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Copper in PDB 2xmv: Copper Chaperone ATX1 From Synechocystis PCC6803 (CU1, Trimeric Form, HIS61TYR Mutant)

Protein crystallography data

The structure of Copper Chaperone ATX1 From Synechocystis PCC6803 (CU1, Trimeric Form, HIS61TYR Mutant), PDB code: 2xmv 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) 29.97 / 1.80
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 47.690, 77.100, 90.500, 90.00, 90.00, 90.00
R / Rfree (%) 19.063 / 25.315

Copper Binding Sites:

The binding sites of Copper atom in the Copper Chaperone ATX1 From Synechocystis PCC6803 (CU1, Trimeric Form, HIS61TYR Mutant) (pdb code 2xmv). This binding sites where shown within 5.0 Angstroms radius around Copper atom.
In total 8 binding sites of Copper where determined in the Copper Chaperone ATX1 From Synechocystis PCC6803 (CU1, Trimeric Form, HIS61TYR Mutant), PDB code: 2xmv:
Jump to Copper binding site number: 1; 2; 3; 4; 5; 6; 7; 8;

Copper binding site 1 out of 8 in 2xmv

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Copper binding site 1 out of 8 in the Copper Chaperone ATX1 From Synechocystis PCC6803 (CU1, Trimeric Form, HIS61TYR Mutant)


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 (CU1, Trimeric Form, HIS61TYR Mutant) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu1065

b:13.8
occ:1.00
 SG A:CYS15 2.2 10.7 1.0
SG A:CYS12 2.2 10.7 1.0
SG C:CYS12 2.4 11.2 1.0
CU A:CU11066 2.6 19.7 1.0
CB C:CYS12 3.2 8.2 1.0
CB A:CYS15 3.4 11.0 1.0
N A:CYS15 3.5 10.2 1.0
CB A:CYS12 3.5 8.4 1.0
N A:CYS12 3.5 10.7 1.0
CA A:CYS15 3.9 10.7 1.0
CA A:CYS12 4.0 9.8 1.0
CB C:ALA14 4.0 8.1 1.0
CB A:ALA11 4.0 12.8 1.0
O A:HOH2011 4.1 9.1 1.0
CU C:CU11065 4.1 13.4 1.0
N A:ALA11 4.2 11.7 1.0
CU B:CU11065 4.2 12.6 1.0
C A:ALA11 4.2 12.8 1.0
O A:CYS12 4.2 9.8 1.0
C A:CYS12 4.3 8.6 1.0
CA A:ALA11 4.4 12.9 1.0
C A:ALA14 4.4 9.6 1.0
CB A:ALA14 4.4 9.7 1.0
N C:ALA14 4.4 8.1 1.0
CA C:CYS12 4.6 10.0 1.0
N A:ALA14 4.7 9.2 1.0
SG B:CYS12 4.7 10.3 1.0
CA A:ALA14 4.7 9.8 1.0
CA C:ALA14 4.9 8.6 1.0
N C:GLU13 4.9 10.6 1.0
C C:CYS12 5.0 10.0 1.0

Copper binding site 2 out of 8 in 2xmv

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Copper binding site 2 out of 8 in the Copper Chaperone ATX1 From Synechocystis PCC6803 (CU1, Trimeric Form, HIS61TYR Mutant)


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 (CU1, Trimeric Form, HIS61TYR Mutant) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu1066

b:19.7
occ:1.00
 O A:HOH2011 2.2 9.1 1.0
SG C:CYS12 2.4 11.2 1.0
SG B:CYS12 2.4 10.3 1.0
SG A:CYS12 2.4 10.7 1.0
CU C:CU11065 2.5 13.4 1.0
CU B:CU11065 2.6 12.6 1.0
CU A:CU11065 2.6 13.8 1.0
CB C:CYS12 3.3 8.2 1.0
CB B:CYS12 3.4 10.6 1.0
CB A:CYS12 3.4 8.4 1.0
N C:CYS12 4.6 10.2 1.0
CA C:CYS12 4.6 10.0 1.0
CB B:ALA11 4.6 11.7 1.0
SG C:CYS15 4.6 11.7 1.0
CB C:ALA11 4.7 11.8 1.0
SG B:CYS15 4.7 10.2 1.0
CA B:CYS12 4.7 10.6 1.0
CA A:CYS12 4.7 9.8 1.0
N B:CYS12 4.7 10.6 1.0
N A:CYS12 4.7 10.7 1.0
SG A:CYS15 4.8 10.7 1.0
CB A:ALA11 4.8 12.8 1.0

Copper binding site 3 out of 8 in 2xmv

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Copper binding site 3 out of 8 in the Copper Chaperone ATX1 From Synechocystis PCC6803 (CU1, Trimeric Form, HIS61TYR Mutant)


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 (CU1, Trimeric Form, HIS61TYR Mutant) within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cu1065

b:12.6
occ:1.00
 SG B:CYS15 2.2 10.2 1.0
SG B:CYS12 2.2 10.3 1.0
SG A:CYS12 2.5 10.7 1.0
CU A:CU11066 2.6 19.7 1.0
CB B:CYS15 3.3 8.6 1.0
CB A:CYS12 3.4 8.4 1.0
N B:CYS15 3.4 7.5 1.0
CB B:CYS12 3.4 10.6 1.0
N B:CYS12 3.5 10.6 1.0
CB B:ALA11 3.8 11.7 1.0
CA B:CYS15 3.8 9.2 1.0
CA B:CYS12 3.9 10.6 1.0
O A:HOH2011 4.0 9.1 1.0
CB A:ALA14 4.0 9.7 1.0
CU C:CU11065 4.0 13.4 1.0
O B:CYS12 4.1 8.9 1.0
N B:ALA11 4.2 11.2 1.0
C B:ALA11 4.2 12.4 1.0
CU A:CU11065 4.2 13.8 1.0
C B:CYS12 4.2 9.7 1.0
CA B:ALA11 4.3 12.5 1.0
C B:ALA14 4.3 9.0 1.0
N A:ALA14 4.5 9.2 1.0
CB B:ALA14 4.5 8.5 1.0
SG C:CYS12 4.6 11.2 1.0
N B:ALA14 4.7 9.2 1.0
CA B:ALA14 4.7 8.6 1.0
CA A:CYS12 4.8 9.8 1.0
CA A:ALA14 4.9 9.8 1.0

Copper binding site 4 out of 8 in 2xmv

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Copper binding site 4 out of 8 in the Copper Chaperone ATX1 From Synechocystis PCC6803 (CU1, Trimeric Form, HIS61TYR Mutant)


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 (CU1, Trimeric Form, HIS61TYR Mutant) within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Cu1065

b:13.4
occ:1.00
 SG C:CYS12 2.2 11.2 1.0
SG C:CYS15 2.2 11.7 1.0
SG B:CYS12 2.4 10.3 1.0
CU A:CU11066 2.5 19.7 1.0
CB B:CYS12 3.3 10.6 1.0
CB C:CYS15 3.4 9.0 1.0
CB C:CYS12 3.5 8.2 1.0
N C:CYS15 3.5 9.3 1.0
N C:CYS12 3.5 10.2 1.0
CB B:ALA14 3.9 8.5 1.0
O A:HOH2011 3.9 9.1 1.0
CA C:CYS15 4.0 9.4 1.0
CA C:CYS12 4.0 10.0 1.0
CB C:ALA11 4.0 11.8 1.0
CU B:CU11065 4.0 12.6 1.0
CU A:CU11065 4.1 13.8 1.0
O C:CYS12 4.3 9.7 1.0
C C:ALA11 4.3 10.4 1.0
C C:CYS12 4.3 10.0 1.0
N C:ALA11 4.3 11.4 1.0
N B:ALA14 4.4 9.2 1.0
CA C:ALA11 4.4 11.1 1.0
CB C:ALA14 4.5 8.1 1.0
C C:ALA14 4.5 8.7 1.0
SG A:CYS12 4.6 10.7 1.0
N C:ALA14 4.7 8.1 1.0
CA B:CYS12 4.7 10.6 1.0
CA C:ALA14 4.8 8.6 1.0
CA B:ALA14 4.8 8.6 1.0
N B:GLU13 4.9 9.4 1.0

Copper binding site 5 out of 8 in 2xmv

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Copper binding site 5 out of 8 in the Copper Chaperone ATX1 From Synechocystis PCC6803 (CU1, Trimeric Form, HIS61TYR Mutant)


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 5 of Copper Chaperone ATX1 From Synechocystis PCC6803 (CU1, Trimeric Form, HIS61TYR Mutant) within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Cu1065

b:15.8
occ:1.00
 SG D:CYS15 2.2 12.9 1.0
SG D:CYS12 2.2 12.1 1.0
SG F:CYS12 2.3 12.7 1.0
CU D:CU11066 2.6 18.7 1.0
CB F:CYS12 3.3 13.1 1.0
CB D:CYS15 3.3 10.3 1.0
N D:CYS15 3.4 10.7 1.0
CB D:CYS12 3.5 11.7 1.0
N D:CYS12 3.6 12.7 1.0
CB D:ALA11 3.9 13.4 1.0
CA D:CYS15 3.9 10.3 1.0
CB F:ALA14 4.0 9.1 1.0
CA D:CYS12 4.0 11.6 1.0
O D:HOH2008 4.1 13.7 1.0
CU F:CU11065 4.1 14.4 1.0
CU E:CU11065 4.1 15.5 1.0
C D:ALA11 4.1 13.6 1.0
N D:ALA11 4.2 11.9 1.0
O D:CYS12 4.2 11.1 1.0
CA D:ALA11 4.3 13.5 1.0
C D:CYS12 4.3 11.6 1.0
N F:ALA14 4.4 10.5 1.0
C D:ALA14 4.4 10.3 1.0
CB D:ALA14 4.6 9.3 1.0
SG E:CYS12 4.7 11.8 1.0
CA F:CYS12 4.7 12.1 1.0
CA F:ALA14 4.8 9.9 1.0
N D:ALA14 4.8 9.5 1.0
CA D:ALA14 4.8 10.3 1.0
N F:GLU13 4.9 11.4 1.0
C F:CYS12 5.0 11.9 1.0

Copper binding site 6 out of 8 in 2xmv

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Copper binding site 6 out of 8 in the Copper Chaperone ATX1 From Synechocystis PCC6803 (CU1, Trimeric Form, HIS61TYR Mutant)


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 6 of Copper Chaperone ATX1 From Synechocystis PCC6803 (CU1, Trimeric Form, HIS61TYR Mutant) within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Cu1066

b:18.7
occ:1.00
 O D:HOH2008 2.2 13.7 1.0
SG F:CYS12 2.4 12.7 1.0
SG D:CYS12 2.4 12.1 1.0
SG E:CYS12 2.4 11.8 1.0
CU E:CU11065 2.5 15.5 1.0
CU D:CU11065 2.6 15.8 1.0
CU F:CU11065 2.6 14.4 1.0
CB F:CYS12 3.3 13.1 1.0
CB D:CYS12 3.4 11.7 1.0
CB E:CYS12 3.5 12.2 1.0
CB D:ALA11 4.6 13.4 1.0
CA F:CYS12 4.6 12.1 1.0
CA D:CYS12 4.7 11.6 1.0
SG D:CYS15 4.7 12.9 1.0
SG F:CYS15 4.7 12.4 1.0
SG E:CYS15 4.7 12.4 1.0
N E:CYS12 4.7 11.6 1.0
N D:CYS12 4.7 12.7 1.0
N F:CYS12 4.7 13.4 1.0
CA E:CYS12 4.7 12.0 1.0
CB F:ALA11 4.7 13.7 1.0
CB E:ALA11 4.8 14.1 1.0
C D:ALA11 5.0 13.6 1.0

Copper binding site 7 out of 8 in 2xmv

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Copper binding site 7 out of 8 in the Copper Chaperone ATX1 From Synechocystis PCC6803 (CU1, Trimeric Form, HIS61TYR Mutant)


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 7 of Copper Chaperone ATX1 From Synechocystis PCC6803 (CU1, Trimeric Form, HIS61TYR Mutant) within 5.0Å range:
probe atom residue distance (Å) B Occ
E:Cu1065

b:15.5
occ:1.00
 SG E:CYS12 2.2 11.8 1.0
SG E:CYS15 2.3 12.4 1.0
SG D:CYS12 2.4 12.1 1.0
CU D:CU11066 2.5 18.7 1.0
CB D:CYS12 3.3 11.7 1.0
CB E:CYS15 3.3 10.1 1.0
N E:CYS15 3.5 9.7 1.0
CB E:CYS12 3.5 12.2 1.0
N E:CYS12 3.6 11.6 1.0
CA E:CYS15 3.9 10.4 1.0
O D:HOH2008 4.0 13.7 1.0
CA E:CYS12 4.0 12.0 1.0
CB D:ALA14 4.0 9.3 1.0
CU F:CU11065 4.0 14.4 1.0
CB E:ALA11 4.1 14.1 1.0
CU D:CU11065 4.1 15.8 1.0
O E:CYS12 4.2 11.0 1.0
C E:ALA11 4.2 13.9 1.0
C E:CYS12 4.3 10.9 1.0
N E:ALA11 4.3 14.1 1.0
C E:ALA14 4.4 9.9 1.0
CA E:ALA11 4.4 14.1 1.0
CB E:ALA14 4.5 10.0 1.0
N D:ALA14 4.5 9.5 1.0
SG F:CYS12 4.6 12.7 1.0
N E:ALA14 4.7 10.3 1.0
CA E:ALA14 4.7 10.0 1.0
CA D:CYS12 4.8 11.6 1.0
CA D:ALA14 4.9 10.3 1.0
N D:GLU13 5.0 10.2 1.0

Copper binding site 8 out of 8 in 2xmv

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Copper binding site 8 out of 8 in the Copper Chaperone ATX1 From Synechocystis PCC6803 (CU1, Trimeric Form, HIS61TYR Mutant)


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 8 of Copper Chaperone ATX1 From Synechocystis PCC6803 (CU1, Trimeric Form, HIS61TYR Mutant) within 5.0Å range:
probe atom residue distance (Å) B Occ
F:Cu1065

b:14.4
occ:1.00
 SG F:CYS15 2.2 12.4 1.0
SG F:CYS12 2.3 12.7 1.0
SG E:CYS12 2.4 11.8 1.0
CU D:CU11066 2.6 18.7 1.0
CB F:CYS15 3.3 10.4 1.0
CB E:CYS12 3.4 12.2 1.0
N F:CYS15 3.4 8.7 1.0
CB F:CYS12 3.4 13.1 1.0
N F:CYS12 3.6 13.4 1.0
CA F:CYS15 3.9 9.8 1.0
CA F:CYS12 3.9 12.1 1.0
CB E:ALA14 4.0 10.0 1.0
CB F:ALA11 4.0 13.7 1.0
CU E:CU11065 4.0 15.5 1.0
O D:HOH2008 4.1 13.7 1.0
CU D:CU11065 4.1 15.8 1.0
O F:CYS12 4.2 10.1 1.0
C F:ALA11 4.2 13.1 1.0
N F:ALA11 4.3 13.2 1.0
C F:CYS12 4.3 11.9 1.0
CA F:ALA11 4.4 13.9 1.0
C F:ALA14 4.4 9.3 1.0
N E:ALA14 4.5 10.3 1.0
CB F:ALA14 4.5 9.1 1.0
SG D:CYS12 4.6 12.1 1.0
N F:ALA14 4.7 10.5 1.0
CA F:ALA14 4.8 9.9 1.0
CA E:CYS12 4.8 12.0 1.0
CA E:ALA14 4.9 10.0 1.0

Reference:

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
Page generated: Wed Jul 31 00:12:37 2024

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