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TitleHigh-resolution crystal structure of human asparagine synthetase enables analysis of inhibitor binding and selectivity.
Journal, issue, pagesCommun Biol, Vol. 2, Page 345-345, Year 2019
Publish dateJun 7, 2018 (structure data deposition date)
AuthorsZhu, W. / Radadiya, A. / Bisson, C. / Wenzel, S. / Nordin, B.E. / Martinez-Marquez, F. / Imasaki, T. / Sedelnikova, S.E. / Coricello, A. / Baumann, P. ...Zhu, W. / Radadiya, A. / Bisson, C. / Wenzel, S. / Nordin, B.E. / Martinez-Marquez, F. / Imasaki, T. / Sedelnikova, S.E. / Coricello, A. / Baumann, P. / Berry, A.H. / Nomanbhoy, T.K. / Kozarich, J.W. / Jin, Y. / Rice, D.W. / Takagi, Y. / Richards, N.G.J.
External linksCommun Biol / PubMed:31552298
MethodsX-ray diffraction
Resolution1.85 Å
Structure data

PDB-6gq3:
Human asparagine synthetase (ASNS) in complex with 6-diazo-5-oxo-L-norleucine (DON) at 1.85 A resolution
Method: X-RAY DIFFRACTION / Resolution: 1.85 Å

Chemicals

ChemComp-ONL:
5-OXO-L-NORLEUCINE

ChemComp-EDO:
1,2-ETHANEDIOL

ChemComp-EPE:
4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID / pH buffer*YM

ChemComp-CL:
Unknown entry

ChemComp-HOH:
WATER

Source
  • homo sapiens (human)
KeywordsBIOSYNTHETIC PROTEIN / L-asparagine biosynthesis / breast cancer / inhibitor development

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