Copper in PDB 2xmu: Copper Chaperone ATX1 From Synechocystis PCC6803 (CU2 Form)

The structure of Copper Chaperone ATX1 From Synechocystis PCC6803 (CU2 Form), PDB code: 2xmu was solved by A.Badarau, S.J.Firbank, A.A.Mccarthy, M.J.Banfield, C.Dennison, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	37.58 / 1.75
Space group	P 1
Cell size a, b, c (Å), α, β, γ (°)	29.243, 29.388, 38.702, 91.69, 101.26, 118.62
R / Rfree (%)	26.707 / 31.157

The binding sites of Copper atom in the Copper Chaperone ATX1 From Synechocystis PCC6803 (CU2 Form) (pdb code 2xmu). This binding sites where shown within 5.0 Angstroms radius around Copper atom.
In total 4 binding sites of Copper where determined in the Copper Chaperone ATX1 From Synechocystis PCC6803 (CU2 Form), PDB code: 2xmu:
Jump to Copper binding site number: 1; 2; 3; 4;

Copper binding site 1 out of 4 in the Copper Chaperone ATX1 From Synechocystis PCC6803 (CU2 Form)


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 1 of Copper Chaperone ATX1 From Synechocystis PCC6803 (CU2 Form) within 5.0Å range: probe atom residue distance (Å) B Occ A:Cu101 b:26.0 occ:1.00 SG A:CYS12 2.1 17.5 1.0 SG A:CYS15 2.1 16.5 1.0 CU B:CU1102 2.5 9.3 0.5 SG B:CYS15 3.0 15.6 1.0 CU B:CU1101 3.1 25.0 1.0 N A:CYS15 3.2 16.1 1.0 N A:CYS12 3.2 18.6 1.0 CB A:CYS12 3.2 19.0 1.0 CB A:CYS15 3.2 16.9 1.0 CA A:CYS12 3.5 18.9 1.0 O A:CYS12 3.6 17.5 1.0 CA A:CYS15 3.7 16.7 1.0 C A:CYS12 3.8 18.9 1.0 CU A:CU1102 3.9 10.7 0.5 C A:ALA11 4.0 19.1 1.0 N A:ALA11 4.1 17.2 1.0 C A:ALA14 4.1 16.9 1.0 CB A:ALA14 4.2 17.6 1.0 NE2 B:HIS61 4.2 18.9 1.0 CA A:ALA11 4.3 18.4 1.0 CB B:CYS15 4.4 17.9 1.0 CB A:ALA11 4.4 19.2 1.0 N A:ALA14 4.4 18.4 1.0 CA A:ALA14 4.5 18.6 1.0 CA B:CYS15 4.7 17.0 1.0 CE1 B:HIS61 4.7 19.3 1.0 N A:GLU13 4.7 18.4 1.0 N B:CYS15 4.8 17.3 1.0 O A:ALA11 4.9 21.1 1.0 SG B:CYS12 4.9 18.7 1.0

Copper binding site 2 out of 4 in the Copper Chaperone ATX1 From Synechocystis PCC6803 (CU2 Form)


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 2 of Copper Chaperone ATX1 From Synechocystis PCC6803 (CU2 Form) within 5.0Å range: probe atom residue distance (Å) B Occ A:Cu102 b:10.7 occ:0.50 NE2 A:HIS61 1.9 22.7 1.0 SG A:CYS15 2.1 16.5 1.0 SG B:CYS12 2.4 18.7 1.0 CU B:CU1101 2.5 25.0 1.0 CE1 A:HIS61 2.6 22.8 1.0 CB A:CYS15 2.9 16.9 1.0 CD2 A:HIS61 3.1 24.3 1.0 CB B:CYS12 3.3 20.1 1.0 CA A:CYS15 3.5 16.7 1.0 ND1 A:HIS61 3.8 24.9 1.0 CU A:CU1101 3.9 26.0 1.0 CG A:HIS61 4.1 25.7 1.0 N B:CYS12 4.3 20.4 1.0 CB B:ALA11 4.3 21.1 1.0 SG B:CYS15 4.4 15.6 1.0 CA B:CYS12 4.4 20.5 1.0 N A:CYS15 4.4 16.1 1.0 O A:ALA59 4.6 24.5 1.0 C A:CYS15 4.6 17.2 1.0 C B:ALA11 4.7 21.6 1.0 CD1 A:ILE10 4.8 22.9 1.0 O A:CYS15 4.9 16.1 1.0 CA A:ILE10 5.0 18.4 1.0

Copper binding site 3 out of 4 in the Copper Chaperone ATX1 From Synechocystis PCC6803 (CU2 Form)


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 3 of Copper Chaperone ATX1 From Synechocystis PCC6803 (CU2 Form) within 5.0Å range: probe atom residue distance (Å) B Occ B:Cu101 b:25.0 occ:1.00 SG B:CYS15 2.1 15.6 1.0 SG B:CYS12 2.2 18.7 1.0 CU A:CU1102 2.5 10.7 0.5 SG A:CYS15 2.8 16.5 1.0 CU A:CU1101 3.1 26.0 1.0 N B:CYS12 3.2 20.4 1.0 CB B:CYS15 3.2 17.9 1.0 N B:CYS15 3.2 17.3 1.0 CB B:CYS12 3.3 20.1 1.0 CA B:CYS12 3.6 20.5 1.0 O B:CYS12 3.7 17.7 1.0 CA B:CYS15 3.7 17.0 1.0 C B:CYS12 3.8 19.5 1.0 CU B:CU1102 3.8 9.3 0.5 C B:ALA11 4.0 21.6 1.0 N B:ALA11 4.0 19.4 1.0 CB B:ALA11 4.1 21.1 1.0 C B:ALA14 4.2 17.6 1.0 NE2 A:HIS61 4.2 22.7 1.0 CA B:ALA11 4.3 21.0 1.0 CB B:ALA14 4.3 17.4 1.0 CB A:CYS15 4.3 16.9 1.0 CA B:ALA14 4.6 18.4 1.0 CE1 A:HIS61 4.6 22.8 1.0 N B:ALA14 4.6 18.2 1.0 CA A:CYS15 4.6 16.7 1.0 N A:CYS15 4.8 16.1 1.0 N B:GLU13 4.8 19.7 1.0 SG A:CYS12 4.8 17.5 1.0 O B:ALA11 4.9 23.8 1.0

Copper binding site 4 out of 4 in the Copper Chaperone ATX1 From Synechocystis PCC6803 (CU2 Form)


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 4 of Copper Chaperone ATX1 From Synechocystis PCC6803 (CU2 Form) within 5.0Å range: probe atom residue distance (Å) B Occ B:Cu102 b:9.3 occ:0.50 NE2 B:HIS61 1.9 18.9 1.0 SG B:CYS15 2.1 15.6 1.0 SG A:CYS12 2.4 17.5 1.0 CU A:CU1101 2.5 26.0 1.0 CE1 B:HIS61 2.7 19.3 1.0 CB B:CYS15 2.9 17.9 1.0 CD2 B:HIS61 3.1 20.4 1.0 CB A:CYS12 3.4 19.0 1.0 CA B:CYS15 3.5 17.0 1.0 CU B:CU1101 3.8 25.0 1.0 ND1 B:HIS61 3.9 20.6 1.0 CG B:HIS61 4.1 21.7 1.0 N B:CYS15 4.3 17.3 1.0 SG A:CYS15 4.4 16.5 1.0 N A:CYS12 4.5 18.6 1.0 O B:ALA59 4.5 22.0 1.0 CA A:CYS12 4.5 18.9 1.0 C B:CYS15 4.6 18.1 1.0 CB A:ALA11 4.7 19.2 1.0 C A:ALA11 4.7 19.1 1.0 CA B:ILE10 4.8 20.0 1.0 O B:CYS15 4.9 17.8 1.0 CB A:ALA14 4.9 17.6 1.0

A.Badarau, S.J.Firbank, A.A.Mccarthy, M.J.Banfield, C.Dennison. Visualizing the Metal-Binding Versatility of Copper Trafficking Sites . Biochemistry V. 49 7798 2010.
ISSN: ISSN 0006-2960
PubMed: 20726513
DOI: 10.1021/BI101064W