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Structure paper

TitleThe reactivity-driven biochemical mechanism of covalent KRASG12Cinhibitors.
Journal, issue, pagesNat. Struct. Mol. Biol., Vol. 25, Page 454-462, Year 2018
Publish dateSep 15, 2017 (structure data deposition date)
AuthorsHansen, R. / Peters, U. / Babbar, A. / Chen, Y. / Feng, J. / Janes, M.R. / Li, L.S. / Ren, P. / Liu, Y. / Zarrinkar, P.P.
External linksNat. Struct. Mol. Biol. / PubMed:29760531
MethodsX-ray diffraction
Resolution1.29 - 1.43 Å
Structure data

PDB-6b0v:
Crystal Structure of small molecule ARS-107 covalently bound to K-Ras G12C
Method: X-RAY DIFFRACTION / Resolution: 1.29 Å

PDB-6b0y:
Crystal Structure of small molecule ARS-917 covalently bound to K-Ras G12C
Method: X-RAY DIFFRACTION / Resolution: 1.43 Å

Chemicals

ChemComp-CA:
Unknown entry

ChemComp-C8G:
1-[3-(4-{[(4,5-dichloro-2-hydroxyphenyl)amino]acetyl}piperazin-1-yl)azetidin-1-yl]propan-1-one

ChemComp-GDP:
GUANOSINE-5'-DIPHOSPHATE / GDP, energy-carrying molecule*YM

ChemComp-HOH:
WATER

ChemComp-8ZG:
1-{4-[6-chloro-7-(2-fluorophenyl)quinazolin-4-yl]piperazin-1-yl}propan-1-one

ChemComp-GOL:
GLYCEROL

Source
  • homo sapiens (human)
KeywordsSIGNALING PROTEIN / small GTPase domain / covalent inhibitor bound / switch II pocket / GDP bound

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