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Copper in PDB 2xmw: Pacs, N-Terminal Domain, From Synechocystis PCC6803

Protein crystallography data

The structure of Pacs, N-Terminal Domain, From Synechocystis PCC6803, PDB code: 2xmw 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) 51.85 / 1.80
Space group P 3 2 1
Cell size a, b, c (Å), α, β, γ (°) 45.580, 45.580, 51.831, 90.00, 90.00, 120.00
R / Rfree (%) 24.332 / 25.922

Copper Binding Sites:

The binding sites of Copper atom in the Pacs, N-Terminal Domain, From Synechocystis PCC6803 (pdb code 2xmw). This binding sites where shown within 5.0 Angstroms radius around Copper atom.
In total only one binding site of Copper was determined in the Pacs, N-Terminal Domain, From Synechocystis PCC6803, PDB code: 2xmw:

Copper binding site 1 out of 1 in 2xmw

Go back to Copper Binding Sites List in 2xmw
Copper binding site 1 out of 1 in the Pacs, N-Terminal Domain, From Synechocystis PCC6803


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 1 of Pacs, N-Terminal Domain, From Synechocystis PCC6803 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu101

b:13.6
occ:1.00
SG A:CYS17 2.2 15.3 1.0
SG A:CYS14 2.2 15.7 1.0
CB A:CYS17 3.4 14.5 1.0
N A:CYS14 3.4 16.0 1.0
N A:CYS17 3.4 15.2 1.0
CB A:CYS14 3.5 14.7 1.0
CA A:CYS17 3.8 14.6 1.0
CA A:CYS14 3.9 15.4 1.0
O A:CYS14 3.9 15.3 1.0
C A:ARG13 4.1 18.6 1.0
N A:ARG13 4.1 18.6 1.0
CB A:ARG13 4.1 19.7 1.0
C A:CYS14 4.2 16.7 1.0
CA A:ARG13 4.3 19.3 1.0
C A:ALA16 4.3 15.4 1.0
CB A:ALA16 4.4 15.3 1.0
N A:ALA16 4.6 14.8 1.0
CA A:ALA16 4.7 15.8 1.0
OH A:TYR65 4.8 19.9 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: Thu Sep 3 16:56:04 2020
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