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Copper in PDB 3lzo: Crystal Structure Analysis of the Copper-Reconstituted P19 Protein From Campylobacter Jejuni at 1.65 A at pH 10.0

Protein crystallography data

The structure of Crystal Structure Analysis of the Copper-Reconstituted P19 Protein From Campylobacter Jejuni at 1.65 A at pH 10.0, PDB code: 3lzo 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) 19.34 / 1.65
Space group P 21 21 2
Cell size a, b, c (Å), α, β, γ (°) 55.831, 72.581, 78.817, 90.00, 90.00, 90.00
R / Rfree (%) 13.9 / 18.7

Copper Binding Sites:

The binding sites of Copper atom in the Crystal Structure Analysis of the Copper-Reconstituted P19 Protein From Campylobacter Jejuni at 1.65 A at pH 10.0 (pdb code 3lzo). 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 the Copper-Reconstituted P19 Protein From Campylobacter Jejuni at 1.65 A at pH 10.0, PDB code: 3lzo:
Jump to Copper binding site number: 1; 2;

Copper binding site 1 out of 2 in 3lzo

Go back to Copper Binding Sites List in 3lzo
Copper binding site 1 out of 2 in the Crystal Structure Analysis of the Copper-Reconstituted P19 Protein From Campylobacter Jejuni at 1.65 A at pH 10.0


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 the Copper-Reconstituted P19 Protein From Campylobacter Jejuni at 1.65 A at pH 10.0 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu200

b:26.3
occ:1.00
NE2 A:HIS42 2.0 20.8 1.0
NE2 A:HIS95 2.0 18.7 1.0
NE2 B:HIS132 2.1 24.2 1.0
OE1 A:GLU44 2.3 24.5 0.7
SD A:MET88 2.7 22.9 1.0
OE2 A:GLU44 2.8 34.5 0.7
CD A:GLU44 2.9 26.4 0.7
CD2 A:HIS42 2.9 18.4 1.0
CE1 B:HIS132 2.9 22.4 1.0
CE1 A:HIS42 3.0 25.4 1.0
CD2 A:HIS95 3.0 20.2 1.0
CE1 A:HIS95 3.0 27.3 1.0
OE2 A:GLU44 3.1 13.1 0.3
CD2 B:HIS132 3.2 26.5 1.0
CD A:GLU44 3.7 15.5 0.3
CG A:GLU44 3.7 15.8 0.3
CG A:MET88 3.8 22.2 1.0
ND1 A:HIS42 4.1 21.8 1.0
CG A:HIS42 4.1 21.1 1.0
ND1 A:HIS95 4.1 24.2 1.0
CG A:HIS95 4.1 21.7 1.0
ND1 B:HIS132 4.1 22.4 1.0
CE A:MET88 4.2 21.7 1.0
CA A:GLY97 4.3 17.9 1.0
CG B:HIS132 4.3 23.5 1.0
CG A:GLU44 4.4 22.7 0.7
OE1 A:GLU44 4.7 18.5 0.3
N A:GLY97 4.8 18.2 1.0
CB A:GLU44 4.9 18.9 0.3
SD A:MET27 5.0 28.0 1.0

Copper binding site 2 out of 2 in 3lzo

Go back to Copper Binding Sites List in 3lzo
Copper binding site 2 out of 2 in the Crystal Structure Analysis of the Copper-Reconstituted P19 Protein From Campylobacter Jejuni at 1.65 A at pH 10.0


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 the Copper-Reconstituted P19 Protein From Campylobacter Jejuni at 1.65 A at pH 10.0 within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cu200

b:25.6
occ:1.00
NE2 B:HIS42 2.0 24.1 1.0
NE2 B:HIS95 2.0 20.2 1.0
NE2 A:HIS132 2.1 19.0 1.0
OE1 B:GLU44 2.2 35.2 1.0
SD B:MET88 2.8 23.5 1.0
CD B:GLU44 2.9 31.6 1.0
OE2 B:GLU44 2.9 25.4 1.0
CD2 B:HIS42 2.9 26.6 1.0
CD2 B:HIS95 3.0 21.7 1.0
CE1 A:HIS132 3.0 24.5 1.0
CE1 B:HIS95 3.0 25.8 1.0
CE1 B:HIS42 3.0 22.9 1.0
CD2 A:HIS132 3.1 20.6 1.0
CG B:MET88 3.8 19.5 1.0
CG B:HIS42 4.1 21.4 1.0
ND1 B:HIS95 4.1 22.4 1.0
ND1 B:HIS42 4.1 24.3 1.0
CE B:MET88 4.1 22.4 1.0
CG B:HIS95 4.1 22.9 1.0
ND1 A:HIS132 4.2 20.5 1.0
CG A:HIS132 4.3 22.5 1.0
CG B:GLU44 4.3 30.5 1.0
CA B:GLY97 4.5 21.2 1.0
O B:HOH1135 4.9 34.9 1.0
N B:GLY97 5.0 19.0 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: Sun Dec 13 11:10:32 2020

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