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TitleFrom Fragment to Lead: De Novo Design and Development toward a Selective FGFR2 Inhibitor.
Journal, issue, pagesJ. Med. Chem., Vol. 65, Page 1481-1504, Year 2022
Publish dateJun 27, 2021 (structure data deposition date)
AuthorsTurner, L.D. / Trinh, C.H. / Hubball, R.A. / Orritt, K.M. / Lin, C.C. / Burns, J.E. / Knowles, M.A. / Fishwick, C.W.G.
External linksJ. Med. Chem. / PubMed:34780700
MethodsX-ray diffraction
Resolution1.71 - 2.28 Å
Structure data

PDB-7ozb:
FGFR1 kinase domain (residues 458-765) with mutations C488A, C584S in complex with 38.
Method: X-RAY DIFFRACTION / Resolution: 1.71 Å

PDB-7ozd:
FGFR1 kinase domain (residues 458-765) with mutations C488A, C584S in complex with 34.
Method: X-RAY DIFFRACTION / Resolution: 1.82 Å

PDB-7ozf:
FGFR1 kinase domain (residues 458-765) with mutations C488A, C584S in complex with 19.
Method: X-RAY DIFFRACTION / Resolution: 1.82 Å

PDB-7ozy:
FGFR2 kinase domain (residues 461-763) in complex with 38.
Method: X-RAY DIFFRACTION / Resolution: 2.28 Å

Chemicals

ChemComp-47I:
4-[3-(4-piperazin-4-ium-1-ylphenyl)-1H-indazol-6-yl]phenol

ChemComp-SO4:
SULFATE ION

ChemComp-EDO:
1,2-ETHANEDIOL

ChemComp-HOH:
WATER

ChemComp-42I:
N-[6-(4-hydroxyphenyl)-1H-indazol-3-yl]benzamide

ChemComp-466:
N-[6-(3-ethoxyphenyl)-1H-indazol-3-yl]benzamide

ChemComp-CL:
Unknown entry

Source
  • homo sapiens (human)
KeywordsTRANSFERASE / FGFR1 / Inhibitor / receptor tyrosine kinase / FGFR2

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