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Copper in PDB 5zp4: Copper Amine Oxidase From Arthrobacter Globiformis Anaerobically Reduced By Ethylamine at pH 10 at 288 K (2)

Enzymatic activity of Copper Amine Oxidase From Arthrobacter Globiformis Anaerobically Reduced By Ethylamine at pH 10 at 288 K (2)

All present enzymatic activity of Copper Amine Oxidase From Arthrobacter Globiformis Anaerobically Reduced By Ethylamine at pH 10 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 10 at 288 K (2), PDB code: 5zp4 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) 35.14 / 1.80
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 193.731, 64.838, 158.974, 90.00, 117.20, 90.00
R / Rfree (%) 14.5 / 16.8

Other elements in 5zp4:

The structure of Copper Amine Oxidase From Arthrobacter Globiformis Anaerobically Reduced By Ethylamine at pH 10 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 10 at 288 K (2) (pdb code 5zp4). 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 (2), PDB code: 5zp4:
Jump to Copper binding site number: 1; 2;

Copper binding site 1 out of 2 in 5zp4

Go back to Copper Binding Sites List in 5zp4
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 (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 10 at 288 K (2) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu701

b:15.9
occ:1.00
 O A:HOH955 1.8 16.8 0.5
NE2 A:HIS431 2.0 12.0 1.0
ND1 A:HIS592 2.1 14.0 1.0
NE2 A:HIS433 2.1 9.6 1.0
O A:HOH802 2.1 15.9 0.5
OH A:TYQ382 2.5 19.8 0.8
CD2 A:HIS431 2.9 9.6 1.0
CE1 A:HIS592 3.0 15.5 1.0
CE1 A:HIS433 3.0 13.3 1.0
CD2 A:HIS433 3.1 11.8 1.0
CE1 A:HIS431 3.1 14.8 1.0
CG A:HIS592 3.1 14.6 1.0
CZ A:TYQ382 3.3 19.9 0.8
CB A:HIS592 3.4 10.9 1.0
N5 A:TYQ382 3.6 45.1 0.8
CE2 A:TYQ382 3.8 28.9 0.8
CG A:HIS431 4.1 9.9 1.0
OZ A:TYQ382 4.1 24.6 0.2
NE2 A:HIS592 4.1 14.3 1.0
ND1 A:HIS431 4.1 10.3 1.0
ND1 A:HIS433 4.2 11.6 1.0
CD2 A:HIS592 4.2 15.3 1.0
CG A:HIS433 4.2 11.3 1.0
CE1 A:TYQ382 4.2 22.7 0.8
O A:HOH818 4.4 15.4 1.0
SD A:MET602 4.9 20.8 1.0
CA A:HIS592 5.0 8.9 1.0
CD2 A:TYQ382 5.0 24.4 0.8

Copper binding site 2 out of 2 in 5zp4

Go back to Copper Binding Sites List in 5zp4
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 (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 10 at 288 K (2) within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cu701

b:15.6
occ:1.00
 O B:HOH1220 1.9 15.7 0.3
CE1 B:HIS431 2.0 9.1 1.0
CD2 B:HIS592 2.1 11.1 1.0
O B:HOH801 2.1 15.1 0.5
NE2 B:HIS433 2.1 12.3 1.0
OH B:TYQ382 2.5 22.2 0.8
NE2 B:HIS431 3.0 18.9 1.0
CG B:HIS592 3.0 15.6 1.0
ND1 B:HIS431 3.0 15.3 1.0
CE1 B:HIS433 3.1 13.4 1.0
CD2 B:HIS433 3.1 12.7 1.0
NE2 B:HIS592 3.1 19.4 1.0
CZ B:TYQ382 3.2 17.6 0.8
N5 B:TYQ382 3.4 38.9 0.8
CB B:HIS592 3.5 11.1 1.0
CE2 B:TYQ382 3.6 28.0 0.8
O B:HOH1278 3.7 51.4 1.0
OZ B:TYQ382 4.0 23.1 0.2
CD2 B:HIS431 4.1 9.6 1.0
ND1 B:HIS592 4.2 18.4 1.0
CG B:HIS431 4.2 10.9 1.0
ND1 B:HIS433 4.2 10.9 1.0
CE1 B:HIS592 4.2 10.5 1.0
CG B:HIS433 4.2 9.4 1.0
CE1 B:TYQ382 4.2 16.7 0.8
O B:HOH812 4.3 14.6 1.0
CD2 B:TYQ382 4.9 22.4 0.8
SD B:MET602 4.9 23.3 1.0
CA B:HIS592 5.0 11.1 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 05:49:00 2025

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