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Sodium 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
Copper (Cu) 2 atoms

Sodium Binding Sites:

The binding sites of Sodium 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 Sodium atom.
In total 2 binding sites of Sodium where determined in the Copper Amine Oxidase From Arthrobacter Globiformis: Aminoresorcinol Form Produced By Anaerobic Reduction with Ethylamine Hydrochloride, PDB code: 3x3z:
Jump to Sodium binding site number: 1; 2;

Sodium binding site 1 out of 2 in 3x3z

Go back to Sodium Binding Sites List in 3x3z
Sodium 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 Sodium with other atoms in the Na 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:Na1003

b:13.9
occ:1.00
OD1 A:ASP581 2.4 18.0 1.0
OD1 A:ASP440 2.4 14.5 1.0
O A:MET441 2.4 13.6 1.0
O A:ILE582 2.5 12.9 1.0
O A:HOH1146 2.6 15.5 1.0
N A:ILE582 3.2 14.1 1.0
N A:MET441 3.4 12.4 1.0
C A:ILE582 3.5 12.9 1.0
C A:MET441 3.5 13.1 1.0
CG A:ASP581 3.6 21.1 1.0
CG A:ASP440 3.7 13.5 1.0
CD1 A:PHE446 3.8 18.5 1.0
C A:ASP581 3.8 14.8 1.0
NH2 A:ARG49 3.8 17.0 1.0
C A:ASP440 3.9 12.4 1.0
CA A:ILE582 3.9 13.5 1.0
CA A:MET441 4.0 12.4 1.0
CA A:ASP581 4.1 15.4 1.0
CE1 A:PHE446 4.2 24.4 1.0
CA A:ASP440 4.3 12.3 1.0
OD2 A:ASP440 4.4 14.4 1.0
CB A:ASP581 4.4 16.0 1.0
OD2 A:ASP581 4.5 22.0 1.0
O A:ASP440 4.5 12.7 1.0
CB A:MET441 4.5 12.2 1.0
O A:ASP581 4.6 15.1 1.0
N A:VAL583 4.6 12.6 1.0
CB A:ASP440 4.6 12.8 1.0
N A:ALA442 4.7 13.6 1.0
CG2 A:VAL583 4.7 12.9 1.0
CB A:TYR546 4.8 16.9 1.0
CG A:PHE446 4.9 19.4 1.0
O A:PHE446 4.9 16.5 1.0
CG1 A:ILE582 5.0 14.8 1.0

Sodium binding site 2 out of 2 in 3x3z

Go back to Sodium Binding Sites List in 3x3z
Sodium 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 Sodium with other atoms in the Na 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:Na1003

b:9.7
occ:1.00
OD1 B:ASP581 2.4 13.4 1.0
OD1 B:ASP440 2.4 10.0 1.0
O B:MET441 2.4 11.0 1.0
O B:ILE582 2.5 9.3 1.0
O B:HOH1119 2.6 13.0 1.0
N B:ILE582 3.2 10.2 1.0
N B:MET441 3.5 8.6 1.0
C B:ILE582 3.5 9.4 1.0
C B:MET441 3.5 9.4 1.0
CG B:ASP581 3.6 14.9 1.0
CG B:ASP440 3.7 11.4 1.0
CD1 B:PHE446 3.7 15.3 1.0
C B:ASP581 3.8 12.3 1.0
NH2 B:ARG49 3.8 14.0 1.0
CA B:ILE582 3.9 11.4 1.0
C B:ASP440 3.9 9.6 1.0
CA B:MET441 4.0 9.3 1.0
CA B:ASP581 4.0 11.1 1.0
CE1 B:PHE446 4.1 21.4 1.0
CA B:ASP440 4.4 8.2 1.0
CB B:ASP581 4.4 11.8 1.0
OD2 B:ASP440 4.5 11.2 1.0
OD2 B:ASP581 4.5 18.1 1.0
O B:ASP440 4.5 9.5 1.0
CB B:MET441 4.5 9.0 1.0
O B:ASP581 4.6 12.5 1.0
N B:VAL583 4.6 8.7 1.0
CB B:ASP440 4.6 8.4 1.0
N B:ALA442 4.7 10.6 1.0
CG2 B:VAL583 4.7 8.5 1.0
CG B:PHE446 4.8 17.1 1.0
CB B:TYR546 4.8 13.2 1.0
O B:PHE446 4.9 13.8 1.0
CG1 B:ILE582 5.0 13.2 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: Tue Dec 15 06:30:46 2020

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