Pub. Date : 2013 Sep
PMID : 23764826
2 Functional Relationships(s)Download |
Sentence | Compound Name | Protein Name | Organism |
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 |