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Copper in PDB 5zoy: Copper Amine Oxidase From Arthrobacter Globiformis Anaerobically Reduced By Ethylamine at pH 7 at 288 K (2)

Enzymatic activity of Copper Amine Oxidase From Arthrobacter Globiformis Anaerobically Reduced By Ethylamine at pH 7 at 288 K (2)

All present enzymatic activity of Copper Amine Oxidase From Arthrobacter Globiformis Anaerobically Reduced By Ethylamine at pH 7 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 7 at 288 K (2), PDB code: 5zoy 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) 39.69 / 1.70
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 193.637, 64.788, 158.954, 90.00, 117.14, 90.00
R / Rfree (%) 15.1 / 17.3

Other elements in 5zoy:

The structure of Copper Amine Oxidase From Arthrobacter Globiformis Anaerobically Reduced By Ethylamine at pH 7 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 7 at 288 K (2) (pdb code 5zoy). 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 7 at 288 K (2), PDB code: 5zoy:
Jump to Copper binding site number: 1; 2;

Copper binding site 1 out of 2 in 5zoy

Go back to Copper Binding Sites List in 5zoy
Copper binding site 1 out of 2 in the Copper Amine Oxidase From Arthrobacter Globiformis Anaerobically Reduced By Ethylamine at pH 7 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 7 at 288 K (2) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu701

b:15.5
occ:1.00
 O A:HOH875 1.8 18.5 0.6
NE2 A:HIS431 1.9 11.5 1.0
ND1 A:HIS592 2.0 15.3 1.0
O A:HOH817 2.0 18.6 0.6
NE2 A:HIS433 2.1 11.9 1.0
OH A:TYQ382 2.6 19.3 0.7
CE1 A:HIS431 2.9 13.1 1.0
CD2 A:HIS431 3.0 12.1 1.0
CE1 A:HIS592 3.0 15.6 1.0
CE1 A:HIS433 3.0 17.9 1.0
CG A:HIS592 3.0 14.0 1.0
CD2 A:HIS433 3.1 13.0 1.0
CB A:HIS592 3.4 10.8 1.0
CZ A:TYQ382 3.4 25.1 0.7
O A:HOH1220 3.6 46.6 1.0
N5 A:TYQ382 3.9 39.4 0.7
CE2 A:TYQ382 4.0 33.7 0.7
ND1 A:HIS431 4.0 13.2 1.0
CG A:HIS431 4.1 11.6 1.0
NE2 A:HIS592 4.1 14.6 1.0
ND1 A:HIS433 4.1 12.7 1.0
CD2 A:HIS592 4.2 13.9 1.0
CG A:HIS433 4.2 11.4 1.0
CE1 A:TYQ382 4.2 25.3 0.7
O A:HOH812 4.3 15.2 1.0
OZ A:TYQ382 4.5 25.6 0.3
CE A:MET602 4.8 23.4 0.3
CA A:HIS592 4.9 12.3 1.0
SD A:MET602 4.9 19.8 0.7
SD A:MET602 5.0 21.5 0.3

Copper binding site 2 out of 2 in 5zoy

Go back to Copper Binding Sites List in 5zoy
Copper binding site 2 out of 2 in the Copper Amine Oxidase From Arthrobacter Globiformis Anaerobically Reduced By Ethylamine at pH 7 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 7 at 288 K (2) within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cu701

b:16.4
occ:1.00
 CE1 B:HIS431 2.0 9.4 1.0
O B:HOH1001 2.1 12.2 0.5
NE2 B:HIS433 2.1 12.6 1.0
CD2 B:HIS592 2.1 11.4 1.0
OH B:TYQ382 2.5 18.0 0.8
NE2 B:HIS431 2.9 16.9 1.0
ND1 B:HIS431 3.0 16.6 1.0
CG B:HIS592 3.0 16.6 1.0
CE1 B:HIS433 3.0 16.3 1.0
CD2 B:HIS433 3.1 11.8 1.0
NE2 B:HIS592 3.2 20.5 1.0
CZ B:TYQ382 3.3 17.6 0.8
CB B:HIS592 3.4 11.0 1.0
O B:HOH1489 3.6 44.5 1.0
N5 B:TYQ382 3.7 41.1 0.8
CE2 B:TYQ382 3.8 29.9 0.8
OZ B:TYQ382 4.0 25.0 0.2
CD2 B:HIS431 4.1 9.9 1.0
CG B:HIS431 4.1 10.2 1.0
ND1 B:HIS433 4.2 12.8 1.0
CE1 B:TYQ382 4.2 20.2 0.8
CG B:HIS433 4.2 9.9 1.0
ND1 B:HIS592 4.2 18.5 1.0
O B:HOH1008 4.2 16.0 1.0
CE1 B:HIS592 4.3 12.4 1.0
CA B:HIS592 4.9 13.0 1.0
SD B:MET602 5.0 21.9 0.8
CD2 B:TYQ382 5.0 24.7 0.8

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: ISSN 0027-8424
PubMed: 30563857
DOI: 10.1073/PNAS.1811837116
Page generated: Wed Jul 31 05:40:48 2024

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