' PHOSPHATASE==
+
 
-
<StructureSection load='3zvm' size='340' side='right' caption='[[3zvm]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
+
==The structural basis for substrate recognition by mammalian polynucleotide kinase 3' phosphatase==
 +
<StructureSection load='3zvm' size='340' side='right'caption='[[3zvm]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
-
<table><tr><td colspan='2'>[[3zvm]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3ZVM OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3ZVM FirstGlance]. <br>
+
<table><tr><td colspan='2'>[[3zvm]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus] and [https://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3ZVM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3ZVM FirstGlance]. <br>
-
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=EPE:4-(2-HYDROXYETHYL)-1-PIPERAZINE+ETHANESULFONIC+ACID'>EPE</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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]] 1.997&#8491;</td></tr>
-
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1ujx|1ujx]], [[3zvl|3zvl]], [[1yj5|1yj5]], [[1yjm|1yjm]], [[3zvn|3zvn]]</td></tr>
+
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=EPE:4-(2-HYDROXYETHYL)-1-PIPERAZINE+ETHANESULFONIC+ACID'>EPE</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></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=3zvm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3zvm OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3zvm RCSB], [http://www.ebi.ac.uk/pdbsum/3zvm PDBsum]</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=3zvm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3zvm OCA], [https://pdbe.org/3zvm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3zvm RCSB], [https://www.ebi.ac.uk/pdbsum/3zvm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3zvm ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
-
[[http://www.uniprot.org/uniprot/PNKP_MOUSE PNKP_MOUSE]] Plays a key role in the repair of DNA damage, functioning as part of both the non-homologous end-joining (NHEJ) and base excision repair (BER) pathways. Through its two catalytic activities, PNK ensures that DNA termini are compatible with extension and ligation by either removing 3'-phosphates from, or by phosphorylating 5'-hydroxyl groups on, the ribose sugar of the DNA backbone.
+
[https://www.uniprot.org/uniprot/PNKP_MOUSE PNKP_MOUSE] Plays a key role in the repair of DNA damage, functioning as part of both the non-homologous end-joining (NHEJ) and base excision repair (BER) pathways. Through its two catalytic activities, PNK ensures that DNA termini are compatible with extension and ligation by either removing 3'-phosphates from, or by phosphorylating 5'-hydroxyl groups on, the ribose sugar of the DNA backbone.
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
Line 17: Line 18:
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
</div>
 +
<div class="pdbe-citations 3zvm" style="background-color:#fffaf0;"></div>
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
 +
[[Category: Large Structures]]
[[Category: Mus musculus]]
[[Category: Mus musculus]]
-
[[Category: Garces, F]]
+
[[Category: Synthetic construct]]
-
[[Category: Oliver, A W]]
+
[[Category: Garces F]]
-
[[Category: Pearl, L H]]
+
[[Category: Oliver AW]]
-
[[Category: Base excision repair]]
+
[[Category: Pearl LH]]
-
[[Category: Ber]]
+
-
[[Category: Cancer]]
+
-
[[Category: Dna repair]]
+
-
[[Category: Hydrolase-transferase-dna complex]]
+
-
[[Category: Nhej]]
+
-
[[Category: Non-homologous end-joining]]
+

Current revision

The structural basis for substrate recognition by mammalian polynucleotide kinase 3' phosphatase

PDB ID 3zvm

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/3zvm"
Personal tools