Copper in PDB 6wee: Copper-Bound M88I Variant of Campylobacter Jejuni P19

The structure of Copper-Bound M88I Variant of Campylobacter Jejuni P19, PDB code: 6wee 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)	30.55 / 2.30
Space group	P 62
Cell size a, b, c (Å), α, β, γ (°)	132.965, 132.965, 104.878, 90, 90, 120
R / Rfree (%)	23.5 / 27.7

The binding sites of Copper atom in the Copper-Bound M88I Variant of Campylobacter Jejuni P19 (pdb code 6wee). This binding sites where shown within 5.0 Angstroms radius around Copper atom.
In total 6 binding sites of Copper where determined in the Copper-Bound M88I Variant of Campylobacter Jejuni P19, PDB code: 6wee:
Jump to Copper binding site number: 1; 2; 3; 4; 5; 6;

Copper binding site 1 out of 6 in the Copper-Bound M88I 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 M88I Variant of Campylobacter Jejuni P19 within 5.0Å range: probe atom residue distance (Å) B Occ A:Cu201 b:51.5 occ:0.85 NE2 A:HIS42 2.0 54.9 1.0 OE1 A:GLU44 2.0 65.6 1.0 NE2 A:HIS95 2.0 51.0 1.0 NE2 B:HIS132 2.1 64.1 1.0 HE1 B:HIS132 2.5 79.1 1.0 CE1 B:HIS132 2.6 65.7 1.0 HG2 A:GLU44 2.9 61.4 1.0 CD2 A:HIS42 2.9 54.3 1.0 CE1 A:HIS95 3.0 49.8 1.0 CD A:GLU44 3.0 61.4 1.0 HD2 A:HIS42 3.0 65.5 1.0 CD2 A:HIS95 3.0 48.3 1.0 CE1 A:HIS42 3.1 54.6 1.0 HE1 A:HIS95 3.1 60.0 1.0 HD2 A:HIS95 3.3 58.2 1.0 CD2 B:HIS132 3.3 63.8 1.0 HE1 A:HIS42 3.3 65.7 1.0 CG A:GLU44 3.4 50.9 1.0 HA3 A:GLY97 3.6 40.2 1.0 HG22 A:ILE88 3.7 39.1 1.0 HD2 B:HIS132 3.8 76.8 1.0 HG3 A:GLU44 3.8 61.4 1.0 HB A:ILE88 3.8 38.0 1.0 ND1 B:HIS132 3.8 64.0 1.0 HG21 A:ILE88 3.8 39.1 1.0 HD13 A:ILE88 3.9 39.1 1.0 ND1 A:HIS95 4.1 48.4 1.0 OE2 A:GLU44 4.1 65.7 1.0 CG A:HIS42 4.1 53.1 1.0 CG2 A:ILE88 4.1 32.3 1.0 ND1 A:HIS42 4.1 53.9 1.0 CG A:HIS95 4.1 45.0 1.0 CG B:HIS132 4.2 59.0 1.0 HB2 A:ALA90 4.3 37.4 1.0 HD12 A:ILE88 4.3 39.1 1.0 CB A:ILE88 4.4 31.4 1.0 HD1 B:HIS132 4.5 77.1 1.0 CA A:GLY97 4.5 33.3 1.0 CD1 A:ILE88 4.6 32.4 1.0 HG13 A:ILE25 4.7 51.0 1.0 CB A:GLU44 4.7 42.7 1.0 HB3 A:GLU44 4.8 51.5 1.0 HD1 A:HIS95 4.8 58.4 1.0 HA2 A:GLY97 4.9 40.2 1.0 HG21 A:ILE25 4.9 55.4 1.0 HD1 A:HIS42 4.9 65.0 1.0

Copper binding site 2 out of 6 in the Copper-Bound M88I 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 M88I Variant of Campylobacter Jejuni P19 within 5.0Å range: probe atom residue distance (Å) B Occ B:Cu201 b:45.1 occ:0.75 OE1 B:GLU44 2.0 62.0 1.0 NE2 B:HIS95 2.1 57.5 1.0 NE2 A:HIS132 2.1 46.2 1.0 NE2 B:HIS42 2.1 45.5 1.0 HD11 B:ILE88 2.4 41.0 1.0 HE1 A:HIS132 2.8 51.6 1.0 CE1 A:HIS132 2.8 42.8 1.0 CE1 B:HIS95 2.8 58.3 1.0 HE1 B:HIS95 2.8 70.2 1.0 CD2 B:HIS42 2.8 44.6 1.0 HD2 B:HIS42 2.9 53.8 1.0 HD12 B:ILE88 2.9 41.0 1.0 CD1 B:ILE88 3.1 34.0 1.0 CD B:GLU44 3.1 60.0 1.0 HG2 B:GLU44 3.2 66.7 1.0 CE1 B:HIS42 3.3 46.0 1.0 CD2 B:HIS95 3.3 56.9 1.0 CD2 A:HIS132 3.3 42.5 1.0 HG13 B:ILE88 3.4 37.5 1.0 HE1 B:MET27 3.5 73.8 1.0 HE1 B:HIS42 3.6 55.5 1.0 HD2 B:HIS95 3.6 68.5 1.0 HD2 A:HIS132 3.7 51.2 1.0 CG B:GLU44 3.7 55.3 1.0 CG1 B:ILE88 3.8 31.0 1.0 HA3 B:GLY97 3.8 41.5 1.0 HD13 B:ILE88 3.9 41.0 1.0 HE2 B:MET27 4.0 73.8 1.0 ND1 A:HIS132 4.0 43.0 1.0 ND1 B:HIS95 4.0 57.0 1.0 CG B:HIS42 4.1 42.6 1.0 HG3 B:GLU44 4.2 66.7 1.0 OE2 B:GLU44 4.2 61.2 1.0 HG13 B:ILE25 4.2 43.7 1.0 CE B:MET27 4.2 61.3 1.0 ND1 B:HIS42 4.2 45.2 1.0 CG B:HIS95 4.3 52.9 1.0 CG A:HIS132 4.3 40.8 1.0 HG12 B:ILE88 4.4 37.5 1.0 HB2 B:ALA90 4.5 21.4 1.0 HG21 B:ILE25 4.5 42.4 1.0 HB B:ILE88 4.7 34.9 1.0 HD1 A:HIS132 4.7 51.9 1.0 HB B:ILE25 4.7 42.5 1.0 HD1 B:HIS95 4.7 68.7 1.0 CA B:GLY97 4.7 34.4 1.0 HB3 B:GLU44 4.8 57.9 1.0 HE3 B:MET27 4.9 73.8 1.0 CB B:ILE88 4.9 28.9 1.0 CB B:GLU44 4.9 48.0 1.0

Copper binding site 3 out of 6 in the Copper-Bound M88I 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 3 of Copper-Bound M88I Variant of Campylobacter Jejuni P19 within 5.0Å range: probe atom residue distance (Å) B Occ C:Cu201 b:41.5 occ:0.90 OE2 C:GLU44 2.1 50.8 1.0 NE2 D:HIS132 2.2 37.6 1.0 NE2 C:HIS95 2.2 30.8 1.0 HD11 C:ILE88 2.2 31.4 1.0 NE2 C:HIS42 2.2 39.0 1.0 HD2 C:HIS42 2.8 44.5 1.0 HD12 C:ILE88 2.8 31.4 1.0 CD2 C:HIS42 2.8 36.9 1.0 CE1 D:HIS132 2.9 33.4 1.0 HE1 D:HIS132 2.9 40.4 1.0 CD1 C:ILE88 2.9 25.9 1.0 HG2 C:GLU44 2.9 54.3 1.0 CE1 C:HIS95 3.0 32.0 1.0 HE1 C:HIS95 3.0 38.6 1.0 CD C:GLU44 3.0 49.5 1.0 CD2 C:HIS95 3.3 30.8 1.0 CD2 D:HIS132 3.3 34.8 1.0 HG13 C:ILE88 3.4 33.4 1.0 CG C:GLU44 3.4 45.0 1.0 CE1 C:HIS42 3.4 37.4 1.0 HD2 C:HIS95 3.6 37.2 1.0 HG3 C:GLU44 3.6 54.3 1.0 HD2 D:HIS132 3.7 42.0 1.0 HD13 C:ILE88 3.7 31.4 1.0 CG1 C:ILE88 3.7 27.6 1.0 HE1 C:HIS42 3.8 45.1 1.0 HA3 C:GLY97 3.9 38.7 1.0 ND1 D:HIS132 4.1 34.5 1.0 CG C:HIS42 4.1 35.5 1.0 OE1 C:GLU44 4.2 50.8 1.0 ND1 C:HIS95 4.2 31.6 1.0 HG12 C:ILE88 4.2 33.4 1.0 ND1 C:HIS42 4.3 37.2 1.0 HB2 C:ALA90 4.3 37.4 1.0 CG D:HIS132 4.3 34.8 1.0 CG C:HIS95 4.4 30.8 1.0 HG13 C:ILE25 4.4 48.6 1.0 SD C:MET27 4.4 59.6 1.0 HG21 C:ILE25 4.6 51.7 1.0 HB C:ILE25 4.8 50.2 1.0 CA C:GLY97 4.8 32.0 1.0 CB C:GLU44 4.8 40.5 1.0 HD1 D:HIS132 4.8 41.6 1.0 HB C:ILE88 4.9 37.6 1.0 HD1 C:HIS95 4.9 38.2 1.0 HE1 C:MET27 4.9 76.0 1.0 CB C:ILE88 5.0 31.1 1.0 HB3 C:GLU44 5.0 48.9 1.0

Copper binding site 4 out of 6 in the Copper-Bound M88I 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 4 of Copper-Bound M88I Variant of Campylobacter Jejuni P19 within 5.0Å range: probe atom residue distance (Å) B Occ D:Cu201 b:49.6 occ:0.80 HD11 D:ILE88 1.8 91.5 1.0 OE1 D:GLU44 1.9 74.4 1.0 NE2 C:HIS132 2.1 28.2 1.0 HD12 D:ILE88 2.1 91.5 1.0 NE2 D:HIS42 2.2 44.0 1.0 NE2 D:HIS95 2.2 35.1 1.0 CD1 D:ILE88 2.4 76.0 1.0 CE1 C:HIS132 2.9 21.3 1.0 HE1 C:HIS132 2.9 25.8 1.0 HG2 D:GLU44 2.9 75.8 1.0 CD D:GLU44 2.9 74.0 1.0 HD13 D:ILE88 3.0 91.5 1.0 CD2 D:HIS42 3.0 40.6 1.0 CE1 D:HIS95 3.1 29.9 1.0 HD2 D:HIS42 3.1 49.0 1.0 HE1 D:HIS95 3.2 36.1 1.0 CD2 D:HIS95 3.2 28.9 1.0 CE1 D:HIS42 3.2 41.0 1.0 CD2 C:HIS132 3.3 22.8 1.0 CG D:GLU44 3.4 63.0 1.0 HD2 D:HIS95 3.5 35.0 1.0 HG13 D:ILE88 3.5 82.9 1.0 HE1 D:HIS42 3.5 49.4 1.0 HE2 D:MET27 3.5 66.8 1.0 CG1 D:ILE88 3.5 68.9 1.0 HD2 C:HIS132 3.5 27.6 1.0 HA3 D:GLY97 3.7 25.4 1.0 HG3 D:GLU44 3.7 75.8 1.0 HE1 D:MET27 3.9 66.8 1.0 HG12 D:ILE88 4.0 82.9 1.0 OE2 D:GLU44 4.0 77.4 1.0 ND1 C:HIS132 4.1 24.2 1.0 CE D:MET27 4.1 55.4 1.0 CG D:HIS42 4.2 38.6 1.0 ND1 D:HIS95 4.2 29.1 1.0 CG C:HIS132 4.3 25.0 1.0 ND1 D:HIS42 4.3 41.3 1.0 CG D:HIS95 4.3 27.5 1.0 SD D:MET27 4.4 51.6 1.0 HB2 D:ALA90 4.5 31.2 1.0 CA D:GLY97 4.6 20.9 1.0 HB D:ILE88 4.6 63.4 1.0 HG13 D:ILE25 4.7 39.3 1.0 CB D:ILE88 4.7 52.6 1.0 CB D:GLU44 4.8 49.0 1.0 HD12 D:LEU22 4.8 40.0 1.0 HG21 D:ILE25 4.8 39.0 1.0 HB3 D:GLU44 4.8 59.1 1.0 HD1 C:HIS132 4.8 29.3 1.0 HB D:ILE25 5.0 36.4 1.0 H D:ALA98 5.0 27.1 1.0 HD1 D:HIS95 5.0 35.2 1.0 HE3 D:MET27 5.0 66.8 1.0

Copper binding site 5 out of 6 in the Copper-Bound M88I 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 5 of Copper-Bound M88I Variant of Campylobacter Jejuni P19 within 5.0Å range: probe atom residue distance (Å) B Occ E:Cu201 b:33.6 occ:0.80 OE1 E:GLU44 2.0 58.4 1.0 NE2 F:HIS132 2.1 35.6 1.0 NE2 E:HIS95 2.1 52.7 1.0 NE2 E:HIS42 2.1 36.5 1.0 HD11 E:ILE88 2.4 40.7 1.0 HE1 F:HIS132 2.7 37.6 1.0 CE1 F:HIS132 2.7 31.1 1.0 CD2 E:HIS42 2.9 33.3 1.0 HD2 E:HIS42 2.9 40.2 1.0 HG2 E:GLU44 2.9 64.8 1.0 CD E:GLU44 3.0 58.4 1.0 CE1 E:HIS95 3.1 53.7 1.0 CD1 E:ILE88 3.1 33.7 1.0 CD2 E:HIS95 3.1 51.7 1.0 HD12 E:ILE88 3.1 40.7 1.0 HE1 E:HIS95 3.2 64.7 1.0 CE1 E:HIS42 3.3 34.4 1.0 HD2 E:HIS95 3.3 62.3 1.0 CD2 F:HIS132 3.3 33.5 1.0 HG13 E:ILE88 3.3 42.5 1.0 CG E:GLU44 3.4 53.8 1.0 HG3 E:GLU44 3.6 64.8 1.0 HE1 E:HIS42 3.6 41.6 1.0 HD2 F:HIS132 3.7 40.4 1.0 HA3 E:GLY97 3.7 40.3 1.0 CG1 E:ILE88 3.8 35.1 1.0 HD13 E:ILE88 3.9 40.7 1.0 ND1 F:HIS132 4.0 34.2 1.0 CG E:HIS42 4.1 31.1 1.0 OE2 E:GLU44 4.2 63.0 1.0 ND1 E:HIS95 4.2 52.6 1.0 ND1 E:HIS42 4.2 32.8 1.0 CG E:HIS95 4.3 49.4 1.0 CG F:HIS132 4.3 33.1 1.0 HG12 E:ILE88 4.3 42.5 1.0 HB2 E:ALA90 4.5 50.5 1.0 HD21 E:LEU22 4.5 49.6 1.0 HG13 E:ILE25 4.5 35.8 1.0 CA E:GLY97 4.7 33.3 1.0 HD1 F:HIS132 4.7 41.3 1.0 O E:HOH356 4.8 29.1 1.0 CB E:GLU44 4.8 44.5 1.0 HB E:ILE88 4.9 43.0 1.0 HB E:ILE25 4.9 34.4 1.0 HB3 E:GLU44 5.0 53.7 1.0 HD1 E:HIS95 5.0 63.4 1.0 CB E:ILE88 5.0 35.6 1.0 HG21 E:ILE25 5.0 40.5 1.0

Copper binding site 6 out of 6 in the Copper-Bound M88I 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 6 of Copper-Bound M88I Variant of Campylobacter Jejuni P19 within 5.0Å range: probe atom residue distance (Å) B Occ F:Cu201 b:103.5 occ:0.95 OE2 F:GLU44 1.9 96.6 1.0 NE2 E:HIS132 2.1 89.8 1.0 NE2 F:HIS95 2.1 93.0 1.0 NE2 F:HIS42 2.1 77.4 1.0 CE1 E:HIS132 2.7 88.0 1.0 HE1 E:HIS132 2.7 105.9 1.0 CE1 F:HIS95 2.8 92.0 1.0 HE1 F:HIS95 2.8 110.6 1.0 CD2 F:HIS42 3.0 71.4 1.0 CE1 F:HIS42 3.1 71.9 1.0 HD13 F:ILE88 3.1 54.9 1.0 HD2 F:HIS42 3.1 86.0 1.0 CD F:GLU44 3.2 85.9 1.0 HG21 F:ILE88 3.2 61.8 1.0 CD2 E:HIS132 3.2 87.0 1.0 CD2 F:HIS95 3.3 90.0 1.0 HE1 F:HIS42 3.3 86.5 1.0 HB F:ILE88 3.4 56.5 1.0 HD12 F:ILE88 3.5 54.9 1.0 HD2 F:HIS95 3.6 108.3 1.0 HD2 E:HIS132 3.6 104.7 1.0 HG22 F:ILE88 3.6 61.8 1.0 HG2 F:GLU44 3.6 82.2 1.0 CG2 F:ILE88 3.7 51.3 1.0 CD1 F:ILE88 3.7 45.5 1.0 HA3 F:GLY97 3.9 48.4 1.0 ND1 E:HIS132 3.9 86.5 1.0 CG F:GLU44 4.0 68.3 1.0 CB F:ILE88 4.0 46.8 1.0 ND1 F:HIS95 4.0 90.0 1.0 OE1 F:GLU44 4.1 91.9 1.0 CG F:HIS42 4.1 67.3 1.0 ND1 F:HIS42 4.1 70.9 1.0 CG E:HIS132 4.2 80.9 1.0 HG21 F:ILE25 4.2 77.2 1.0 HB2 F:ALA90 4.2 30.5 1.0 CG F:HIS95 4.3 82.7 1.0 HG13 F:ILE25 4.4 78.7 1.0 CG1 F:ILE88 4.5 46.3 1.0 HD11 F:ILE88 4.5 54.9 1.0 HG3 F:GLU44 4.5 82.2 1.0 HD1 E:HIS132 4.6 104.0 1.0 HG23 F:ILE88 4.6 61.8 1.0 HD1 F:HIS95 4.8 108.3 1.0 CA F:GLY97 4.8 40.1 1.0 HD12 F:ILE25 4.9 79.0 1.0 HB3 F:GLU44 4.9 67.3 1.0 HD1 F:HIS42 4.9 85.4 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