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Structure paper

TitleThe CDK9 C-helix Exhibits Conformational Plasticity That May Explain the Selectivity of CAN508.
Journal, issue, pagesAcs Chem. Biol., Vol. 7, Page 811-816, Year 2012
Publish dateSep 1, 2011 (structure data deposition date)
AuthorsBaumli, S. / Hole, A.J. / Noble, M.E. / Endicott, J.A.
External linksAcs Chem. Biol. / PubMed:22292676
MethodsX-ray diffraction
Resolution2 - 3.234 Å
Structure data

PDB-3tn8:
CDK9/cyclin T in complex with CAN508
Method: X-RAY DIFFRACTION / Resolution: 2.95 Å

PDB-3tnh:
CDK9/cyclin T in complex with CAN508
Method: X-RAY DIFFRACTION / Resolution: 3.202 Å

PDB-3tni:
structure of CDK9/cyclin T F241L
Method: X-RAY DIFFRACTION / Resolution: 3.234 Å

PDB-3tnw:
Structure of CDK2/cyclin A in complex with CAN508
Method: X-RAY DIFFRACTION / Resolution: 2 Å

Chemicals

ChemComp-PO4:
PHOSPHATE ION

ChemComp-F18:
4-[(E)-(3,5-DIAMINO-1H-PYRAZOL-4-YL)DIAZENYL]PHENOL

ChemComp-GOL:
GLYCEROL

ChemComp-HOH:
WATER

ChemComp-NA:
Unknown entry

Source
  • homo sapiens (human)
  • bos taurus (domestic cattle)
KeywordsTRANSFERASE/TRANSFERASE INHIBITOR / cyclin dependent kinase / Kinase / cyclin / phosphotransfer / CDK-cyclin complex / TRANSFERASE-TRANSFERASE INHIBITOR complex / phosphtransfer / cyclin T / phosphorylated on threonine 186 / kinase cyclin / phosphotransferase / cyclin A / phosphorylation at CDK2 threonine 160

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