+Search query
-Structure paper
Title | A disulfide-stabilized conformer of methionine synthase reveals an unexpected role for the histidine ligand of the cobalamin cofactor. |
---|---|
Journal, issue, pages | Proc. Natl. Acad. Sci. Usa, Vol. 105, Page 4115-4120, Year 2008 |
Publish date | Jan 3, 2008 (structure data deposition date) |
![]() | Datta, S. / Koutmos, M. / Pattridge, K.A. / Ludwig, M.L. / Matthews, R.G. |
![]() | ![]() ![]() |
Methods | X-ray diffraction |
Resolution | 2.3 Å |
Structure data | ![]() PDB-3bul: |
Chemicals | ![]() ChemComp-B12: ![]() ChemComp-HOH: |
Source |
|
![]() | TRANSFERASE / MetH / REACTIVATION CONFORMATION / H759 / COBALAMIN / INTERMODULAR INTERACTIONS / Amino-acid biosynthesis / Cobalt / Metal-binding / Methionine biosynthesis / Methyltransferase / S-adenosyl-L-methionine |