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Potassium 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:

Chlorine (Cl) 2 atoms
Copper (Cu) 2 atoms
Sodium (Na) 2 atoms

Potassium Binding Sites:

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

Potassium binding site 1 out of 2 in 3x3z

Go back to Potassium Binding Sites List in 3x3z
Potassium 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 Potassium with other atoms in the K 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:K1004

b:28.5
occ:1.00
 O A:HOH1425 2.7 27.9 1.0
OG A:SER562 2.9 30.5 1.0
O A:ALA93 3.0 23.0 1.0
O A:ALA94 3.0 21.2 1.0
NH1 A:ARG148 3.2 30.6 0.5
C A:ALA94 3.7 20.1 1.0
CA A:ALA94 3.8 19.2 1.0
CB A:SER562 3.9 24.8 1.0
C A:ALA93 4.0 21.0 1.0
O A:HOH1421 4.4 20.8 1.0
N A:ALA94 4.4 19.6 1.0
CZ A:ARG148 4.5 29.5 0.5
N A:SER562 4.5 19.6 1.0
CA A:SER562 4.9 22.0 1.0
CE1 A:HIS561 4.9 22.8 1.0
N A:THR95 4.9 17.8 1.0

Potassium binding site 2 out of 2 in 3x3z

Go back to Potassium Binding Sites List in 3x3z
Potassium 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 Potassium with other atoms in the K 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:K1004

b:17.4
occ:1.00
 O B:VAL79 2.6 15.1 1.0
O B:HOH1298 2.8 20.1 1.0
O B:THR80 2.8 19.1 1.0
C B:THR80 3.5 17.9 1.0
C B:VAL79 3.8 15.3 1.0
N B:GLY82 3.9 16.7 1.0
CA B:THR80 4.1 19.3 1.0
CA B:GLY82 4.2 15.7 1.0
N B:ASN81 4.3 17.0 1.0
OE1 B:GLU22 4.3 20.5 1.0
C B:ASN81 4.4 17.2 1.0
O B:HOH1353 4.4 25.1 1.0
N B:THR80 4.4 16.2 1.0
CG B:GLU22 4.6 15.5 1.0
CA B:ASN81 4.7 17.5 1.0
CD B:GLU22 4.8 20.2 1.0
CA B:VAL79 4.9 13.8 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 Aug 12 09:54:12 2024

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