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Copper in PDB 5ffc: Copm in the Cu(II)-Bound Form

Protein crystallography data

The structure of Copm in the Cu(II)-Bound Form, PDB code: 5ffc was solved by S.Zhao, X.Wang, L.Liu, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 27.10 / 2.01
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 32.240, 86.669, 53.431, 90.00, 92.33, 90.00
R / Rfree (%) 22.6 / 26.9

Copper Binding Sites:

The binding sites of Copper atom in the Copm in the Cu(II)-Bound Form (pdb code 5ffc). This binding sites where shown within 5.0 Angstroms radius around Copper atom.
In total 2 binding sites of Copper where determined in the Copm in the Cu(II)-Bound Form, PDB code: 5ffc:
Jump to Copper binding site number: 1; 2;

Copper binding site 1 out of 2 in 5ffc

Go back to Copper Binding Sites List in 5ffc
Copper binding site 1 out of 2 in the Copm in the Cu(II)-Bound Form


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 1 of Copm in the Cu(II)-Bound Form within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu201

b:55.1
occ:1.00
OD2 A:ASP59 1.8 52.4 0.9
ND1 A:HIS56 1.9 49.0 1.0
NE2 A:HIS148 2.2 41.4 1.0
CG A:ASP59 2.7 45.4 1.0
CE1 A:HIS56 2.8 51.2 1.0
OD1 A:ASP59 2.8 43.7 0.1
CG A:HIS56 3.0 50.3 1.0
CD2 A:HIS148 3.0 37.5 1.0
O A:HIS56 3.2 44.8 1.0
CA A:HIS56 3.3 46.9 1.0
CE1 A:HIS148 3.3 40.9 1.0
CB A:HIS56 3.5 49.8 1.0
C A:HIS56 3.7 48.0 1.0
NE2 A:HIS56 3.9 51.5 1.0
CD2 A:HIS56 4.1 51.3 1.0
CB A:ASP59 4.1 44.2 1.0
CG A:HIS148 4.2 37.0 1.0
O A:MET124 4.3 46.9 1.0
CE A:MET151 4.3 45.5 1.0
ND1 A:HIS148 4.3 37.5 1.0
CA A:ALA125 4.4 42.0 1.0
N A:HIS56 4.5 47.5 1.0
O A:PRO55 4.7 53.3 1.0
CE A:MET117 4.8 54.9 1.0
SD A:MET117 4.9 62.9 1.0
C A:PRO55 5.0 48.8 1.0

Copper binding site 2 out of 2 in 5ffc

Go back to Copper Binding Sites List in 5ffc
Copper binding site 2 out of 2 in the Copm in the Cu(II)-Bound Form


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 2 of Copm in the Cu(II)-Bound Form within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu202

b:56.2
occ:1.00
NE2 A:HIS121 2.5 40.8 1.0
NE2 A:HIS118 2.6 51.3 1.0
O A:HOH360 2.6 43.3 1.0
CD2 A:HIS121 3.1 42.0 1.0
CD2 A:HIS118 3.1 45.5 1.0
CE1 A:HIS118 3.7 53.0 1.0
CE1 A:HIS121 3.7 41.2 1.0
CG A:HIS118 4.3 53.9 1.0
CG A:HIS121 4.4 39.7 1.0
O A:GLN119 4.5 38.1 1.0
ND1 A:HIS118 4.6 55.0 1.0
ND1 A:HIS121 4.6 42.2 1.0

Reference:

S.Zhao, X.Wang, G.Niu, W.Dong, J.Wang, Y.Fang, Y.Lin, L.Liu. Structural Basis For Copper/Silver Binding By the Synechocystis Metallochaperone Copm Acta Crystallogr.,Sect.D V. 72 997 2016.
ISSN: ESSN 1399-0047
DOI: 10.1107/S2059798316011943
Page generated: Mon Jul 14 04:34:30 2025

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