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Copper in PDB 5zoz: Copper Amine Oxidase From Arthrobacter Globiformis Anaerobically Reduced By Ethylamine at pH 8 at 288 K (1)

Enzymatic activity of Copper Amine Oxidase From Arthrobacter Globiformis Anaerobically Reduced By Ethylamine at pH 8 at 288 K (1)

All present enzymatic activity of Copper Amine Oxidase From Arthrobacter Globiformis Anaerobically Reduced By Ethylamine at pH 8 at 288 K (1):
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 (1), PDB code: 5zoz 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) 39.70 / 1.70
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 193.824, 65.018, 159.011, 90.00, 117.14, 90.00
R / Rfree (%) 14.9 / 16.9

Other elements in 5zoz:

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

Copper binding site 1 out of 2 in 5zoz

Go back to Copper Binding Sites List in 5zoz
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 (1)


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 (1) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu701

b:15.5
occ:1.00
 O A:HOH864 1.8 20.9 0.6
NE2 A:HIS431 2.0 11.4 1.0
NE2 A:HIS433 2.0 12.9 1.0
O A:HOH803 2.1 22.3 0.7
ND1 A:HIS592 2.1 16.7 1.0
OH A:TYQ382 2.6 23.3 0.8
CE1 A:HIS431 2.9 13.0 1.0
CD2 A:HIS431 3.0 11.3 1.0
CE1 A:HIS433 3.0 16.2 1.0
CD2 A:HIS433 3.0 13.7 1.0
CE1 A:HIS592 3.1 18.3 1.0
CG A:HIS592 3.1 16.2 1.0
CZ A:TYQ382 3.3 26.7 0.8
CB A:HIS592 3.4 11.7 1.0
O A:HOH1233 3.6 58.7 1.0
N5 A:TYQ382 3.7 41.5 0.8
CE2 A:TYQ382 3.8 35.2 0.8
ND1 A:HIS431 4.0 11.7 1.0
CG A:HIS431 4.1 11.1 1.0
ND1 A:HIS433 4.1 12.3 1.0
CG A:HIS433 4.2 12.4 1.0
NE2 A:HIS592 4.2 15.5 1.0
CE1 A:TYQ382 4.2 28.6 0.8
OZ A:TYQ382 4.2 29.6 0.2
CD2 A:HIS592 4.2 14.6 1.0
O A:HOH808 4.3 15.5 1.0
CE A:MET602 4.8 27.9 0.2
SD A:MET602 4.9 22.0 0.8
CA A:HIS592 4.9 12.9 1.0
SD A:MET602 5.0 21.3 0.2

Copper binding site 2 out of 2 in 5zoz

Go back to Copper Binding Sites List in 5zoz
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 (1)


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 (1) within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cu701

b:16.7
occ:1.00
 O B:HOH995 1.8 15.3 0.3
NE2 B:HIS431 2.0 13.8 1.0
NE2 B:HIS433 2.0 13.2 1.0
O B:HOH801 2.1 21.9 0.6
CD2 B:HIS592 2.1 12.4 1.0
OH B:TYQ382 2.5 22.2 0.8
CD2 B:HIS431 3.0 11.2 1.0
CE1 B:HIS431 3.0 12.8 1.0
CG B:HIS592 3.0 15.8 1.0
CE1 B:HIS433 3.0 15.1 1.0
CD2 B:HIS433 3.0 13.5 1.0
NE2 B:HIS592 3.2 19.4 1.0
CZ B:TYQ382 3.3 17.9 0.8
CB B:HIS592 3.4 11.2 1.0
N5 B:TYQ382 3.6 42.3 0.8
CE2 B:TYQ382 3.7 30.8 0.8
O B:HOH1271 3.7 47.7 1.0
OZ B:TYQ382 4.0 23.8 0.2
ND1 B:HIS431 4.1 14.4 1.0
CG B:HIS431 4.1 10.2 1.0
ND1 B:HIS433 4.1 11.5 1.0
CG B:HIS433 4.2 9.4 1.0
ND1 B:HIS592 4.2 18.8 1.0
CE1 B:TYQ382 4.2 19.5 0.8
O B:HOH805 4.3 16.9 1.0
CE1 B:HIS592 4.3 12.3 1.0
SD B:MET602 4.9 22.1 0.8
CD2 B:TYQ382 4.9 22.0 0.8
CA B:HIS592 5.0 11.8 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 05:48:04 2025

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