Title : Can the local enzyme scaffold act as an H-donor for a Co(I)H bond formation? The curious case of methionine synthase-bound cob(I)alamin.

Pub. Date : 2013 Sep

PMID : 23764826






2 Functional Relationships(s)
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1 The analysis of existing crystallographic data for the reactivation conformation of MetH enzyme (1K7Y (@3.0 A); 1K98 (@3.8 A) and 3IVA (@2.7 A)) indicates that the Y1139 residue and the beta-axial H2O ligand in the MetH-bound Co(II)Cbx complex are equidistant from the Co(II) ion (Y1139Co(II)=3.97 A; H2OCo(II)=3.96 A). Carboxin 5-methyltetrahydrofolate-homocysteine methyltransferase Homo sapiens
2 The analysis of existing crystallographic data for the reactivation conformation of MetH enzyme (1K7Y (@3.0 A); 1K98 (@3.8 A) and 3IVA (@2.7 A)) indicates that the Y1139 residue and the beta-axial H2O ligand in the MetH-bound Co(II)Cbx complex are equidistant from the Co(II) ion (Y1139Co(II)=3.97 A; H2OCo(II)=3.96 A). Carboxin 5-methyltetrahydrofolate-homocysteine methyltransferase Homo sapiens