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Copper in PDB 5zp7: Copper Amine Oxidase From Arthrobacter Globiformis Anaerobically Reduced By Ethylamine at pH 6 at 277 K (3)

Enzymatic activity of Copper Amine Oxidase From Arthrobacter Globiformis Anaerobically Reduced By Ethylamine at pH 6 at 277 K (3)

All present enzymatic activity of Copper Amine Oxidase From Arthrobacter Globiformis Anaerobically Reduced By Ethylamine at pH 6 at 277 K (3):
1.4.3.21;

Protein crystallography data

The structure of Copper Amine Oxidase From Arthrobacter Globiformis Anaerobically Reduced By Ethylamine at pH 6 at 277 K (3), PDB code: 5zp7 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) 39.66 / 1.63
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 193.730, 64.374, 158.865, 90.00, 117.19, 90.00
R / Rfree (%) 14.9 / 16.6

Other elements in 5zp7:

The structure of Copper Amine Oxidase From Arthrobacter Globiformis Anaerobically Reduced By Ethylamine at pH 6 at 277 K (3) also contains other interesting chemical elements:

Sodium (Na) 2 atoms

Copper Binding Sites:

The binding sites of Copper atom in the Copper Amine Oxidase From Arthrobacter Globiformis Anaerobically Reduced By Ethylamine at pH 6 at 277 K (3) (pdb code 5zp7). 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 6 at 277 K (3), PDB code: 5zp7:
Jump to Copper binding site number: 1; 2;

Copper binding site 1 out of 2 in 5zp7

Go back to Copper Binding Sites List in 5zp7
Copper binding site 1 out of 2 in the Copper Amine Oxidase From Arthrobacter Globiformis Anaerobically Reduced By Ethylamine at pH 6 at 277 K (3)


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 6 at 277 K (3) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu1001

b:19.6
occ:1.00
NE2 A:HIS431 1.9 14.6 1.0
O A:HOH1119 2.0 32.5 1.0
ND1 A:HIS592 2.1 19.8 1.0
NE2 A:HIS433 2.1 14.2 1.0
O A:HOH1368 2.1 24.5 0.5
OH A:TYQ382 2.6 28.9 0.7
CE1 A:HIS431 2.8 16.5 1.0
CD2 A:HIS431 3.0 14.7 1.0
CE1 A:HIS592 3.0 19.5 1.0
CD2 A:HIS433 3.0 17.4 1.0
CE1 A:HIS433 3.0 16.6 1.0
CG A:HIS592 3.1 17.4 1.0
CZ A:TYQ382 3.3 24.1 0.7
CB A:HIS592 3.4 15.8 1.0
O A:HOH1515 3.7 47.4 1.0
N5 A:TYQ382 3.8 41.6 0.7
CE2 A:TYQ382 3.8 35.3 0.7
ND1 A:HIS431 4.0 16.6 1.0
CG A:HIS431 4.1 15.4 1.0
NE2 A:HIS592 4.1 18.6 1.0
ND1 A:HIS433 4.2 15.3 1.0
CE1 A:TYQ382 4.2 29.7 0.7
CG A:HIS433 4.2 14.0 1.0
CD2 A:HIS592 4.2 16.8 1.0
O A:HOH1505 4.2 22.9 0.4
O A:HOH1111 4.3 20.0 1.0
OZ A:TYQ382 4.5 30.4 0.3
CA A:HIS592 4.9 14.6 1.0
SD A:MET602 5.0 28.2 1.0

Copper binding site 2 out of 2 in 5zp7

Go back to Copper Binding Sites List in 5zp7
Copper binding site 2 out of 2 in the Copper Amine Oxidase From Arthrobacter Globiformis Anaerobically Reduced By Ethylamine at pH 6 at 277 K (3)


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 6 at 277 K (3) within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cu701

b:18.3
occ:1.00
NE2 B:HIS431 2.0 14.7 1.0
ND1 B:HIS592 2.0 17.7 1.0
NE2 B:HIS433 2.1 13.9 1.0
O B:HOH801 2.1 27.4 1.0
OH B:TYQ382 2.3 33.5 0.6
O B:HOH1203 2.5 19.5 0.5
CE1 B:HIS431 2.9 16.6 1.0
CD2 B:HIS431 3.0 13.3 1.0
CE1 B:HIS592 3.0 20.8 1.0
CD2 B:HIS433 3.0 17.1 1.0
CE1 B:HIS433 3.0 17.7 1.0
CG B:HIS592 3.1 15.9 1.0
CZ B:TYQ382 3.3 26.1 0.6
CB B:HIS592 3.4 16.3 1.0
N5 B:TYQ382 3.5 38.8 0.6
O B:HOH1238 3.6 45.0 1.0
CE2 B:TYQ382 3.8 34.0 0.6
ND1 B:HIS431 4.1 13.4 1.0
CG B:HIS431 4.1 14.4 1.0
NE2 B:HIS592 4.1 16.9 1.0
ND1 B:HIS433 4.2 16.8 1.0
CD2 B:HIS592 4.2 18.3 1.0
CG B:HIS433 4.2 13.8 1.0
O B:HOH927 4.3 17.9 1.0
CE1 B:TYQ382 4.3 26.1 0.6
OZ B:TYQ382 4.6 26.8 0.4
SD B:MET602 4.9 22.8 0.3
CA B:HIS592 4.9 13.4 1.0
SD B:MET602 5.0 28.3 0.7

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 05:49:16 2025

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