Atomistry » Sodium » PDB 3wxt-3zu5 » 3x3z
Atomistry »
  Sodium »
    PDB 3wxt-3zu5 »
      3x3z »

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

Last articles

Zn in 8WB0
Zn in 8WAX
Zn in 8WAU
Zn in 8WAZ
Zn in 8WAY
Zn in 8WAV
Zn in 8WAW
Zn in 8WAT
Zn in 8W7M
Zn in 8WD3
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy