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Structure paper

TitleExploiting an allosteric binding site of PRMT3 yields potent and selective inhibitors.
Journal, issue, pagesJ. Med. Chem., Vol. 56, Page 2110-2124, Year 2013
Publish dateOct 30, 2012 (structure data deposition date)
AuthorsLiu, F. / Li, F. / Ma, A. / Dobrovetsky, E. / Dong, A. / Gao, C. / Korboukh, I. / Liu, J. / Smil, D. / Brown, P.J. ...Liu, F. / Li, F. / Ma, A. / Dobrovetsky, E. / Dong, A. / Gao, C. / Korboukh, I. / Liu, J. / Smil, D. / Brown, P.J. / Frye, S.V. / Arrowsmith, C.H. / Schapira, M. / Vedadi, M. / Jin, J.
External linksJ. Med. Chem. / PubMed:23445220
MethodsX-ray diffraction
Resolution2.3 Å
Structure data

PDB-4hsg:
Crystal structure of human PRMT3 in complex with an allosteric inhibitor (PRMT3- KTD)
Method: X-RAY DIFFRACTION / Resolution: 2.3 Å

Chemicals

ChemComp-KTD:
1-(1,2,3-benzothiadiazol-6-yl)-3-(2-oxo-2-phenylethyl)urea

ChemComp-UNX:
Unknown entry

ChemComp-HOH:
WATER

Source
  • homo sapiens (human)
KeywordsTRANSFERASE/TRANSFERASE INHIBITOR / PRMT3 / allosteric inhibitor / Structural Genomics / Structural Genomics Consortium / SGC / TRANSFERASE-TRANSFERASE INHIBITOR complex

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