This short presumed domain is about 50 amino acid residues long. It often contains two cysteines that may be functionally important. This domain is found in copper transporting ATPases, some phenol hydroxylases and in a set of uncharacterised membrane proteins including Q9CNI0. This domain is named after three of the most conserved amino acids it contains. The domain may be metal binding, possibly copper ions. This domain is duplicated in some copper transporting ATPases.
Sazinsky MH, Bard J, Di Donato A, Lippard SJ.
Crystal structure of the toluene/o-xylene monooxygenase hydroxylase from Pseudomonas stutzeri OX1. Insight into the substrate specificity, substrate channeling, and active site tuning of multicomponent monooxygenases.
J. Biol. Chem. 279 2004 30600-10
[PubMed: 15096510] http://dx.doi.org/10.1074/jbc.M400710200
McCormick MS, Sazinsky MH, Condon KL, Lippard SJ.
X-ray crystal structures of manganese(II)-reconstituted and native toluene/o-xylene monooxygenase hydroxylase reveal rotamer shifts in conserved residues and an enhanced view of the protein interior.
J. Am. Chem. Soc. 128 2006 15108-10
[PubMed: 17117860] http://dx.doi.org/10.1021/ja064837r
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