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Structure paper

TitleGlycine N-methyltransferases: a comparison of the crystal structures and kinetic properties of recombinant human, mouse and rat enzymes.
Journal, issue, pagesProteins, Vol. 57, Page 331-337, Year 2004
Publish dateOct 17, 2003 (structure data deposition date)
AuthorsPakhomova, S. / Luka, Z. / Grohmann, S. / Wagner, C. / Newcomer, M.E.
External linksProteins / PubMed:15340920
MethodsX-ray diffraction
Resolution2.55 - 3 Å
Structure data

PDB-1r74:
Crystal Structure of Human Glycine N-Methyltransferase
Method: X-RAY DIFFRACTION / Resolution: 2.55 Å

PDB-1r8x:
Crystal Structure of Mouse Glycine N-Methyltransferase (Tetragonal Form)
Method: X-RAY DIFFRACTION / Resolution: 2.95 Å

PDB-1r8y:
Crystal Structure of Mouse Glycine N-Methyltransferase (Monoclinic Form)
Method: X-RAY DIFFRACTION / Resolution: 3 Å

Chemicals

ChemComp-BME:
BETA-MERCAPTOETHANOL

ChemComp-CIT:
CITRIC ACID

ChemComp-HOH:
WATER

ChemComp-TRS:
2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL / pH buffer*YM

Source
  • homo sapiens (human)
  • mus musculus (house mouse)
KeywordsTRANSFERASE / Glycine N-Methyltransferase / human

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