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Copper in PDB 3lzp: Crystal Structure Analysis of the 'As-Isolated' P19 Protein From Campylobacter Jejuni at 1.65 A at pH 9.0

Protein crystallography data

The structure of Crystal Structure Analysis of the 'As-Isolated' P19 Protein From Campylobacter Jejuni at 1.65 A at pH 9.0, PDB code: 3lzp 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) 18.80 / 1.65
Space group P 21 21 2
Cell size a, b, c (Å), α, β, γ (°) 53.706, 72.533, 75.185, 90.00, 90.00, 90.00
R / Rfree (%) 15.7 / 19.5

Copper Binding Sites:

The binding sites of Copper atom in the Crystal Structure Analysis of the 'As-Isolated' P19 Protein From Campylobacter Jejuni at 1.65 A at pH 9.0 (pdb code 3lzp). 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 'As-Isolated' P19 Protein From Campylobacter Jejuni at 1.65 A at pH 9.0, PDB code: 3lzp:
Jump to Copper binding site number: 1; 2;

Copper binding site 1 out of 2 in 3lzp

Go back to Copper Binding Sites List in 3lzp
Copper binding site 1 out of 2 in the Crystal Structure Analysis of the 'As-Isolated' P19 Protein From Campylobacter Jejuni at 1.65 A at pH 9.0


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 'As-Isolated' P19 Protein From Campylobacter Jejuni at 1.65 A at pH 9.0 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu200

b:21.4
occ:1.00
NE2 A:HIS42 2.0 13.7 1.0
NE2 A:HIS95 2.0 21.3 1.0
NE2 B:HIS132 2.1 15.7 1.0
SD A:MET88 2.3 21.8 1.0
CE1 A:HIS95 2.9 23.1 1.0
CE1 A:HIS42 2.9 18.5 1.0
CD2 A:HIS42 3.0 23.1 1.0
CE1 B:HIS132 3.0 21.3 1.0
CD2 A:HIS95 3.1 19.5 1.0
CD2 B:HIS132 3.2 18.6 1.0
CG A:MET88 3.3 18.3 1.0
CE A:MET88 3.5 21.6 1.0
OE2 A:GLU44 3.7 31.9 1.0
ND1 A:HIS42 4.0 16.5 1.0
CG A:HIS42 4.1 15.7 1.0
ND1 A:HIS95 4.1 25.9 1.0
ND1 B:HIS132 4.2 21.5 1.0
CG A:HIS95 4.2 20.4 1.0
CG B:HIS132 4.3 17.6 1.0
CA A:GLY97 4.3 15.5 1.0
CD A:GLU44 4.5 30.0 1.0
CB A:MET88 4.6 16.9 1.0
CG A:GLU44 4.7 31.1 1.0
N A:GLY97 4.9 18.5 1.0
C A:GLY97 4.9 16.8 1.0

Copper binding site 2 out of 2 in 3lzp

Go back to Copper Binding Sites List in 3lzp
Copper binding site 2 out of 2 in the Crystal Structure Analysis of the 'As-Isolated' P19 Protein From Campylobacter Jejuni at 1.65 A at pH 9.0


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 'As-Isolated' P19 Protein From Campylobacter Jejuni at 1.65 A at pH 9.0 within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cu200

b:20.3
occ:1.00
NE2 B:HIS42 2.0 21.4 1.0
NE2 B:HIS95 2.1 18.9 1.0
NE2 A:HIS132 2.1 18.4 1.0
SD B:MET88 2.3 21.5 1.0
CE1 B:HIS95 2.9 23.1 1.0
CE1 A:HIS132 3.0 19.3 1.0
CE1 B:HIS42 3.0 20.0 1.0
CD2 B:HIS42 3.0 20.2 1.0
CG B:MET88 3.1 19.4 1.0
CD2 B:HIS95 3.2 18.4 1.0
CD2 A:HIS132 3.3 20.4 1.0
CE B:MET88 3.5 18.7 1.0
ND1 B:HIS42 4.1 18.6 1.0
OE2 B:GLU44 4.1 24.8 1.0
ND1 B:HIS95 4.1 22.4 1.0
CG B:HIS42 4.1 19.0 1.0
ND1 A:HIS132 4.1 20.3 1.0
CA B:GLY97 4.2 15.6 1.0
CG B:HIS95 4.3 15.6 1.0
CG A:HIS132 4.3 19.0 1.0
CG1 B:ILE25 4.4 21.2 1.0
CD1 B:ILE25 4.4 20.4 1.0
CB B:MET88 4.6 20.2 1.0
CG B:GLU44 4.7 19.0 1.0
N B:GLY97 4.7 17.0 1.0
CD B:GLU44 4.8 23.3 1.0
C B:GLY97 4.8 12.1 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: Fri Sep 4 08:08:25 2020
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