Sodium in PDB 3x3y: Copper Amine Oxidase From Arthrobacter Globiformis Anaerobically Reduced By Histamine

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

The structure of Copper Amine Oxidase From Arthrobacter Globiformis Anaerobically Reduced By Histamine, PDB code: 3x3y 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)	36.46 / 1.50
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	193.471, 63.247, 157.906, 90.00, 117.73, 90.00
R / Rfree (%)	16.2 / 17.7

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

Potassium	(K)	2 atoms
Copper	(Cu)	2 atoms

The binding sites of Sodium atom in the Copper Amine Oxidase From Arthrobacter Globiformis Anaerobically Reduced By Histamine (pdb code 3x3y). This binding sites where shown within 5.0 Angstroms radius around Sodium atom.
In total 2 binding sites of Sodium where determined in the Copper Amine Oxidase From Arthrobacter Globiformis Anaerobically Reduced By Histamine, PDB code: 3x3y:
Jump to Sodium binding site number: 1; 2;

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


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 1 of Copper Amine Oxidase From Arthrobacter Globiformis Anaerobically Reduced By Histamine within 5.0Å range: probe atom residue distance (Å) B Occ A:Na709 b:7.8 occ:1.00 OD1 A:ASP581 2.4 12.3 1.0 O A:MET441 2.4 9.8 1.0 OD1 A:ASP440 2.4 9.9 1.0 O A:ILE582 2.5 9.3 1.0 O A:HOH808 2.7 10.8 1.0 N A:ILE582 3.2 10.3 1.0 N A:MET441 3.4 8.7 1.0 C A:ILE582 3.5 8.7 1.0 C A:MET441 3.5 8.8 1.0 CG A:ASP581 3.6 14.7 1.0 CG A:ASP440 3.7 11.0 1.0 CD1 A:PHE446 3.8 15.3 1.0 C A:ASP581 3.8 11.6 1.0 NH2 A:ARG49 3.9 13.7 1.0 C A:ASP440 3.9 9.4 1.0 CA A:ILE582 3.9 10.5 1.0 CA A:MET441 4.0 9.1 1.0 CA A:ASP581 4.0 9.8 1.0 CE1 A:PHE446 4.2 18.5 1.0 CA A:ASP440 4.4 6.4 1.0 CB A:ASP581 4.4 11.5 1.0 OD2 A:ASP440 4.5 10.6 1.0 O A:ASP440 4.5 9.8 1.0 OD2 A:ASP581 4.5 16.5 1.0 CB A:MET441 4.5 9.5 1.0 O A:ASP581 4.6 11.6 1.0 N A:VAL583 4.6 7.2 1.0 CB A:ASP440 4.6 8.0 1.0 N A:ALA442 4.7 9.0 1.0 CG2 A:VAL583 4.8 8.6 1.0 CB A:TYR546 4.8 13.4 1.0 CG A:PHE446 4.9 16.6 1.0 O A:PHE446 4.9 14.0 1.0 CG1 A:ILE582 5.0 12.6 1.0

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


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 2 of Copper Amine Oxidase From Arthrobacter Globiformis Anaerobically Reduced By Histamine within 5.0Å range: probe atom residue distance (Å) B Occ B:Na706 b:17.1 occ:1.00 O B:MET441 2.4 16.6 1.0 OD1 B:ASP440 2.4 17.7 1.0 OD1 B:ASP581 2.4 20.4 1.0 O B:ILE582 2.6 15.8 1.0 O B:HOH814 2.7 17.4 1.0 N B:ILE582 3.3 17.4 1.0 N B:MET441 3.4 14.9 1.0 C B:MET441 3.5 15.9 1.0 C B:ILE582 3.5 16.2 1.0 CG B:ASP440 3.7 16.4 1.0 CG B:ASP581 3.7 24.6 1.0 NH2 B:ARG49 3.8 20.8 1.0 CD1 B:PHE446 3.8 21.9 1.0 C B:ASP581 3.9 18.3 1.0 C B:ASP440 3.9 15.6 1.0 CA B:MET441 3.9 14.9 1.0 CA B:ILE582 4.0 16.6 1.0 CA B:ASP581 4.1 19.2 1.0 CE1 B:PHE446 4.3 25.8 1.0 CA B:ASP440 4.4 14.8 1.0 OD2 B:ASP440 4.5 17.1 1.0 CB B:MET441 4.5 14.6 1.0 O B:ASP440 4.5 15.2 1.0 CB B:ASP581 4.5 20.1 1.0 OD2 B:ASP581 4.6 24.3 1.0 CB B:ASP440 4.6 15.5 1.0 N B:ALA442 4.7 15.9 1.0 N B:VAL583 4.7 15.2 1.0 O B:ASP581 4.7 18.5 1.0 CB B:TYR546 4.8 18.9 1.0 CG2 B:VAL583 4.8 16.8 1.0 CG B:PHE446 4.9 24.7 1.0 O B:PHE446 4.9 19.3 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