2ckc: Difference between revisions
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<StructureSection load='2ckc' size='340' side='right'caption='[[2ckc]], [[NMR_Ensembles_of_Models | 25 NMR models]]' scene=''> | <StructureSection load='2ckc' size='340' side='right'caption='[[2ckc]], [[NMR_Ensembles_of_Models | 25 NMR models]]' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2ckc]] is a 1 chain structure with sequence from [ | <table><tr><td colspan='2'>[[2ckc]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2CKC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2CKC FirstGlance]. <br> | ||
</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | </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=2ckc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ckc OCA], [https://pdbe.org/2ckc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ckc RCSB], [https://www.ebi.ac.uk/pdbsum/2ckc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ckc ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
Revision as of 06:57, 1 December 2021
Solution structures of the BRK domains of the human Chromo Helicase Domain 7 and 8, reveals structural similarity with GYF domain suggesting a role in protein interaction
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Proteopedia Page Contributors and Editors (what is this?)
Categories:
- Human
- Large Structures
- Ab, E
- Daniels, M
- Diercks, T
- Folkers, G E
- Jong, R N.de
- Kaptein, R
- Xiaoyun, J
- Atp-binding
- Brk domain
- Chromatin regulator
- Chromatin remodeling
- Disease mutation
- Dna-binding
- Helicase
- Hydrolase
- Nuclear protein
- Nucleotide-binding
- Phosphorylation
- Protein-protein interaction
- Transcription
- Transcription elongation
- Transcription regulation
