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TitleA Back-to-Front Fragment-Based Drug Design Search Strategy Targeting the DFG-Out Pocket of Protein Tyrosine Kinases.
Journal, issue, pagesACS MED. CHEM. LETT., Vol. 3, Page 342-346, Year 2012
Publish dateAug 25, 2011 (structure data deposition date)
AuthorsIwata, H. / Oki, H. / Okada, K. / Takagi, T. / Tawada, M. / Miyazaki, Y. / Imamura, S. / Hori, A. / Lawson, J.D. / Hixon, M.S. ...Iwata, H. / Oki, H. / Okada, K. / Takagi, T. / Tawada, M. / Miyazaki, Y. / Imamura, S. / Hori, A. / Lawson, J.D. / Hixon, M.S. / Kimura, H. / Miki, H.
External linksACS MED. CHEM. LETT. / PubMed:24900475
MethodsX-ray diffraction
Resolution2.3 - 2.49 Å
Structure data

PDB-3vhk:
Crystal structure of the VEGFR2 kinase domain in complex with a back pocket binder
Method: X-RAY DIFFRACTION / Resolution: 2.49 Å

PDB-3vid:
Crystal structure of human VEGFR2 kinase domain with Compound A.
Method: X-RAY DIFFRACTION / Resolution: 2.3 Å

Chemicals

ChemComp-BPK:
{3-[(5-methyl-2-phenyl-1,3-oxazol-4-yl)methoxy]phenyl}methanol

ChemComp-EDO:
1,2-ETHANEDIOL

ChemComp-HOH:
WATER

ChemComp-4TT:
4,5,6,11-tetrahydro-1H-pyrazolo[4',3':6,7]cyclohepta[1,2-b]indole

Source
  • homo sapiens (human)
KeywordsTRANSFERASE / vegfr2 / kinase domain / complex / KINASE / PHOSPHORYLATION

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