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Results 1 - 6 of 6
EC Number
Metals/Ions
Commentary
Reference
Fe3+
required, the peptA (eptA promoter) is induced sevenfold in the presence of Fe3+
Mg2+
metal ions present in the active site are coordinated to Thr280 and to residues conserved among the family of transferases; required, two Mg2+ ions per enzyme molecule, binding structure model
more
three bound metal ions (two Zn2+ and a Mg2+) are implicated in catalysis
Zn2+
extracellular zinc induces phosphoethanolamine addition to Pseudomonas aeruginosa lipid A via the ColRS two-component system
Zn2+
metal ions present in the active site are coordinated to Thr280 and to residues conserved among the family of transferases, interaction of the Zn2+ with the active site, binding site structure, overview. The second Zn2+ ion is coordinated by the side chains of His383, His465, and one of the oxygen atoms of the phosphate group attached to Thr280. In LptA, two types of coordination around the Zn1 are observed depending on the state of Thr280. In the case of non-phosphorylated Thr280, the coordination about Zn1 is tetrahedral with the fourth ligand being the free phosphate group. In contrast, when Thr280 is phosphorylated, a penta-coordinated metal is observed with the hydroxyl oxygen atom of Thr280 and one of the phosphate oxygen atoms each interacting weakly with the metal; required, one Zn2+ ion per enzyme molecule coordinated tetrahedrally by the side chains of Glu240, Asp452, and His453 and the hydroxyl oxygen atom of Thr280, very strong binding to the enzyme, binding structure model
Zn2+
zinc-binding residues of the phosphoenzyme intermediate, overview. The cEptC active site contains a tetrahedrally coordinated zinc ion and a putative nucleophilic threonine, Thr266, covalently bound to a phosphoryl group to form phosphothreonine
Results 1 - 6 of 6