Copper in PDB 3lzr: Crystal Structure Analysis of Manganese Treated P19 Protein From Campylobacter Jejuni at 2.73 A at pH 9 and Manganese Peak Wavelength (1.893 A)

The structure of Crystal Structure Analysis of Manganese Treated P19 Protein From Campylobacter Jejuni at 2.73 A at pH 9 and Manganese Peak Wavelength (1.893 A), PDB code: 3lzr 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)	19.26 / 2.73
Space group	P 21 21 2
Cell size a, b, c (Å), α, β, γ (°)	54.499, 73.797, 75.217, 90.00, 90.00, 90.00
R / Rfree (%)	19.5 / 24.5

The structure of Crystal Structure Analysis of Manganese Treated P19 Protein From Campylobacter Jejuni at 2.73 A at pH 9 and Manganese Peak Wavelength (1.893 A) 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 2.73 A at pH 9 and Manganese Peak Wavelength (1.893 A) (pdb code 3lzr). 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 2.73 A at pH 9 and Manganese Peak Wavelength (1.893 A), PDB code: 3lzr:
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 2.73 A at pH 9 and Manganese Peak Wavelength (1.893 A)


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 2.73 A at pH 9 and Manganese Peak Wavelength (1.893 A) within 5.0Å range: probe atom residue distance (Å) B Occ A:Cu200 b:41.4 occ:1.00 NE2 A:HIS95 2.1 30.7 1.0 NE2 A:HIS42 2.2 35.5 1.0 NE2 B:HIS132 2.3 33.8 1.0 SD A:MET88 2.4 31.8 1.0 CE1 A:HIS42 2.9 34.4 1.0 CE1 A:HIS95 3.0 31.4 1.0 CE1 B:HIS132 3.1 34.6 1.0 CD2 A:HIS95 3.1 30.9 1.0 CG A:MET88 3.2 33.1 1.0 CD2 A:HIS42 3.3 33.9 1.0 CD2 B:HIS132 3.4 35.5 1.0 CE A:MET88 3.7 30.8 1.0 OE2 A:GLU44 4.0 39.1 1.0 ND1 A:HIS42 4.1 34.1 1.0 ND1 A:HIS95 4.2 33.1 1.0 CG A:HIS95 4.2 31.6 1.0 ND1 B:HIS132 4.3 34.0 1.0 CA A:GLY97 4.3 32.2 1.0 CG A:HIS42 4.3 33.2 1.0 CD1 A:ILE25 4.3 41.4 1.0 CG1 A:ILE25 4.4 43.4 1.0 CG A:GLU44 4.4 35.9 1.0 CG B:HIS132 4.5 35.2 1.0 CD A:GLU44 4.5 37.8 1.0 CB A:MET88 4.6 33.6 1.0 N A:GLY97 4.7 31.9 1.0 C A:GLY97 4.8 33.0 1.0

Copper binding site 2 out of 2 in the Crystal Structure Analysis of Manganese Treated P19 Protein From Campylobacter Jejuni at 2.73 A at pH 9 and Manganese Peak Wavelength (1.893 A)


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 2.73 A at pH 9 and Manganese Peak Wavelength (1.893 A) within 5.0Å range: probe atom residue distance (Å) B Occ B:Cu200 b:44.5 occ:1.00 NE2 B:HIS95 2.1 36.2 1.0 NE2 A:HIS132 2.2 34.3 1.0 NE2 B:HIS42 2.2 38.9 1.0 SD B:MET88 2.5 38.3 1.0 CE1 A:HIS132 3.0 34.6 1.0 CE1 B:HIS95 3.1 37.9 1.0 CD2 B:HIS95 3.1 34.8 1.0 CE1 B:HIS42 3.1 37.3 1.0 CD2 B:HIS42 3.2 37.1 1.0 CD2 A:HIS132 3.4 36.1 1.0 CG B:MET88 3.4 35.8 1.0 OE1 B:GLU44 3.8 42.7 1.0 CE B:MET88 3.8 34.6 1.0 ND1 A:HIS132 4.2 34.4 1.0 ND1 B:HIS95 4.2 36.2 1.0 CG B:HIS95 4.2 34.1 1.0 ND1 B:HIS42 4.2 36.7 1.0 CG B:HIS42 4.3 35.9 1.0 CA B:GLY97 4.3 33.2 1.0 CG A:HIS132 4.4 35.3 1.0 CD B:GLU44 4.5 42.2 1.0 CG B:GLU44 4.6 38.1 1.0 CB B:MET88 4.8 35.2 1.0 N B:GLY97 4.8 32.9 1.0 C B:GLY97 5.0 33.6 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