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Structure paper

TitleStructure and Biocatalytic Scope of Coclaurine N-Methyltransferase.
Journal, issue, pagesAngew. Chem. Int. Ed. Engl., Vol. 57, Page 10600-10604, Year 2018
Publish dateMay 22, 2018 (structure data deposition date)
AuthorsBennett, M.R. / Thompson, M.L. / Shepherd, S.A. / Dunstan, M.S. / Herbert, A.J. / Smith, D.R.M. / Cronin, V.A. / Menon, B.R.K. / Levy, C. / Micklefield, J.
External linksAngew. Chem. Int. Ed. Engl. / PubMed:29791083
MethodsX-ray diffraction
Resolution2.35 - 2.847 Å
Structure data

PDB-6gkv:
Crystal structure of Coclaurine N-Methyltransferase (CNMT) bound to N-methylheliamine and SAH
Method: X-RAY DIFFRACTION / Resolution: 2.35 Å

PDB-6gky:
Crystal structure of Coclaurine N-Methyltransferase (CNMT) bound to N-methylheliamine and SAH
Method: X-RAY DIFFRACTION / Resolution: 2.847 Å

PDB-6gkz:
Crystal structure of Coclaurine N-Methyltransferase (CNMT) bound to N-methylheliamine and SAH
Method: X-RAY DIFFRACTION / Resolution: 2.43 Å

Chemicals

ChemComp-SAH:
S-ADENOSYL-L-HOMOCYSTEINE

ChemComp-F2W:
6,7-dimethoxy-2-methyl-1,2,3,4-tetrahydroisoquinolin-2-ium

ChemComp-HOH:
WATER

ChemComp-F2Z:
6,7-dimethoxy-2,4-dihydro-1~{H}-isoquinolin-3-one

Source
  • coptis japonica (Japanese goldthread)
KeywordsTRANSFERASE / N-methylheliamine / Coclaurine N-Methyltransferase

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