6skz
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Structure of the closed conformation of CtTel1== | |
| - | + | <StructureSection load='6skz' size='340' side='right'caption='[[6skz]], [[Resolution|resolution]] 3.40Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[6skz]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Chaetomium_thermophilum_(strain_dsm_1495_/_cbs_144.50_/_imi_039719) Chaetomium thermophilum (strain dsm 1495 / cbs 144.50 / imi 039719)]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6SKZ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6SKZ FirstGlance]. <br> | |
| - | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=AGS:PHOSPHOTHIOPHOSPHORIC+ACID-ADENYLATE+ESTER'>AGS</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> | |
| - | [[Category: | + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Non-specific_serine/threonine_protein_kinase Non-specific serine/threonine protein kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.11.1 2.7.11.1] </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=6skz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6skz OCA], [http://pdbe.org/6skz PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6skz RCSB], [http://www.ebi.ac.uk/pdbsum/6skz PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6skz ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/G0S4S9_CHATD G0S4S9_CHATD]] Serine/threonine protein kinase which activates checkpoint signaling upon genotoxic stresses such as ionizing radiation (IR), ultraviolet light (UV), or DNA replication stalling, thereby acting as a DNA damage sensor. Recognizes the substrate consensus sequence [ST]-Q. Phosphorylates histone H2A to form H2AS128ph (gamma-H2A) at sites of DNA damage, involved in the regulation of DNA damage response mechanism. Required for the control of telomere length and genome stability.[RuleBase:RU365027] | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Non-specific serine/threonine protein kinase]] | ||
| + | [[Category: Eustermann, S E]] | ||
| + | [[Category: Hopfner, K P]] | ||
| + | [[Category: Jansma, M]] | ||
| + | [[Category: Kostrewa, D]] | ||
| + | [[Category: Lammens, K]] | ||
| + | [[Category: Alpha solenoid]] | ||
| + | [[Category: Dimer]] | ||
| + | [[Category: Dna damage signaling]] | ||
| + | [[Category: Kinase]] | ||
| + | [[Category: Nucleus]] | ||
| + | [[Category: Pikk]] | ||
| + | [[Category: Tranferase]] | ||
| + | [[Category: Transferase]] | ||
Revision as of 09:10, 30 October 2019
Structure of the closed conformation of CtTel1
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