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Copper in PDB 3x3z: Copper Amine Oxidase From Arthrobacter Globiformis: Aminoresorcinol Form Produced By Anaerobic Reduction with Ethylamine Hydrochloride

Enzymatic activity of Copper Amine Oxidase From Arthrobacter Globiformis: Aminoresorcinol Form Produced By Anaerobic Reduction with Ethylamine Hydrochloride

All present enzymatic activity of Copper Amine Oxidase From Arthrobacter Globiformis: Aminoresorcinol Form Produced By Anaerobic Reduction with Ethylamine Hydrochloride:
1.4.3.21;

Protein crystallography data

The structure of Copper Amine Oxidase From Arthrobacter Globiformis: Aminoresorcinol Form Produced By Anaerobic Reduction with Ethylamine Hydrochloride, PDB code: 3x3z was solved by T.Okajima, S.Nakanishi, T.Murakawa, M.Kataoka, H.Hayashi, A.Hamaguchi, T.Nakai, Y.Kawano, H.Yamaguchi, K.Tanizawa, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 22.28 / 1.51
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 192.548, 62.729, 157.647, 90.00, 117.62, 90.00
R / Rfree (%) 16.1 / 17.8

Other elements in 3x3z:

The structure of Copper Amine Oxidase From Arthrobacter Globiformis: Aminoresorcinol Form Produced By Anaerobic Reduction with Ethylamine Hydrochloride also contains other interesting chemical elements:

Potassium (K) 2 atoms
Chlorine (Cl) 2 atoms
Sodium (Na) 2 atoms

Copper Binding Sites:

The binding sites of Copper atom in the Copper Amine Oxidase From Arthrobacter Globiformis: Aminoresorcinol Form Produced By Anaerobic Reduction with Ethylamine Hydrochloride (pdb code 3x3z). This binding sites where shown within 5.0 Angstroms radius around Copper atom.
In total 2 binding sites of Copper where determined in the Copper Amine Oxidase From Arthrobacter Globiformis: Aminoresorcinol Form Produced By Anaerobic Reduction with Ethylamine Hydrochloride, PDB code: 3x3z:
Jump to Copper binding site number: 1; 2;

Copper binding site 1 out of 2 in 3x3z

Go back to Copper Binding Sites List in 3x3z
Copper binding site 1 out of 2 in the Copper Amine Oxidase From Arthrobacter Globiformis: Aminoresorcinol Form Produced By Anaerobic Reduction with Ethylamine Hydrochloride


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 1 of Copper Amine Oxidase From Arthrobacter Globiformis: Aminoresorcinol Form Produced By Anaerobic Reduction with Ethylamine Hydrochloride within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu1001

b:11.9
occ:1.00
 ND1 A:HIS592 2.0 11.8 1.0
NE2 A:HIS433 2.0 9.0 1.0
NE2 A:HIS431 2.0 9.7 1.0
O A:HOH1342 2.4 24.6 1.0
CL A:CL1002 2.5 14.7 1.0
CE1 A:HIS592 3.0 14.4 1.0
CD2 A:HIS433 3.0 11.8 1.0
CE1 A:HIS431 3.0 10.6 1.0
CE1 A:HIS433 3.0 10.3 1.0
CG A:HIS592 3.0 10.5 1.0
CD2 A:HIS431 3.0 9.5 1.0
CB A:HIS592 3.4 10.5 1.0
NE2 A:HIS592 4.1 11.1 1.0
ND1 A:HIS431 4.1 10.2 1.0
ND1 A:HIS433 4.1 10.6 1.0
CD2 A:HIS592 4.1 10.9 1.0
CG A:HIS433 4.1 9.6 1.0
O A:HOH1805 4.1 48.8 1.0
CG A:HIS431 4.1 9.6 1.0
O A:HOH1609 4.3 38.1 1.0
O A:HOH1110 4.4 12.2 1.0
O A:HOH1160 4.5 16.0 1.0
OZ A:TYQ382 4.8 16.4 1.0
CA A:HIS592 4.9 9.8 1.0

Copper binding site 2 out of 2 in 3x3z

Go back to Copper Binding Sites List in 3x3z
Copper binding site 2 out of 2 in the Copper Amine Oxidase From Arthrobacter Globiformis: Aminoresorcinol Form Produced By Anaerobic Reduction with Ethylamine Hydrochloride


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 2 of Copper Amine Oxidase From Arthrobacter Globiformis: Aminoresorcinol Form Produced By Anaerobic Reduction with Ethylamine Hydrochloride within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cu1001

b:11.3
occ:1.00
 CL B:CL1002 1.9 57.2 0.4
NE2 B:HIS433 2.0 8.2 1.0
ND1 B:HIS592 2.0 11.7 1.0
NE2 B:HIS431 2.0 7.7 1.0
O B:HOH1888 2.3 29.6 1.0
OH B:TYQ382 2.6 7.6 0.6
CD2 B:HIS433 3.0 10.1 1.0
CE1 B:HIS592 3.0 13.6 1.0
CE1 B:HIS431 3.0 7.7 1.0
CG B:HIS592 3.0 9.6 1.0
CE1 B:HIS433 3.0 10.2 1.0
CD2 B:HIS431 3.0 8.3 1.0
CB B:HIS592 3.3 11.2 1.0
CZ B:TYQ382 3.4 18.3 0.6
O B:HOH1725 3.5 36.2 1.0
N5 B:TYQ382 3.8 24.4 0.6
CE2 B:TYQ382 4.0 20.5 0.6
NE2 B:HIS592 4.1 11.9 1.0
ND1 B:HIS431 4.1 9.2 1.0
ND1 B:HIS433 4.1 10.2 1.0
CD2 B:HIS592 4.1 10.2 1.0
CG B:HIS433 4.1 7.3 1.0
CG B:HIS431 4.1 7.3 1.0
CE1 B:TYQ382 4.3 16.3 0.6
O B:HOH1132 4.4 11.8 1.0
CA B:HIS592 4.8 9.9 1.0
OZ B:TYQ382 4.9 9.8 0.4
SD B:MET602 5.0 28.5 1.0

Reference:

T.Murakawa, A.Hamaguchi, S.Nakanishi, M.Kataoka, T.Nakai, Y.Kawano, H.Yamaguchi, H.Hayashi, K.Tanizawa, T.Okajima. Probing the Catalytic Mechanism of Copper Amine Oxidase From Arthrobacter Globiformis with Halide Ions J.Biol.Chem. 2015.
ISSN: ESSN 1083-351X
DOI: 10.1074/JBC.M115.662726
Page generated: Mon Jul 14 03:18:20 2025

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