Zinc in PDB 6wje: Copper Resistance Protein Copg- Form 2

The structure of Copper Resistance Protein Copg- Form 2, PDB code: 6wje was solved by A.C.Hausrath, A.T.Ly, M.M.Mcevoy, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	55.42 / 2.50
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	63.700, 87.460, 143.270, 90.00, 90.00, 90.00
R / Rfree (%)	18.8 / 24.5

The structure of Copper Resistance Protein Copg- Form 2 also contains other interesting chemical elements:

Copper

(Cu)

20 atoms

Pages:

>>> Page 1 <<< Page 2, Binding sites: 11 - 20; Page 3, Binding sites: 21 - 30; Page 4, Binding sites: 31 - 35;

Binding sites:

The binding sites of Zinc atom in the Copper Resistance Protein Copg- Form 2 (pdb code 6wje). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 35 binding sites of Zinc where determined in the Copper Resistance Protein Copg- Form 2, PDB code: 6wje:
Jump to Zinc binding site number: 1; 2; 3; 4; 5; 6; 7; 8; 9; 10;

Zinc binding site 1 out of 35 in the Copper Resistance Protein Copg- Form 2


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Copper Resistance Protein Copg- Form 2 within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn204 b:45.8 occ:1.00 OE2 A:GLU98 2.1 50.0 1.0 NE2 A:HIS22 2.1 42.1 1.0 OD2 A:ASP18 2.3 45.1 1.0 OE1 A:GLU98 2.3 42.5 1.0 OD1 A:ASP18 2.4 33.1 1.0 O A:HOH317 2.4 33.1 1.0 CD A:GLU98 2.5 49.2 1.0 CG A:ASP18 2.6 32.5 1.0 CE1 A:HIS22 3.0 45.9 1.0 CD2 A:HIS22 3.2 41.8 1.0 O A:HOH318 3.7 51.3 1.0 O A:HOH306 3.8 51.4 1.0 CG A:GLU98 4.1 47.1 1.0 CB A:ASP18 4.1 33.6 1.0 ND1 A:HIS22 4.2 45.6 1.0 CG A:HIS22 4.3 45.2 1.0 CA A:GLY96 4.3 34.5 1.0 N A:GLY96 4.4 38.7 1.0 O A:ASP18 4.8 37.4 1.0 O A:ACT209 4.8 49.0 1.0 CA B:GLY14 4.9 49.4 1.0 C A:GLY96 4.9 39.8 1.0 CA A:ASP18 5.0 36.4 1.0

Zinc binding site 2 out of 35 in the Copper Resistance Protein Copg- Form 2


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Copper Resistance Protein Copg- Form 2 within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn205 b:65.6 occ:1.00 NE2 A:HIS33 2.1 51.1 1.0 OD1 A:ASP6 2.1 62.8 1.0 OD2 A:ASP6 2.3 59.3 1.0 CG A:ASP6 2.5 48.5 1.0 O A:HOH323 2.5 58.4 1.0 CD2 A:HIS33 2.9 50.0 1.0 CE1 A:HIS33 3.2 53.1 1.0 ZN A:ZN211 3.2 74.0 1.0 O A:HOH302 3.8 54.0 1.0 CB A:ASP6 3.9 43.2 1.0 CG A:HIS33 4.1 52.7 1.0 NE2 A:HIS8 4.2 64.0 1.0 ND1 A:HIS33 4.2 53.6 1.0 OG1 A:THR31 4.3 52.4 1.0 CE1 A:HIS8 4.9 66.7 1.0 CA A:ASP6 5.0 42.9 1.0

Zinc binding site 3 out of 35 in the Copper Resistance Protein Copg- Form 2


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 3 of Copper Resistance Protein Copg- Form 2 within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn206 b:82.3 occ:1.00 OD1 A:ASP10 2.1 69.5 1.0 OD1 B:ASP101 2.1 66.0 1.0 O B:HOH322 2.2 57.4 1.0 O B:HOH304 2.6 63.1 1.0 CG B:ASP101 2.8 60.5 1.0 OD2 B:ASP101 2.9 67.4 1.0 CG A:ASP10 2.9 61.7 1.0 OD2 A:ASP10 3.1 56.6 1.0 CB B:ASP101 4.3 54.6 1.0 CB A:ASP10 4.3 50.4 1.0 CB A:ALA36 4.7 69.7 1.0 N A:ALA11 4.9 54.0 1.0 N B:ASP101 4.9 54.6 1.0 CA B:ASP101 4.9 55.9 1.0 CA A:ALA36 4.9 71.5 1.0

Zinc binding site 4 out of 35 in the Copper Resistance Protein Copg- Form 2


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 4 of Copper Resistance Protein Copg- Form 2 within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn207 b:91.9 occ:1.00 O A:HOH320 2.2 47.9 1.0 O A:HOH301 2.2 63.5 1.0 OE2 A:GLU78 2.8 80.5 1.0 O A:HOH314 2.8 49.1 1.0 CD A:GLU78 3.6 78.4 1.0 OE1 A:GLU78 3.7 76.8 1.0 CG A:GLU78 5.0 56.8 1.0

Zinc binding site 5 out of 35 in the Copper Resistance Protein Copg- Form 2


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 5 of Copper Resistance Protein Copg- Form 2 within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn208 b:80.5 occ:1.00 OD1 B:ASP10 2.1 65.0 1.0 OD2 A:ASP101 2.1 81.1 1.0 OD1 A:ASP101 2.2 63.5 1.0 O A:HOH305 2.2 53.6 1.0 CG A:ASP101 2.5 67.9 1.0 O A:HOH319 2.6 80.4 1.0 CG B:ASP10 3.0 63.8 1.0 OD2 B:ASP10 3.2 56.7 1.0 CB A:ASP101 4.1 67.1 1.0 CB B:ASP10 4.4 53.6 1.0 N A:ASP101 4.9 57.7 1.0 N B:ALA11 4.9 56.0 1.0 CA A:ASP101 4.9 65.9 1.0

Zinc binding site 6 out of 35 in the Copper Resistance Protein Copg- Form 2


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 6 of Copper Resistance Protein Copg- Form 2 within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn210 b:90.2 occ:0.81 OE1 A:GLU35 2.8 76.1 1.0 CB A:ASP37 3.0 77.2 1.0 N A:ASP37 3.4 73.1 1.0 CA A:ASP37 3.7 74.7 1.0 N A:ALA36 3.8 70.6 1.0 CB A:GLU35 3.8 68.1 1.0 CD A:GLU35 3.9 76.0 1.0 CA A:GLU35 4.2 55.4 1.0 C A:GLU35 4.2 63.4 1.0 C A:ALA36 4.3 75.5 1.0 CG A:ASP37 4.3 82.5 1.0 CG A:GLU35 4.4 72.7 1.0 O A:ASP37 4.4 78.6 1.0 C A:ASP37 4.4 72.8 1.0 CA A:ALA36 4.5 71.5 1.0 OD2 A:ASP37 4.6 80.8 1.0 O A:HOH324 4.9 65.9 1.0 CB A:ALA36 5.0 69.7 1.0

Zinc binding site 7 out of 35 in the Copper Resistance Protein Copg- Form 2


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 7 of Copper Resistance Protein Copg- Form 2 within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn211 b:74.0 occ:1.00 O A:HOH302 3.1 54.0 1.0 ZN A:ZN205 3.2 65.6 1.0 NE2 A:HIS8 3.5 64.0 1.0 CE1 A:HIS8 3.6 66.7 1.0 OD2 A:ASP6 4.0 59.3 1.0 NH2 A:ARG44 4.0 74.1 1.0 NE2 A:HIS33 4.2 51.1 1.0 CD2 A:HIS33 4.4 50.0 1.0 O A:HOH323 4.5 58.4 1.0 NH1 A:ARG44 4.7 72.0 1.0 CZ A:ARG44 4.7 76.2 1.0 CD2 A:HIS8 4.8 51.6 1.0 CE1 A:HIS33 4.9 53.1 1.0 ND1 A:HIS8 4.9 54.5 1.0

Zinc binding site 8 out of 35 in the Copper Resistance Protein Copg- Form 2


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 8 of Copper Resistance Protein Copg- Form 2 within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn204 b:46.0 occ:1.00 OE2 B:GLU98 2.1 40.4 1.0 NE2 B:HIS22 2.2 48.4 1.0 OD2 B:ASP18 2.3 48.7 1.0 OD1 B:ASP18 2.3 51.3 1.0 CG B:ASP18 2.6 43.1 1.0 O B:HOH320 2.8 42.8 1.0 CD B:GLU98 3.0 46.1 1.0 CE1 B:HIS22 3.1 46.1 1.0 OE1 B:GLU98 3.2 42.5 1.0 CD2 B:HIS22 3.2 46.9 1.0 O B:HOH315 3.5 47.4 1.0 CB B:ASP18 4.1 41.4 1.0 ND1 B:HIS22 4.3 52.1 1.0 CG B:HIS22 4.3 43.9 1.0 CG B:GLU98 4.4 39.4 1.0 CA A:GLY14 4.4 38.5 1.0 CA B:GLY96 4.5 34.1 1.0 N B:GLY96 4.5 41.4 1.0 O B:ASP18 4.8 41.0 1.0 CA B:ASP18 4.9 43.6 1.0

Zinc binding site 9 out of 35 in the Copper Resistance Protein Copg- Form 2


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 9 of Copper Resistance Protein Copg- Form 2 within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn205 b:96.6 occ:0.91 O B:HOH309 2.0 51.6 1.0 OD2 B:ASP6 2.0 72.8 1.0 NE2 B:HIS8 2.1 70.5 1.0 O B:HOH321 2.4 63.5 1.0 CE1 B:HIS8 2.5 69.4 1.0 CG B:ASP6 3.2 67.0 1.0 CD2 B:HIS33 3.3 64.8 1.0 CD2 B:HIS8 3.4 59.5 1.0 NE2 B:HIS33 3.7 66.8 1.0 OD1 B:ASP6 3.8 68.6 1.0 ND1 B:HIS8 3.8 61.5 1.0 CG B:HIS8 4.3 56.2 1.0 CG B:HIS33 4.4 67.9 1.0 CB B:ASP6 4.4 54.8 1.0 CE1 B:HIS33 4.9 67.2 1.0

Zinc binding site 10 out of 35 in the Copper Resistance Protein Copg- Form 2


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 10 of Copper Resistance Protein Copg- Form 2 within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn206 b:93.2 occ:0.65 OD2 B:ASP32 2.1 66.4 1.0 O B:HOH323 2.6 60.3 1.0 CG B:ASP32 3.0 57.8 1.0 CB B:ASP32 3.3 48.7 1.0 O B:HOH311 3.3 56.2 1.0 NH2 B:ARG9 4.2 67.3 1.0 OD1 B:ASP32 4.2 59.3 1.0 ZN B:ZN207 4.3 1.0 0.8 CA B:ASP32 4.8 54.4 1.0 CG2 B:ILE20 4.8 41.2 1.0 CD1 B:ILE20 4.8 34.2 1.0

A.C.Hausrath, N.A.Ramirez, A.T.Ly, M.M.Mcevoy. The Bacterial Copper-Resistance Protein Copg Contains A Cysteine-Bridged Tetranuclear Copper Cluster J.Biol.Chem. 2020.
ISSN: ESSN 1083-351X