5efq: Difference between revisions

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 ==Crystal structure of human Cdk13/Cyclin K in complex with ADP-aluminum fluoride==
-<StructureSection load='5efq' size='340' side='right' caption='[[5efq]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
+<StructureSection load='5efq' size='340' side='right'caption='[[5efq]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[5efq]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5EFQ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5EFQ FirstGlance]. <br>
+<table><tr><td colspan='2'>[[5efq]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5EFQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5EFQ FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=AF3:ALUMINUM+FLUORIDE'>AF3</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]] 2&#8491;</td></tr>
-<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=TPO:PHOSPHOTHREONINE'>TPO</scene></td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=AF3:ALUMINUM+FLUORIDE'>AF3</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=TPO:PHOSPHOTHREONINE'>TPO</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=5efq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5efq OCA], [http://pdbe.org/5efq PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5efq RCSB], [http://www.ebi.ac.uk/pdbsum/5efq 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=5efq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5efq OCA], [https://pdbe.org/5efq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5efq RCSB], [https://www.ebi.ac.uk/pdbsum/5efq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5efq ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/CDK13_HUMAN CDK13_HUMAN]] Cyclin-dependent kinase which displays CTD kinase activity and is required for RNA splicing. Has CTD kinase activity by hyperphosphorylating the C-terminal heptapeptide repeat domain (CTD) of the largest RNA polymerase II subunit RPB1, thereby acting as a key regulator of transcription elongation. Required for RNA splicing, probably by phosphorylating SRSF1/SF2. Required during hematopoiesis. In case of infection by HIV-1 virus, interacts with HIV-1 Tat protein acetylated at 'Lys-50' and 'Lys-51', thereby increasing HIV-1 mRNA splicing and promoting the production of the doubly spliced HIV-1 protein Nef.<ref>PMID:16721827</ref> <ref>PMID:1731328</ref> <ref>PMID:18480452</ref> <ref>PMID:20952539</ref>  [[http://www.uniprot.org/uniprot/CCNK_HUMAN CCNK_HUMAN]] May play a role in transcriptional regulation. In vitro, is associated with a kinase activity toward both RNA polymerase II C-terminal domain and CDK2 (CAK).<ref>PMID:10574912</ref>
+[https://www.uniprot.org/uniprot/CDK13_HUMAN CDK13_HUMAN] Cyclin-dependent kinase which displays CTD kinase activity and is required for RNA splicing. Has CTD kinase activity by hyperphosphorylating the C-terminal heptapeptide repeat domain (CTD) of the largest RNA polymerase II subunit RPB1, thereby acting as a key regulator of transcription elongation. Required for RNA splicing, probably by phosphorylating SRSF1/SF2. Required during hematopoiesis. In case of infection by HIV-1 virus, interacts with HIV-1 Tat protein acetylated at 'Lys-50' and 'Lys-51', thereby increasing HIV-1 mRNA splicing and promoting the production of the doubly spliced HIV-1 protein Nef.<ref>PMID:16721827</ref> <ref>PMID:1731328</ref> <ref>PMID:18480452</ref> <ref>PMID:20952539</ref>
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 18: / Line 19: @@
 </div>
 <div class="pdbe-citations 5efq" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[Cyclin 3D structures|Cyclin 3D structures]]
+*[[Cyclin-dependent kinase 3D structures|Cyclin-dependent kinase 3D structures]]
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Anand, K]]
+[[Category: Homo sapiens]]
-[[Category: Geyer, M]]
+[[Category: Large Structures]]
-[[Category: Greifenberg, A K]]
+[[Category: Anand K]]
-[[Category: Hoenig, D]]
+[[Category: Geyer M]]
-[[Category: Adp]]
+[[Category: Greifenberg AK]]
-[[Category: Cyclin]]
+[[Category: Hoenig D]]
-[[Category: Kinase]]
-[[Category: Transferase]]