1P0Y
Crystal structure of the SET domain of LSMT bound to MeLysine and AdoHcy
Summary for 1P0Y
Entry DOI | 10.2210/pdb1p0y/pdb |
Related | 1MLV 1OZV |
Descriptor | Ribulose-1,5 bisphosphate carboxylase/oxygenase large subunit N-methyltransferase, chloroplast, S-ADENOSYL-L-HOMOCYSTEINE, N-METHYL-LYSINE, ... (4 entities in total) |
Functional Keywords | set domain, lysine n-methylation, multiple methylation, photosynthesis, post-translational modification, transferase |
Biological source | Pisum sativum (pea) |
Cellular location | Plastid, chloroplast: Q43088 |
Total number of polymer chains | 3 |
Total formula weight | 153521.36 |
Authors | Trievel, R.C.,Flynn, E.M.,Houtz, R.L.,Hurley, J.H. (deposition date: 2003-04-11, release date: 2003-07-01, Last modification date: 2023-08-16) |
Primary citation | Trievel, R.C.,Flynn, E.M.,Houtz, R.L.,Hurley, J.H. Mechanism of multiple lysine methylation by the SET domain enzyme Rubisco LSMT Nat.Struct.Biol., 10:545-552, 2003 Cited by PubMed: 12819771DOI: 10.1038/nsb946 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.55 Å) |
Structure validation
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