6GQ3
Human asparagine synthetase (ASNS) in complex with 6-diazo-5-oxo-L-norleucine (DON) at 1.85 A resolution
Summary for 6GQ3
Entry DOI | 10.2210/pdb6gq3/pdb |
Descriptor | Asparagine synthetase [glutamine-hydrolyzing], 5-OXO-L-NORLEUCINE, 1,2-ETHANEDIOL, ... (6 entities in total) |
Functional Keywords | l-asparagine biosynthesis, breast cancer, inhibitor development, biosynthetic protein |
Biological source | Homo sapiens (Human) |
Total number of polymer chains | 2 |
Total formula weight | 129997.70 |
Authors | Zhu, W.,Radadiya, A.,Bisson, C.,Jin, Y.,Nordin, B.E.,Imasaki, T.,Wenzel, S.,Sedelnikova, S.E.,Berry, A.H.,Nomanbhoy, T.K.,Kozarich, J.W.,Takagi, Y.,Rice, D.W.,Richards, N.G.J. (deposition date: 2018-06-07, release date: 2019-09-18, Last modification date: 2024-01-17) |
Primary citation | 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. High-resolution crystal structure of human asparagine synthetase enables analysis of inhibitor binding and selectivity. Commun Biol, 2:345-345, 2019 Cited by PubMed: 31552298DOI: 10.1038/s42003-019-0587-z PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.85 Å) |
Structure validation
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