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Copper in PDB 3zx1: Multicopper Oxidase From Campylobacter Jejuni: A Metallo-Oxidase

Protein crystallography data

The structure of Multicopper Oxidase From Campylobacter Jejuni: A Metallo-Oxidase, PDB code: 3zx1 was solved by C.S.Silva, P.Durao, A.Fillat, P.F.Lindley, L.O.Martins, I.Bento, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 49.51 / 1.95
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 48.810, 94.860, 50.380, 90.00, 100.63, 90.00
R / Rfree (%) 16.02 / 20.714

Copper Binding Sites:

The binding sites of Copper atom in the Multicopper Oxidase From Campylobacter Jejuni: A Metallo-Oxidase (pdb code 3zx1). This binding sites where shown within 5.0 Angstroms radius around Copper atom.
In total 4 binding sites of Copper where determined in the Multicopper Oxidase From Campylobacter Jejuni: A Metallo-Oxidase, PDB code: 3zx1:
Jump to Copper binding site number: 1; 2; 3; 4;

Copper binding site 1 out of 4 in 3zx1

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Copper binding site 1 out of 4 in the Multicopper Oxidase From Campylobacter Jejuni: A Metallo-Oxidase


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 1 of Multicopper Oxidase From Campylobacter Jejuni: A Metallo-Oxidase within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu601

b:20.5
occ:1.00
ND1 A:HIS500 2.0 20.0 1.0
ND1 A:HIS439 2.0 20.2 1.0
SG A:CYS495 2.3 18.2 1.0
CE1 A:HIS439 2.9 20.8 1.0
CG A:HIS500 3.0 18.3 1.0
CE1 A:HIS500 3.0 21.0 1.0
CG A:HIS439 3.1 19.7 1.0
CB A:CYS495 3.3 17.7 1.0
CB A:HIS500 3.3 18.7 1.0
SD A:MET505 3.4 22.8 1.0
CB A:HIS439 3.4 15.7 1.0
CD1 A:ILE497 3.8 14.2 1.0
CB A:ILE497 4.0 17.8 1.0
NE2 A:HIS439 4.1 20.5 1.0
NE2 A:HIS500 4.1 21.4 1.0
CA A:HIS439 4.1 16.3 1.0
CD2 A:HIS500 4.1 18.9 1.0
CD2 A:HIS439 4.1 16.7 1.0
CE A:MET505 4.4 24.4 1.0
CG1 A:ILE497 4.4 15.5 1.0
O A:ASP438 4.6 19.4 1.0
CA A:CYS495 4.7 17.6 1.0
CD A:PRO440 4.7 15.9 1.0
CG2 A:ILE497 4.7 18.0 1.0
N A:ILE497 4.8 17.6 1.0
CA A:HIS500 4.8 19.8 1.0
CG A:MET505 4.9 21.8 1.0
CA A:ILE497 4.9 17.1 1.0
O A:ILE497 5.0 19.4 1.0
CD1 A:PHE405 5.0 25.2 1.0

Copper binding site 2 out of 4 in 3zx1

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Copper binding site 2 out of 4 in the Multicopper Oxidase From Campylobacter Jejuni: A Metallo-Oxidase


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 2 of Multicopper Oxidase From Campylobacter Jejuni: A Metallo-Oxidase within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu602

b:20.4
occ:0.60
ND1 A:HIS141 2.0 14.4 1.0
NE2 A:HIS180 2.0 14.2 1.0
NE2 A:HIS496 2.2 23.2 1.0
O1 A:OXY605 2.2 15.8 0.6
CE1 A:HIS180 2.5 17.9 1.0
CE1 A:HIS141 2.6 13.2 1.0
O2 A:OXY605 2.6 19.5 0.6
CE1 A:HIS496 3.1 21.2 1.0
CG A:HIS141 3.2 14.8 1.0
CD2 A:HIS496 3.2 22.2 1.0
CD2 A:HIS180 3.3 15.3 1.0
CU A:CU604 3.6 22.3 0.2
CD2 A:HIS139 3.8 25.3 1.0
CB A:HIS141 3.8 12.9 1.0
ND1 A:HIS180 3.8 17.7 1.0
NE2 A:HIS141 3.9 15.8 1.0
CD2 A:HIS141 4.1 12.3 1.0
CG A:HIS180 4.2 12.8 1.0
ND1 A:HIS496 4.2 19.3 1.0
CG A:HIS496 4.3 19.0 1.0
CD2 A:HIS442 4.3 16.3 1.0
NE2 A:HIS442 4.3 23.7 1.0
CZ2 A:TRP178 4.3 14.2 1.0
NE2 A:HIS139 4.4 27.9 1.0
CU A:CU603 4.4 25.1 0.3
CE2 A:TRP178 4.7 10.8 1.0
NE1 A:TRP178 4.8 13.8 1.0
CA A:HIS141 4.8 15.0 1.0
CG A:HIS139 4.9 22.7 1.0
CD2 A:HIS182 5.0 28.5 0.6

Copper binding site 3 out of 4 in 3zx1

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Copper binding site 3 out of 4 in the Multicopper Oxidase From Campylobacter Jejuni: A Metallo-Oxidase


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 3 of Multicopper Oxidase From Campylobacter Jejuni: A Metallo-Oxidase within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu603

b:25.1
occ:0.30
NE2 A:HIS444 2.0 26.3 1.0
NE2 A:HIS494 2.0 19.5 1.0
NE2 A:HIS182 2.0 27.9 0.4
NE2 A:HIS182 2.0 30.4 0.6
O2 A:OXY605 2.1 19.5 0.6
O1 A:OXY605 2.3 15.8 0.6
CD2 A:HIS182 2.4 26.6 0.4
CE1 A:HIS444 2.5 27.8 1.0
CD2 A:HIS182 2.6 28.5 0.6
CE1 A:HIS494 2.6 19.6 1.0
CE1 A:HIS182 3.0 31.6 0.6
CD2 A:HIS494 3.2 19.9 1.0
CD2 A:HIS444 3.2 25.6 1.0
CE1 A:HIS182 3.2 27.8 0.4
CU A:CU604 3.6 22.3 0.2
CG A:HIS182 3.6 26.8 0.6
CG A:HIS182 3.6 25.4 0.4
ND1 A:HIS182 3.7 30.7 0.6
ND1 A:HIS444 3.8 29.4 1.0
ND1 A:HIS494 3.8 19.3 1.0
CD2 A:HIS442 3.9 16.3 1.0
ND1 A:HIS182 4.0 26.7 0.4
CG A:HIS494 4.1 19.1 1.0
CG A:HIS444 4.1 24.6 1.0
CD2 A:HIS139 4.3 25.3 1.0
CU A:CU602 4.4 20.4 0.6
NE2 A:HIS139 4.5 27.9 1.0
NE2 A:HIS442 4.5 23.7 1.0
OE1 A:GLU501 4.5 29.3 1.0
NE2 A:HIS496 4.7 23.2 1.0
CD2 A:HIS496 4.7 22.2 1.0
CB A:HIS182 4.9 25.0 1.0
CG A:HIS139 4.9 22.7 1.0
CD A:GLU501 5.0 29.1 1.0

Copper binding site 4 out of 4 in 3zx1

Go back to Copper Binding Sites List in 3zx1
Copper binding site 4 out of 4 in the Multicopper Oxidase From Campylobacter Jejuni: A Metallo-Oxidase


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 4 of Multicopper Oxidase From Campylobacter Jejuni: A Metallo-Oxidase within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu604

b:22.3
occ:0.20
NE2 A:HIS442 1.9 23.7 1.0
NE2 A:HIS139 1.9 27.9 1.0
O1 A:OXY605 2.5 15.8 0.6
CD2 A:HIS139 2.6 25.3 1.0
CD2 A:HIS442 2.7 16.3 1.0
CE1 A:HIS139 3.0 26.5 1.0
CE1 A:HIS442 3.1 18.2 1.0
NE2 A:HIS444 3.1 26.3 1.0
O A:HOH2092 3.2 29.9 1.0
CD2 A:HIS444 3.2 25.6 1.0
CE1 A:HIS444 3.5 27.8 1.0
O2 A:OXY605 3.5 19.5 0.6
CU A:CU603 3.6 25.1 0.3
CU A:CU602 3.6 20.4 0.6
ND1 A:HIS141 3.6 14.4 1.0
CG A:HIS444 3.7 24.6 1.0
CG A:HIS139 3.8 22.7 1.0
ND1 A:HIS444 3.8 29.4 1.0
CG A:HIS442 3.9 17.0 1.0
CE1 A:HIS141 3.9 13.2 1.0
CG A:HIS141 3.9 14.8 1.0
ND1 A:HIS139 3.9 27.6 1.0
ND1 A:HIS442 4.0 15.9 1.0
CA A:HIS141 4.2 15.0 1.0
NE2 A:HIS141 4.4 15.8 1.0
CD2 A:HIS141 4.4 12.3 1.0
CB A:HIS141 4.4 12.9 1.0
N A:GLY142 4.5 14.2 1.0
CA A:HIS444 4.5 22.6 1.0
CB A:HIS444 4.6 23.7 1.0
NE2 A:HIS494 4.6 19.5 1.0
C A:HIS141 4.9 14.7 1.0
NE2 A:HIS496 4.9 23.2 1.0
N A:HIS444 4.9 22.2 1.0
CD2 A:HIS182 5.0 26.6 0.4

Reference:

C.S.Silva, P.Durao, A.Fillat, P.F.Lindley, L.O.Martins, I.Bento. Crystal Structure of the Multicopper Oxidase From the Pathogenic Bacterium Campylobacter Jejuni CGUG11284: Characterization of A Metallo-Oxidase. Metallomics V. 4 37 2012.
ISSN: ISSN 1756-5901
PubMed: 22127520
DOI: 10.1039/C1MT00156F
Page generated: Sun Dec 13 11:13:10 2020

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