Copper in PDB 6wed: Copper-Bound E44Q Variant of Campylobacter Jejuni P19

The structure of Copper-Bound E44Q Variant of Campylobacter Jejuni P19, PDB code: 6wed was solved by A.C.Chan, M.E.Murphy, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	28.51 / 1.90
Space group	P 21 21 2
Cell size a, b, c (Å), α, β, γ (°)	55.347, 73.336, 78.957, 90, 90, 90
R / Rfree (%)	17.4 / 22.2

The binding sites of Copper atom in the Copper-Bound E44Q Variant of Campylobacter Jejuni P19 (pdb code 6wed). This binding sites where shown within 5.0 Angstroms radius around Copper atom.
In total 2 binding sites of Copper where determined in the Copper-Bound E44Q Variant of Campylobacter Jejuni P19, PDB code: 6wed:
Jump to Copper binding site number: 1; 2;

Copper binding site 1 out of 2 in the Copper-Bound E44Q Variant of Campylobacter Jejuni P19


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 1 of Copper-Bound E44Q Variant of Campylobacter Jejuni P19 within 5.0Å range: probe atom residue distance (Å) B Occ A:Cu201 b:19.0 occ:0.80 NE2 A:HIS42 2.0 20.0 1.0 NE2 A:HIS95 2.1 22.9 1.0 NE2 B:HIS132 2.2 20.7 1.0 SD A:MET88 2.2 21.3 1.0 CE1 A:HIS42 2.9 21.9 1.0 HG3 A:MET88 3.0 26.5 1.0 CE1 B:HIS132 3.0 20.6 1.0 CD2 A:HIS42 3.0 19.3 1.0 CE1 A:HIS95 3.0 24.9 1.0 HE1 B:HIS132 3.1 24.7 1.0 CG A:MET88 3.1 22.1 1.0 HE1 A:HIS42 3.1 26.3 1.0 HE1 A:HIS95 3.2 29.8 1.0 CD2 A:HIS95 3.2 19.2 1.0 HD2 A:HIS42 3.2 23.2 1.0 CD2 B:HIS132 3.3 21.6 1.0 HG2 A:MET88 3.3 26.5 1.0 HA3 A:GLY97 3.3 20.6 1.0 HE3 A:MET88 3.4 26.6 1.0 CE A:MET88 3.4 22.2 1.0 HD2 A:HIS95 3.4 23.1 1.0 HD2 B:HIS132 3.6 25.9 1.0 HG12 A:ILE25 3.6 23.9 1.0 HD11 A:ILE25 3.6 26.1 1.0 HE1 A:MET88 3.6 26.6 1.0 ND1 A:HIS42 4.0 18.7 1.0 CG A:HIS42 4.1 17.1 1.0 HE2 A:MET88 4.2 26.6 1.0 ND1 B:HIS132 4.2 22.3 1.0 ND1 A:HIS95 4.2 24.4 1.0 CA A:GLY97 4.3 17.2 1.0 CG A:HIS95 4.3 23.4 1.0 CG1 A:ILE25 4.4 19.9 1.0 CG B:HIS132 4.4 23.4 1.0 CD1 A:ILE25 4.4 21.8 1.0 CB A:MET88 4.6 20.0 1.0 OE1 A:GLN44 4.6 27.5 1.0 HB2 A:ALA90 4.7 32.0 1.0 HB2 A:MET88 4.7 24.0 1.0 HG13 A:ILE25 4.7 23.9 1.0 HD13 A:ILE25 4.7 26.1 1.0 N A:GLY97 4.8 19.5 1.0 HD1 A:HIS42 4.8 22.4 1.0 C A:GLY97 4.8 17.2 1.0 HA2 A:GLY97 4.9 20.6 1.0 HB3 A:MET88 4.9 24.0 1.0 HD1 B:HIS132 4.9 26.7 1.0 HD1 A:HIS95 5.0 29.2 1.0 H A:GLY97 5.0 23.4 1.0

Copper binding site 2 out of 2 in the Copper-Bound E44Q Variant of Campylobacter Jejuni P19


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 2 of Copper-Bound E44Q Variant of Campylobacter Jejuni P19 within 5.0Å range: probe atom residue distance (Å) B Occ B:Cu201 b:18.7 occ:0.70 NE2 B:HIS95 2.1 25.0 1.0 NE2 A:HIS132 2.1 24.6 1.0 NE2 B:HIS42 2.1 24.7 1.0 SD B:MET88 2.3 23.3 1.0 CE1 B:HIS95 2.9 22.5 1.0 CE1 A:HIS132 3.0 27.3 1.0 HG3 B:MET88 3.0 24.1 1.0 CE1 B:HIS42 3.0 27.4 1.0 HE1 B:HIS95 3.0 27.0 1.0 CD2 B:HIS42 3.1 26.5 1.0 HE1 A:HIS132 3.1 32.8 1.0 CG B:MET88 3.1 20.1 1.0 CD2 A:HIS132 3.2 27.0 1.0 CD2 B:HIS95 3.2 21.0 1.0 HE1 B:HIS42 3.2 32.9 1.0 HD2 B:HIS42 3.3 31.8 1.0 HG2 B:MET88 3.3 24.1 1.0 HD2 A:HIS132 3.4 32.4 1.0 HD2 B:HIS95 3.4 25.2 1.0 CE B:MET88 3.5 27.5 1.0 HE3 B:MET88 3.5 33.0 1.0 HA3 B:GLY97 3.5 27.4 1.0 HD11 B:ILE25 3.5 52.4 1.0 HG12 B:ILE25 3.6 48.4 1.0 HE1 B:MET88 3.7 33.0 1.0 HD13 B:ILE25 4.0 52.4 1.0 ND1 B:HIS95 4.1 21.9 1.0 ND1 B:HIS42 4.1 26.2 1.0 CD1 B:ILE25 4.1 43.6 1.0 ND1 A:HIS132 4.1 25.4 1.0 CG B:HIS42 4.2 26.2 1.0 CG B:HIS95 4.3 20.9 1.0 CG A:HIS132 4.3 27.1 1.0 HE2 B:MET88 4.3 33.0 1.0 CG1 B:ILE25 4.4 40.3 1.0 CA B:GLY97 4.4 22.9 1.0 CB B:MET88 4.6 18.4 1.0 OE1 B:GLN44 4.6 26.8 1.0 N B:GLY97 4.7 23.5 1.0 HB2 B:MET88 4.8 22.1 1.0 H B:GLY97 4.8 28.2 1.0 O B:HOH311 4.8 36.2 1.0 HB2 B:ALA90 4.8 27.8 1.0 HD1 B:HIS95 4.8 26.2 1.0 HD1 B:HIS42 4.9 31.5 1.0 HG13 B:ILE25 4.9 48.4 1.0 HD1 A:HIS132 4.9 30.5 1.0 C B:GLY97 4.9 22.8 1.0 HG21 B:ILE25 4.9 42.8 1.0 HB3 B:MET88 4.9 22.1 1.0

A.C.K.Chan, H.Lin, D.Koch, G.Grass, D.H.Nies, M.E.P.Murphy. A Copper Site Is Required For Iron Transport By the Periplasmic Proteins P19 and Fetp. Metallomics V. 12 1530 2020.
ISSN: ESSN 1756-591X
PubMed: 32780051
DOI: 10.1039/D0MT00130A