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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)

Protein crystallography data

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

Other elements in 3lzr:

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

Copper Binding Sites:

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 3lzr

Go back to Copper Binding Sites List in 3lzr
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 3lzr

Go back to Copper Binding Sites List in 3lzr
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

Reference:

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
Page generated: Wed Oct 28 14:24:35 2020
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