Copper in PDB 3lzq: Crystal Structure Analysis of Manganese Treated P19 Protein From Campylobacter Jejuni at 1.41 A at pH 9

The structure of Crystal Structure Analysis of Manganese Treated P19 Protein From Campylobacter Jejuni at 1.41 A at pH 9, PDB code: 3lzq was solved by T.I.Doukov, A.C.K.Chan, M.Scofield, A.B.Ramin, S.A.L.Tom-Yew, M.E.P.Murphy, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	19.21 / 1.41
Space group	P 21 21 2
Cell size a, b, c (Å), α, β, γ (°)	54.357, 73.619, 75.049, 90.00, 90.00, 90.00
R / Rfree (%)	16.7 / 20.8

The structure of Crystal Structure Analysis of Manganese Treated P19 Protein From Campylobacter Jejuni at 1.41 A at pH 9 also contains other interesting chemical elements:

Manganese

(Mn)

2 atoms

The binding sites of Copper atom in the Crystal Structure Analysis of Manganese Treated P19 Protein From Campylobacter Jejuni at 1.41 A at pH 9 (pdb code 3lzq). This binding sites where shown within 5.0 Angstroms radius around Copper atom.
In total 2 binding sites of Copper where determined in the Crystal Structure Analysis of Manganese Treated P19 Protein From Campylobacter Jejuni at 1.41 A at pH 9, PDB code: 3lzq:
Jump to Copper binding site number: 1; 2;

Copper binding site 1 out of 2 in the Crystal Structure Analysis of Manganese Treated P19 Protein From Campylobacter Jejuni at 1.41 A at pH 9


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 1 of Crystal Structure Analysis of Manganese Treated P19 Protein From Campylobacter Jejuni at 1.41 A at pH 9 within 5.0Å range: probe atom residue distance (Å) B Occ A:Cu200 b:19.9 occ:1.00 NE2 B:HIS132 2.0 13.5 1.0 NE2 A:HIS42 2.1 18.1 1.0 NE2 A:HIS95 2.1 12.7 1.0 SD A:MET88 2.2 18.2 1.0 CE1 B:HIS132 2.9 14.3 1.0 CE1 A:HIS95 2.9 17.5 1.0 CE1 A:HIS42 3.0 20.4 1.0 CD2 A:HIS42 3.0 15.2 1.0 CG A:MET88 3.1 18.1 1.0 CD2 B:HIS132 3.2 20.0 1.0 CD2 A:HIS95 3.2 13.4 1.0 CE A:MET88 3.5 17.4 1.0 OE2 A:GLU44 4.0 18.9 1.0 ND1 B:HIS132 4.0 15.7 1.0 ND1 A:HIS42 4.1 16.9 1.0 ND1 A:HIS95 4.1 22.1 1.0 CG A:HIS42 4.2 15.4 1.0 CG B:HIS132 4.2 18.4 1.0 CG A:HIS95 4.2 13.7 1.0 CA A:GLY97 4.3 16.7 1.0 CG1 A:ILE25 4.3 18.5 1.0 CD1 A:ILE25 4.4 18.1 1.0 CB A:MET88 4.4 17.7 1.0 CG A:GLU44 4.7 16.0 1.0 CD A:GLU44 4.7 19.3 1.0 N A:GLY97 4.8 17.2 1.0 C A:GLY97 4.8 16.4 1.0

Copper binding site 2 out of 2 in the Crystal Structure Analysis of Manganese Treated P19 Protein From Campylobacter Jejuni at 1.41 A at pH 9


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 2 of Crystal Structure Analysis of Manganese Treated P19 Protein From Campylobacter Jejuni at 1.41 A at pH 9 within 5.0Å range: probe atom residue distance (Å) B Occ B:Cu200 b:28.1 occ:1.00 NE2 B:HIS42 2.0 21.8 1.0 NE2 B:HIS95 2.1 22.0 1.0 NE2 A:HIS132 2.2 24.6 1.0 SD B:MET88 2.2 24.2 1.0 CE1 B:HIS42 2.9 24.7 1.0 CE1 B:HIS95 3.0 26.4 1.0 CD2 B:HIS42 3.1 25.9 1.0 CD2 B:HIS95 3.1 21.9 1.0 CD2 A:HIS132 3.2 21.7 1.0 CE1 A:HIS132 3.2 22.9 1.0 CG B:MET88 3.2 22.5 1.0 CE B:MET88 3.6 25.4 1.0 OE2 B:GLU44 3.6 35.6 1.0 ND1 B:HIS42 4.0 25.2 1.0 ND1 B:HIS95 4.2 24.0 1.0 CG B:HIS42 4.2 23.8 1.0 CG B:HIS95 4.3 17.2 1.0 CD B:GLU44 4.3 30.4 1.0 CG B:GLU44 4.3 29.2 1.0 ND1 A:HIS132 4.3 24.3 1.0 CA B:GLY97 4.3 20.1 1.0 CG A:HIS132 4.3 21.8 1.0 SD B:MET27 4.5 39.5 1.0 CB B:MET88 4.6 17.5 1.0 N B:GLY97 4.8 18.9 1.0 C B:GLY97 5.0 20.4 1.0

A.C.Chan, T.I.Doukov, M.Scofield, S.A.Tom-Yew, A.B.Ramin, J.K.Mackichan, E.C.Gaynor, M.E.Murphy. Structure and Function of P19, A High-Affinity Iron Transporter of the Human Pathogen Campylobacter Jejuni. J.Mol.Biol. V. 401 590 2010.
ISSN: ISSN 0022-2836
PubMed: 20600116
DOI: 10.1016/J.JMB.2010.06.038