Atomistry » Copper » PDB 2vr7-2xv0 » 2xmj
Atomistry »
  Copper »
    PDB 2vr7-2xv0 »
      2xmj »

Copper in PDB 2xmj: Visualising the Metal-Binding Versatility of Copper Trafficking Sites: ATX1 Side-to-Side (Aerobic)

Protein crystallography data

The structure of Visualising the Metal-Binding Versatility of Copper Trafficking Sites: ATX1 Side-to-Side (Aerobic), PDB code: 2xmj 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) 10.00 / 1.08
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 63.460, 41.654, 55.832, 90.00, 107.70, 90.00
R / Rfree (%) n/a / 14.9

Other elements in 2xmj:

The structure of Visualising the Metal-Binding Versatility of Copper Trafficking Sites: ATX1 Side-to-Side (Aerobic) also contains other interesting chemical elements:

Chlorine (Cl) 2 atoms
Sodium (Na) 1 atom

Copper Binding Sites:

The binding sites of Copper atom in the Visualising the Metal-Binding Versatility of Copper Trafficking Sites: ATX1 Side-to-Side (Aerobic) (pdb code 2xmj). This binding sites where shown within 5.0 Angstroms radius around Copper atom.
In total 4 binding sites of Copper where determined in the Visualising the Metal-Binding Versatility of Copper Trafficking Sites: ATX1 Side-to-Side (Aerobic), PDB code: 2xmj:
Jump to Copper binding site number: 1; 2; 3; 4;

Copper binding site 1 out of 4 in 2xmj

Go back to Copper Binding Sites List in 2xmj
Copper binding site 1 out of 4 in the Visualising the Metal-Binding Versatility of Copper Trafficking Sites: ATX1 Side-to-Side (Aerobic)


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 1 of Visualising the Metal-Binding Versatility of Copper Trafficking Sites: ATX1 Side-to-Side (Aerobic) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu1065

b:5.5
occ:1.00
SG B:CYS12 2.2 5.4 1.0
SG A:CYS12 2.2 5.3 1.0
CL A:CL1067 2.4 6.8 0.5
CU B:CU1065 2.6 5.5 1.0
CU A:CU1068 2.7 5.4 1.0
CB A:CYS12 3.2 4.5 1.0
CB B:CYS12 3.2 5.0 1.0
O A:HOH2016 4.0 15.4 1.0
CB A:ALA11 4.4 5.6 1.0
CA A:CYS12 4.4 4.6 1.0
CA B:CYS12 4.4 5.2 1.0
N B:CYS12 4.4 5.1 1.0
N A:CYS12 4.4 4.6 1.0
CB B:ALA11 4.4 6.2 1.0
SG B:CYS15 4.5 5.0 1.0
SG A:CYS15 4.6 4.8 1.0
C B:ALA11 4.6 5.1 1.0
C A:ALA11 4.7 4.7 1.0
CU B:CU1066 4.7 5.1 1.0
CB B:ALA14 4.9 6.0 1.0
O B:HOH2033 4.9 12.2 1.0
O B:ALA11 4.9 6.0 1.0
O A:ALA11 4.9 5.5 1.0
CB A:ALA14 5.0 6.4 1.0
O A:HOH2038 5.0 11.1 1.0

Copper binding site 2 out of 4 in 2xmj

Go back to Copper Binding Sites List in 2xmj
Copper binding site 2 out of 4 in the Visualising the Metal-Binding Versatility of Copper Trafficking Sites: ATX1 Side-to-Side (Aerobic)


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 2 of Visualising the Metal-Binding Versatility of Copper Trafficking Sites: ATX1 Side-to-Side (Aerobic) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu1068

b:5.4
occ:1.00
SG A:CYS12 2.2 5.3 1.0
SG A:CYS15 2.2 4.8 1.0
CU A:CU1065 2.7 5.5 1.0
CU B:CU1066 2.9 5.1 1.0
CU B:CU1065 3.0 5.5 1.0
CB A:CYS15 3.2 4.5 1.0
N A:CYS15 3.2 4.6 1.0
N A:CYS12 3.2 4.6 1.0
CB A:CYS12 3.3 4.5 1.0
O A:CYS12 3.6 4.7 1.0
CA A:CYS12 3.6 4.6 1.0
CA A:CYS15 3.7 4.8 1.0
C A:CYS12 3.8 4.6 1.0
SG B:CYS12 3.8 5.4 1.0
SG B:CYS15 3.9 5.0 1.0
CB A:ALA11 3.9 5.6 1.0
C A:ALA11 3.9 4.7 1.0
N A:ALA11 4.0 4.9 1.0
C A:ALA14 4.1 4.5 1.0
CA A:ALA11 4.2 4.8 1.0
CB A:ALA14 4.2 6.4 1.0
N A:ALA14 4.3 5.2 1.0
CA A:ALA14 4.4 5.4 1.0
CB B:ALA14 4.5 6.0 1.0
N A:GLU13 4.7 4.8 1.0
O A:ALA11 4.8 5.5 1.0
CL A:CL1067 4.8 6.8 0.5

Copper binding site 3 out of 4 in 2xmj

Go back to Copper Binding Sites List in 2xmj
Copper binding site 3 out of 4 in the Visualising the Metal-Binding Versatility of Copper Trafficking Sites: ATX1 Side-to-Side (Aerobic)


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 3 of Visualising the Metal-Binding Versatility of Copper Trafficking Sites: ATX1 Side-to-Side (Aerobic) within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cu1065

b:5.5
occ:1.00
SG B:CYS15 2.2 5.0 1.0
SG B:CYS12 2.2 5.4 1.0
CU A:CU1065 2.6 5.5 1.0
CU B:CU1066 3.0 5.1 1.0
CU A:CU1068 3.0 5.4 1.0
N B:CYS15 3.1 4.7 1.0
CB B:CYS15 3.2 4.5 1.0
N B:CYS12 3.2 5.1 1.0
CB B:CYS12 3.3 5.0 1.0
O B:CYS12 3.6 5.0 1.0
CA B:CYS12 3.6 5.2 1.0
CA B:CYS15 3.7 4.4 1.0
C B:CYS12 3.8 4.8 1.0
SG A:CYS12 3.8 5.3 1.0
C B:ALA11 3.9 5.1 1.0
SG A:CYS15 3.9 4.8 1.0
CB B:ALA11 4.0 6.2 1.0
N B:ALA11 4.0 5.1 1.0
C B:ALA14 4.1 4.5 1.0
CA B:ALA11 4.1 5.4 1.0
CB B:ALA14 4.2 6.0 1.0
N B:ALA14 4.3 5.3 1.0
CA B:ALA14 4.4 5.3 1.0
CB A:ALA14 4.5 6.4 1.0
N B:GLU13 4.7 4.9 1.0
O B:ALA11 4.8 6.0 1.0
CL A:CL1067 4.8 6.8 0.5
C B:CYS15 5.0 4.7 1.0

Copper binding site 4 out of 4 in 2xmj

Go back to Copper Binding Sites List in 2xmj
Copper binding site 4 out of 4 in the Visualising the Metal-Binding Versatility of Copper Trafficking Sites: ATX1 Side-to-Side (Aerobic)


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 4 of Visualising the Metal-Binding Versatility of Copper Trafficking Sites: ATX1 Side-to-Side (Aerobic) within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cu1066

b:5.1
occ:1.00
SG B:CYS15 2.2 5.0 1.0
SG A:CYS15 2.2 4.8 1.0
CL A:CL1066 2.4 5.1 1.0
CU A:CU1068 2.9 5.4 1.0
CU B:CU1065 3.0 5.5 1.0
CB B:CYS15 3.2 4.5 1.0
CB A:CYS15 3.2 4.5 1.0
CA B:CYS15 3.2 4.4 1.0
CA A:CYS15 3.3 4.8 1.0
N A:CYS15 3.4 4.6 1.0
N B:CYS15 3.4 4.7 1.0
C B:ALA14 4.0 4.5 1.0
C A:ALA14 4.0 4.5 1.0
O B:ALA14 4.2 5.4 1.0
O A:ALA14 4.3 4.9 1.0
CB A:ALA14 4.5 6.4 1.0
CB B:ALA14 4.5 6.0 1.0
NE2 A:HIS61 4.6 8.9 1.0
C B:CYS15 4.7 4.7 1.0
SG A:CYS12 4.7 5.3 1.0
NE2 B:HIS61 4.7 10.5 1.0
CU A:CU1065 4.7 5.5 1.0
C A:CYS15 4.7 4.9 1.0
SG B:CYS12 4.7 5.4 1.0
CE1 B:HIS61 4.8 11.2 1.0
CE1 A:HIS61 4.8 10.0 1.0
CA A:ALA14 4.8 5.4 1.0
CA B:ALA14 4.9 5.3 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: Sun Dec 13 11:07:37 2020

Last articles

Zn in 8WB0
Zn in 8WAX
Zn in 8WAU
Zn in 8WAZ
Zn in 8WAY
Zn in 8WAV
Zn in 8WAW
Zn in 8WAT
Zn in 8W7M
Zn in 8WD3
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy