3LCC

Structure of a SAM-dependent halide methyltransferase from Arabidopsis thaliana

Summary for 3LCC

Entry DOI	10.2210/pdb3lcc/pdb
Descriptor	Putative methyl chloride transferase, S-ADENOSYL-L-HOMOCYSTEINE, CHLORIDE ION, ... (4 entities in total)
Functional Keywords	halide methyltransferase, transferase
Biological source	Arabidopsis thaliana (thale cress)
Total number of polymer chains	1
Total formula weight	26805.64
Authors	Schmidberger, J.W.,O'Hagan, D.,Naismith, J.H. (deposition date: 2010-01-10, release date: 2010-05-19, Last modification date: 2023-11-01)
Primary citation	Schmidberger, J.W.,James, A.B.,Edwards, R.,Naismith, J.H.,O'Hagan, D. Halomethane Biosynthesis: Structure of a SAM-Dependent Halide Methyltransferase from Arabidopsis thaliana Angew.Chem.Int.Ed.Engl., 49:3646-3648, 2010 Cited by PubMed Abstract: A product structure of the halomethane producing enzyme in plants () is reported and a model for presentation of chloride/bromide ion to the methyl group of S-adenosyl-L-methionine (SAM) is presented to rationalise nucleophilic halide attack for halomethane production, gaseous natural products that are produced globally. PubMed: 20376845 DOI: 10.1002/anie.201000119 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (1.8 Å)

Structure validation