2ckc: Difference between revisions
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|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
|DOMAIN= | |||
|RELATEDENTRY= | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2ckc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ckc OCA], [http://www.ebi.ac.uk/pdbsum/2ckc PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2ckc RCSB]</span> | |||
}} | }} | ||
'''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''' | '''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''' | ||
==About this Structure== | ==About this Structure== | ||
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[[Category: transcription regulation]] | [[Category: transcription regulation]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 02:22:44 2008'' | ||
Revision as of 02:22, 31 March 2008
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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
About this StructureAbout this Structure
2CKC is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Page seeded by OCA on Mon Mar 31 02:22:44 2008
Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)
OCACategories:
- Pages with broken file links
- Homo sapiens
- Single protein
- 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