2pvm

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<StructureSection load='2pvm' size='340' side='right'caption='[[2pvm]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
<StructureSection load='2pvm' size='340' side='right'caption='[[2pvm]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[2pvm]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Maize Maize]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2PVM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2PVM FirstGlance]. <br>
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<table><tr><td colspan='2'>[[2pvm]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Zea_mays Zea mays]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2PVM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2PVM FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=P29:4-(2-(1H-IMIDAZOL-4-YL)ETHYLAMINO)-2-(PHENYLAMINO)PYRAZOLO[1,5-A][1,3,5]TRIAZINE-8-CARBONITRILE'>P29</scene></td></tr>
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</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>
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<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=CSO:S-HYDROXYCYSTEINE'>CSO</scene></td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CSO:S-HYDROXYCYSTEINE'>CSO</scene>, <scene name='pdbligand=P29:4-(2-(1H-IMIDAZOL-4-YL)ETHYLAMINO)-2-(PHENYLAMINO)PYRAZOLO[1,5-A][1,3,5]TRIAZINE-8-CARBONITRILE'>P29</scene></td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2pvh|2pvh]], [[2pvj|2pvj]], [[2pvk|2pvk]], [[2pvl|2pvl]], [[2pvn|2pvn]]</div></td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ACK2 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4577 MAIZE])</td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Non-specific_serine/threonine_protein_kinase Non-specific serine/threonine protein kinase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.11.1 2.7.11.1] </span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2pvm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2pvm OCA], [https://pdbe.org/2pvm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2pvm RCSB], [https://www.ebi.ac.uk/pdbsum/2pvm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2pvm ProSAT]</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=2pvm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2pvm OCA], [https://pdbe.org/2pvm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2pvm RCSB], [https://www.ebi.ac.uk/pdbsum/2pvm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2pvm ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[https://www.uniprot.org/uniprot/CSK2A_MAIZE CSK2A_MAIZE]] Casein kinases are operationally defined by their preferential utilization of acidic proteins such as caseins as substrates. The alpha chain contains the catalytic site.
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[https://www.uniprot.org/uniprot/CSK2A_MAIZE CSK2A_MAIZE] Casein kinases are operationally defined by their preferential utilization of acidic proteins such as caseins as substrates. The alpha chain contains the catalytic site.
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Maize]]
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[[Category: Zea mays]]
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[[Category: Non-specific serine/threonine protein kinase]]
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[[Category: Almassy R]]
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[[Category: Almassy, R]]
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[[Category: Averill A]]
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[[Category: Averill, A]]
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[[Category: Chu S]]
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[[Category: Chu, S]]
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[[Category: Erickson P]]
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[[Category: Erickson, P]]
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[[Category: Lu J]]
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[[Category: Lu, J]]
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[[Category: Margosiak S]]
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[[Category: Margosiak, S]]
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[[Category: Nie Z]]
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[[Category: Nie, Z]]
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[[Category: Perretta C]]
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[[Category: Perretta, C]]
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[[Category: Yager KM]]
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[[Category: Yager, K M]]
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[[Category: Casein kinase ii]]
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[[Category: Enzyme-inhibitor complex]]
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[[Category: Protein kinase ck2]]
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[[Category: Structure-based drug design]]
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[[Category: Transferase]]
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Revision as of 11:09, 30 August 2023

Structure-Based Design of Pyrazolo[1,5-a][1,3,5]triazine Derivatives as Potent Inhibitors of Protein Kinase CK2

PDB ID 2pvm

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