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Copper in PDB 5zp0: Copper Amine Oxidase From Arthrobacter Globiformis Anaerobically Reduced By Ethylamine at pH 8 at 288 K (2)

Enzymatic activity of Copper Amine Oxidase From Arthrobacter Globiformis Anaerobically Reduced By Ethylamine at pH 8 at 288 K (2)

All present enzymatic activity of Copper Amine Oxidase From Arthrobacter Globiformis Anaerobically Reduced By Ethylamine at pH 8 at 288 K (2):
1.4.3.21;

Protein crystallography data

The structure of Copper Amine Oxidase From Arthrobacter Globiformis Anaerobically Reduced By Ethylamine at pH 8 at 288 K (2), PDB code: 5zp0 was solved by T.Murakawa, S.Baba, Y.Kawano, H.Hayashi, T.Yano, K.Tanizawa, T.Kumasaka, M.Yamamoto, T.Okajima, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 39.68 / 1.74
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 193.986, 65.077, 158.957, 90.00, 117.18, 90.00
R / Rfree (%) 15 / 17.7

Other elements in 5zp0:

The structure of Copper Amine Oxidase From Arthrobacter Globiformis Anaerobically Reduced By Ethylamine at pH 8 at 288 K (2) also contains other interesting chemical elements:

Sodium (Na) 3 atoms

Copper Binding Sites:

The binding sites of Copper atom in the Copper Amine Oxidase From Arthrobacter Globiformis Anaerobically Reduced By Ethylamine at pH 8 at 288 K (2) (pdb code 5zp0). 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 Ethylamine at pH 8 at 288 K (2), PDB code: 5zp0:
Jump to Copper binding site number: 1; 2;

Copper binding site 1 out of 2 in 5zp0

Go back to Copper Binding Sites List in 5zp0
Copper binding site 1 out of 2 in the Copper Amine Oxidase From Arthrobacter Globiformis Anaerobically Reduced By Ethylamine at pH 8 at 288 K (2)


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 Ethylamine at pH 8 at 288 K (2) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu701

b:16.3
occ:1.00
 O A:HOH988 1.9 24.6 0.8
NE2 A:HIS431 2.0 11.7 1.0
O A:HOH935 2.0 15.6 0.5
NE2 A:HIS433 2.0 13.7 1.0
ND1 A:HIS592 2.1 18.8 1.0
OH A:TYQ382 2.8 25.4 0.7
CE1 A:HIS431 2.9 14.5 1.0
CD2 A:HIS431 3.0 11.4 1.0
CD2 A:HIS433 3.0 12.1 1.0
CE1 A:HIS433 3.0 16.4 1.0
CE1 A:HIS592 3.0 16.8 1.0
CG A:HIS592 3.1 17.0 1.0
CB A:HIS592 3.4 13.4 1.0
CZ A:TYQ382 3.5 32.3 0.7
O A:HOH1300 3.8 33.0 0.7
ND1 A:HIS431 4.0 12.2 1.0
CG A:HIS431 4.1 11.0 1.0
N5 A:TYQ382 4.1 47.8 0.7
CE2 A:TYQ382 4.1 39.4 0.7
ND1 A:HIS433 4.1 11.3 1.0
CG A:HIS433 4.2 10.7 1.0
NE2 A:HIS592 4.2 15.6 1.0
CD2 A:HIS592 4.2 15.7 1.0
CE1 A:TYQ382 4.3 33.6 0.7
O A:HOH808 4.3 15.6 1.0
OZ A:TYQ382 4.5 32.0 0.3
SD A:MET602 4.9 21.4 0.8
CA A:HIS592 4.9 15.7 1.0
CE A:MET602 5.0 21.4 0.8

Copper binding site 2 out of 2 in 5zp0

Go back to Copper Binding Sites List in 5zp0
Copper binding site 2 out of 2 in the Copper Amine Oxidase From Arthrobacter Globiformis Anaerobically Reduced By Ethylamine at pH 8 at 288 K (2)


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 Ethylamine at pH 8 at 288 K (2) within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cu701

b:18.1
occ:1.00
 O B:HOH1284 1.9 16.6 0.3
CE1 B:HIS431 2.0 10.6 1.0
O B:HOH805 2.0 18.7 0.5
ND1 B:HIS592 2.0 17.9 1.0
NE2 B:HIS433 2.1 15.1 1.0
OH B:TYQ382 2.6 23.7 0.9
NE2 B:HIS431 2.9 17.2 1.0
CE1 B:HIS592 3.0 20.2 1.0
CE1 B:HIS433 3.0 16.8 1.0
ND1 B:HIS431 3.0 16.2 1.0
CG B:HIS592 3.1 15.8 1.0
CD2 B:HIS433 3.1 12.6 1.0
CZ B:TYQ382 3.3 23.4 0.9
CB B:HIS592 3.4 12.8 1.0
O B:HOH1230 3.6 47.2 1.0
N5 B:TYQ382 3.7 44.2 0.9
CE2 B:TYQ382 3.8 34.7 0.9
CD2 B:HIS431 4.1 11.2 1.0
OZ B:TYQ382 4.1 27.9 0.1
NE2 B:HIS592 4.1 19.0 1.0
ND1 B:HIS433 4.1 13.7 1.0
CG B:HIS431 4.2 12.0 1.0
CD2 B:HIS592 4.2 15.9 1.0
CG B:HIS433 4.2 12.7 1.0
CE1 B:TYQ382 4.2 26.1 0.9
O B:HOH811 4.3 16.1 1.0
CA B:HIS592 4.9 11.7 1.0
SD B:MET602 5.0 26.2 1.0

Reference:

T.Murakawa, S.Baba, Y.Kawano, H.Hayashi, T.Yano, T.Kumasaka, M.Yamamoto, K.Tanizawa, T.Okajima. In Crystallothermodynamic Analysis of Conformational Change of the Topaquinone Cofactor in Bacterial Copper Amine Oxidase. Proc. Natl. Acad. Sci. V. 116 135 2019U.S.A..
ISSN: ESSN 1091-6490
PubMed: 30563857
DOI: 10.1073/PNAS.1811837116
Page generated: Mon Jul 14 05:48:27 2025

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