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TitleCrystal complexes of a predicted S-adenosylmethionine-dependent methyltransferase reveal a typical AdoMet binding domain and a substrate recognition domain
Journal, issue, pagesProtein Sci., Vol. 12, Page 1432-1442, Year 2003
Publish dateJul 17, 2002 (structure data deposition date)
AuthorsMiller, D.J. / Ouellette, N. / Evdokimova, E. / Savchenko, A. / Edwards, A. / Anderson, W.F.
External linksProtein Sci. / PubMed:12824489
MethodsX-ray diffraction
Resolution1.9 Å
Structure data

PDB-1m6y:
Crystal Structure Analysis of TM0872, a Putative SAM-dependent Methyltransferase, Complexed with SAH
Method: X-RAY DIFFRACTION / Resolution: 1.9 Å

PDB-1n2x:
Crystal Structure Analysis of TM0872, a Putative SAM-dependent Methyltransferase, Complexed with SAM
Method: X-RAY DIFFRACTION / Resolution: 1.9 Å

Chemicals

ChemComp-SO4:
SULFATE ION

ChemComp-SAH:
S-ADENOSYL-L-HOMOCYSTEINE

ChemComp-HOH:
WATER

ChemComp-SAM:
S-ADENOSYLMETHIONINE

Source
  • thermotoga maritima (bacteria)
KeywordsTRANSFERASE / SAM-dependent Methyltransferase Fold / Protein-Cofactor Product Complex / Structural Genomics / PSI / Protein Structure Initiative / Midwest Center for Structural Genomics / MCSG / Protein-SAM Methyl Donor Complex

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