Manganese 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:

Copper

(Cu)

2 atoms

The binding sites of Manganese 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 Manganese atom.
In total 2 binding sites of Manganese 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 Manganese binding site number: 1; 2;

Manganese 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 Manganese with other atoms in the Mn 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:Mn201 b:42.7 occ:0.25 OD2 A:ASP92 2.4 40.2 1.0 OE1 A:GLU44 2.7 39.3 1.0 OE2 A:GLU3 2.7 66.3 1.0 CD A:GLU3 3.3 64.0 1.0 OE1 A:GLU3 3.3 65.7 1.0 CG A:ASP92 3.4 39.7 1.0 OD1 A:ASP92 3.8 42.0 1.0 CD A:GLU44 3.8 37.8 1.0 OD1 A:ASP46 4.2 45.9 1.0 OE2 A:GLU44 4.2 39.1 1.0 OD2 A:ASP46 4.4 46.6 1.0 CG2 A:VAL20 4.6 34.8 1.0 CG A:GLU3 4.6 60.5 1.0 CB A:ASP92 4.7 38.5 1.0 CG A:ASP46 4.7 40.7 1.0

Manganese 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 Manganese with other atoms in the Mn 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:Mn201 b:34.5 occ:0.25 OE2 B:GLU44 3.0 45.5 1.0 OD2 B:ASP46 3.2 44.0 1.0 OE2 B:GLU3 3.3 70.3 1.0 O B:HOH1007 3.3 28.8 1.0 OD2 B:ASP92 3.5 40.5 1.0 OD1 B:ASP46 3.7 43.2 1.0 CG B:ASP46 3.8 40.9 1.0 CD B:GLU3 4.0 68.6 1.0 OE1 B:GLU3 4.0 71.0 1.0 CD B:GLU44 4.2 42.2 1.0 CG B:ASP92 4.5 41.0 1.0 CG2 B:VAL20 4.7 41.0 1.0 OD1 B:ASP92 4.8 41.4 1.0 OE1 B:GLU44 4.9 42.7 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