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Copper in PDB 5zp3: Copper Amine Oxidase From Arthrobacter Globiformis Anaerobically Reduced By Ethylamine at pH 10 at 288 K (1)

Enzymatic activity of Copper Amine Oxidase From Arthrobacter Globiformis Anaerobically Reduced By Ethylamine at pH 10 at 288 K (1)

All present enzymatic activity of Copper Amine Oxidase From Arthrobacter Globiformis Anaerobically Reduced By Ethylamine at pH 10 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 10 at 288 K (1), PDB code: 5zp3 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) 33.27 / 1.78
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 193.811, 64.969, 159.054, 90.00, 117.20, 90.00
R / Rfree (%) 14.7 / 17.2

Other elements in 5zp3:

The structure of Copper Amine Oxidase From Arthrobacter Globiformis Anaerobically Reduced By Ethylamine at pH 10 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 10 at 288 K (1) (pdb code 5zp3). 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 10 at 288 K (1), PDB code: 5zp3:
Jump to Copper binding site number: 1; 2;

Copper binding site 1 out of 2 in 5zp3

Go back to Copper Binding Sites List in 5zp3
Copper binding site 1 out of 2 in the Copper Amine Oxidase From Arthrobacter Globiformis Anaerobically Reduced By Ethylamine at pH 10 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 10 at 288 K (1) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu701

b:20.3
occ:1.00
O A:HOH1166 1.9 24.3 0.5
CE1 A:HIS431 2.0 12.3 1.0
ND1 A:HIS592 2.1 20.1 1.0
NE2 A:HIS433 2.1 14.7 1.0
O A:HOH960 2.1 23.8 0.6
OH A:TYQ382 2.4 30.2 0.8
NE2 A:HIS431 2.8 20.1 1.0
CE1 A:HIS592 3.0 23.5 1.0
CE1 A:HIS433 3.0 18.1 1.0
ND1 A:HIS431 3.1 18.8 1.0
CD2 A:HIS433 3.1 16.3 1.0
CG A:HIS592 3.1 20.6 1.0
CZ A:TYQ382 3.2 27.4 0.8
N5 A:TYQ382 3.4 45.7 0.8
CB A:HIS592 3.5 16.2 1.0
CE2 A:TYQ382 3.6 34.0 0.8
CD2 A:HIS431 4.1 13.0 1.0
NE2 A:HIS592 4.2 20.0 1.0
ND1 A:HIS433 4.2 16.1 1.0
CE1 A:TYQ382 4.2 26.7 0.8
CG A:HIS431 4.2 13.8 1.0
CD2 A:HIS592 4.2 19.2 1.0
CG A:HIS433 4.2 15.5 1.0
O A:HOH812 4.3 19.3 1.0
OZ A:TYQ382 4.3 29.6 0.2
CD2 A:TYQ382 4.8 29.4 0.8
SD A:MET602 4.9 26.8 1.0
CG1 A:VAL406 5.0 19.5 1.0
CA A:HIS592 5.0 16.0 1.0

Copper binding site 2 out of 2 in 5zp3

Go back to Copper Binding Sites List in 5zp3
Copper binding site 2 out of 2 in the Copper Amine Oxidase From Arthrobacter Globiformis Anaerobically Reduced By Ethylamine at pH 10 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 10 at 288 K (1) within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cu701

b:19.6
occ:1.00
O B:HOH1011 2.0 18.9 0.6
NE2 B:HIS431 2.0 14.4 1.0
ND1 B:HIS592 2.1 20.6 1.0
NE2 B:HIS433 2.1 15.2 1.0
OH B:TYQ382 2.2 26.5 0.8
O B:HOH1205 2.8 8.9 0.1
CD2 B:HIS431 2.9 14.3 1.0
CE1 B:HIS592 3.0 21.5 1.0
CZ B:TYQ382 3.0 24.7 0.8
CE1 B:HIS433 3.1 15.2 1.0
CE1 B:HIS431 3.1 16.9 1.0
CG B:HIS592 3.1 21.7 1.0
CD2 B:HIS433 3.2 17.7 1.0
N5 B:TYQ382 3.2 43.3 0.8
CE2 B:TYQ382 3.4 31.2 0.8
CB B:HIS592 3.5 17.6 1.0
O B:HOH1200 3.8 58.0 1.0
OZ B:TYQ382 3.9 27.0 0.2
CE1 B:TYQ382 4.1 22.6 0.8
CG B:HIS431 4.1 12.8 1.0
NE2 B:HIS592 4.1 21.8 1.0
ND1 B:HIS431 4.1 14.8 1.0
CD2 B:HIS592 4.2 21.3 1.0
ND1 B:HIS433 4.2 15.2 1.0
O B:HOH842 4.2 19.4 1.0
CG B:HIS433 4.3 17.0 1.0
CD2 B:TYQ382 4.7 26.0 0.8
CG1 B:VAL406 4.9 22.4 1.0
SD B:MET602 4.9 28.0 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: Sun Dec 13 11:21:22 2020

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