Copper (I) Efflux Regulator Protein Expressed in E. Coli Bacteria
A copper regulating protein that consists of two identical chains that each bind one Cu(1) ion.
Each ligand binds to the terminal end of the chain.
Chain A Spacefill
Chain B Spacefill
Notice how each chain looks identical.
Surface Rendering
Electrostatic Surface Potential
The binding sites for the ligands are negative (red) it is unknown why one binding site appears more negative than the other.
Active site consisting of Cys112 and Cys120
Zoom to Active Site
Cartoon Secondary Structure
The pink represents α-helices and the goldenrod represents the β-sheets
Click the button twice to see the detailed active site in a thicker wireframe display.
Of the amino acids in the active site, only the cysteine residues come in contact with the Cu(I) ligand.
Since only the cysteine residues come in contact with the Cu(I), the other negatively charged residues (aspartic acid and serine) surrounding the ligand draw the Cu(I) into its resting place within the protein. The electropotential shows the negative areas which attract the positively charged Cu(I).
ic Charge
Regions
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Consisting of the copper and water molecules.
Bacbone B with ligand
Click back and forth between backbone buttons to see each ligand.
Created by: Mr.'s James E. Kuderer and Abraham J. Cass