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. 

Original Settings

Zoom In

Zoom Out

Spin Off

Spin On

Ligand spacefill

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

Original Settings

Active site Spacefill

Active site Cartoon

Zoom to Active Site

Spin Off

Zoom Out

Cartoon Secondary Structure

The pink represents α-helices and the goldenrod represents the β-sheets

Detailed Active Site

Click the button twice to see the detailed active site in a thicker wireframe display.

Metal in Active Site

Of the amino acids in the active site, only the cysteine residues come in contact with the Cu(I) ligand.

Detailed Active Site Electrostatic Potential

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).

Detailed Active Site Electric Charge

Regions

Original Settings

Click twice to see wireframe.

Heteroatom Regions

Consisting of the copper and water molecules.

Copper Ligands

Bacbone A with ligand

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