Copper in PDB 3x3x: Copper Amine Oxidase From Arthrobacter Globiformis Anaerobically Reduced By Phenylethylamine

All present enzymatic activity of Copper Amine Oxidase From Arthrobacter Globiformis Anaerobically Reduced By Phenylethylamine:
1.4.3.21;

The structure of Copper Amine Oxidase From Arthrobacter Globiformis Anaerobically Reduced By Phenylethylamine, PDB code: 3x3x 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)	20.41 / 1.57
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	191.658, 62.890, 158.006, 90.00, 117.48, 90.00
R / Rfree (%)	21.5 / 24.3

The structure of Copper Amine Oxidase From Arthrobacter Globiformis Anaerobically Reduced By Phenylethylamine also contains other interesting chemical elements:

Sodium

(Na)

3 atoms

The binding sites of Copper atom in the Copper Amine Oxidase From Arthrobacter Globiformis Anaerobically Reduced By Phenylethylamine (pdb code 3x3x). 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 Anaerobically Reduced By Phenylethylamine, PDB code: 3x3x:
Jump to Copper binding site number: 1; 2;

Copper binding site 1 out of 2 in the Copper Amine Oxidase From Arthrobacter Globiformis Anaerobically Reduced By Phenylethylamine


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 Anaerobically Reduced By Phenylethylamine within 5.0Å range: probe atom residue distance (Å) B Occ A:Cu701 b:13.8 occ:1.00 NE2 A:HIS433 1.9 15.0 1.0 NE2 A:HIS431 2.0 13.8 1.0 ND1 A:HIS592 2.1 13.4 1.0 OH A:TYQ382 2.8 17.1 1.0 CD2 A:HIS433 2.9 14.8 1.0 CE1 A:HIS433 2.9 14.9 1.0 CD2 A:HIS431 3.0 12.0 1.0 CE1 A:HIS431 3.0 12.4 1.0 CG A:HIS592 3.0 13.4 1.0 CE1 A:HIS592 3.1 15.8 1.0 CB A:HIS592 3.3 13.4 1.0 CZ A:TYQ382 3.6 17.5 1.0 ND1 A:HIS433 4.0 17.1 1.0 CG A:HIS433 4.1 13.8 1.0 ND1 A:HIS431 4.1 11.9 1.0 CG A:HIS431 4.1 13.3 1.0 CD2 A:HIS592 4.2 13.8 1.0 NE2 A:HIS592 4.2 16.0 1.0 N5 A:TYQ382 4.3 26.0 1.0 CE2 A:TYQ382 4.3 24.1 1.0 CE1 A:TYQ382 4.4 19.3 1.0 O A:HOH835 4.6 13.7 1.0 CA A:HIS592 4.8 14.0 1.0 SD A:MET602 4.9 22.0 1.0

Copper binding site 2 out of 2 in the Copper Amine Oxidase From Arthrobacter Globiformis Anaerobically Reduced By Phenylethylamine


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 Anaerobically Reduced By Phenylethylamine within 5.0Å range: probe atom residue distance (Å) B Occ B:Cu701 b:13.4 occ:1.00 NE2 B:HIS433 2.0 9.9 1.0 ND1 B:HIS592 2.1 10.5 1.0 NE2 B:HIS431 2.1 11.7 1.0 CD2 B:HIS433 2.9 12.7 1.0 OH B:TYQ382 2.9 15.9 1.0 CE1 B:HIS433 3.0 14.3 1.0 CG B:HIS592 3.0 17.5 1.0 CE1 B:HIS431 3.0 11.7 1.0 CD2 B:HIS431 3.0 6.9 1.0 CE1 B:HIS592 3.1 14.2 1.0 CB B:HIS592 3.3 14.0 1.0 O B:HOH1377 3.4 26.8 1.0 CZ B:TYQ382 3.7 17.2 1.0 ND1 B:HIS433 4.1 16.1 1.0 CG B:HIS433 4.1 10.5 1.0 ND1 B:HIS431 4.1 11.1 1.0 CG B:HIS431 4.2 8.9 1.0 CD2 B:HIS592 4.2 16.9 1.0 NE2 B:HIS592 4.2 13.4 1.0 N5 B:TYQ382 4.3 24.4 1.0 CE2 B:TYQ382 4.4 18.8 1.0 CE1 B:TYQ382 4.5 15.9 1.0 O B:HOH829 4.6 14.1 1.0 CA B:HIS592 4.8 10.6 1.0

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