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.


5jkr

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (18:57, 20 September 2023) (edit) (undo)
 
Line 3: Line 3:
<StructureSection load='5jkr' size='340' side='right'caption='[[5jkr]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
<StructureSection load='5jkr' size='340' side='right'caption='[[5jkr]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
-
<table><tr><td colspan='2'>[[5jkr]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Vaccc Vaccc]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5JKR OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5JKR FirstGlance]. <br>
+
<table><tr><td colspan='2'>[[5jkr]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Vaccinia_virus_Copenhagen Vaccinia virus Copenhagen]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5JKR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5JKR FirstGlance]. <br>
-
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</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]] 2.6&#8491;</td></tr>
-
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">UNG, D4R ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10249 VACCC]), A20R ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10249 VACCC])</td></tr>
+
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
-
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Uracil-DNA_glycosylase Uracil-DNA glycosylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.2.27 3.2.2.27] </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=5jkr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5jkr OCA], [https://pdbe.org/5jkr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5jkr RCSB], [https://www.ebi.ac.uk/pdbsum/5jkr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5jkr ProSAT]</span></td></tr>
-
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5jkr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5jkr OCA], [http://pdbe.org/5jkr PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5jkr RCSB], [http://www.ebi.ac.uk/pdbsum/5jkr PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5jkr ProSAT]</span></td></tr>
+
</table>
</table>
== Function ==
== Function ==
-
[[http://www.uniprot.org/uniprot/UNG_VACCC UNG_VACCC]] Excises uracil residues from the DNA which can arise as a result of misincorporation of dUMP residues by DNA polymerase or due to deamination of cytosine. Also part of a heterodimeric processivity factor which potentiates the DNA polymerase activity. Binds to DNA (By similarity). [[http://www.uniprot.org/uniprot/A20_VACCC A20_VACCC]] Plays an essential role in viral DNA replication by acting as the polymerase processivity factor together with protein D4. May serve as a bridge which links the DNA polymerase E9 and the uracil DNA glycosylase (By similarity).
+
[https://www.uniprot.org/uniprot/UNG_VACCC UNG_VACCC] Excises uracil residues from the DNA which can arise as a result of misincorporation of dUMP residues by DNA polymerase or due to deamination of cytosine. Also part of a heterodimeric processivity factor which potentiates the DNA polymerase activity. Binds to DNA (By similarity).
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
Line 28: Line 27:
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
-
[[Category: Uracil-DNA glycosylase]]
+
[[Category: Vaccinia virus Copenhagen]]
-
[[Category: Vaccc]]
+
[[Category: Brazzolotto X]]
-
[[Category: Brazzolotto, X]]
+
[[Category: Burmeister WP]]
-
[[Category: Burmeister, W P]]
+
[[Category: Contesto-Richefeu C]]
-
[[Category: Contesto-Richefeu, C]]
+
[[Category: Iseni F]]
-
[[Category: Iseni, F]]
+
[[Category: Peyrefitte CN]]
-
[[Category: Peyrefitte, C N]]
+
[[Category: Tarbouriech N]]
-
[[Category: Tarbouriech, N]]
+
-
[[Category: Dna binding]]
+
-
[[Category: Dna polymerase binding]]
+
-
[[Category: Dna polymerase processivity factor]]
+
-
[[Category: Hydrolase-replication complex]]
+

Current revision

vaccinia virus D4/A20(1-50)w43a mutant

PDB ID 5jkr

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools