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Copper in PDB 5zpi: Copper Amine Oxidase From Arthrobacter Globiformis Anaerobically Reduced By Ethylamine at pH 6 at 293 K (3)

Enzymatic activity of Copper Amine Oxidase From Arthrobacter Globiformis Anaerobically Reduced By Ethylamine at pH 6 at 293 K (3)

All present enzymatic activity of Copper Amine Oxidase From Arthrobacter Globiformis Anaerobically Reduced By Ethylamine at pH 6 at 293 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 293 K (3), PDB code: 5zpi 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) 40.35 / 1.75
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 193.133, 64.215, 158.779, 90.00, 117.06, 90.00
R / Rfree (%) 15.3 / 17.5

Other elements in 5zpi:

The structure of Copper Amine Oxidase From Arthrobacter Globiformis Anaerobically Reduced By Ethylamine at pH 6 at 293 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 293 K (3) (pdb code 5zpi). 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 293 K (3), PDB code: 5zpi:
Jump to Copper binding site number: 1; 2;

Copper binding site 1 out of 2 in 5zpi

Go back to Copper Binding Sites List in 5zpi
Copper binding site 1 out of 2 in the Copper Amine Oxidase From Arthrobacter Globiformis Anaerobically Reduced By Ethylamine at pH 6 at 293 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 293 K (3) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu1001

b:17.1
occ:1.00
 NE2 A:HIS431 2.0 13.9 1.0
O A:HOH1164 2.0 27.1 1.0
NE2 A:HIS433 2.1 12.5 1.0
CD2 A:HIS592 2.1 11.3 1.0
O A:HOH1378 2.1 19.2 0.6
OH A:TYQ382 2.6 21.3 0.7
CD2 A:HIS431 2.9 12.0 1.0
CG A:HIS592 3.0 14.5 1.0
CE1 A:HIS431 3.0 15.1 1.0
CD2 A:HIS433 3.0 15.2 1.0
CE1 A:HIS433 3.1 15.7 1.0
NE2 A:HIS592 3.2 18.6 1.0
CZ A:TYQ382 3.3 27.2 0.7
CB A:HIS592 3.4 10.8 1.0
CE2 A:TYQ382 4.0 35.5 0.7
N5 A:TYQ382 4.0 32.3 0.7
ND1 A:HIS431 4.1 12.7 1.0
CG A:HIS431 4.1 12.0 1.0
O A:HOH1474 4.1 20.0 0.5
CE1 A:TYQ382 4.1 36.2 0.7
ND1 A:HIS433 4.2 11.8 1.0
ND1 A:HIS592 4.2 16.3 1.0
CG A:HIS433 4.2 11.7 1.0
OZ A:TYQ382 4.2 34.2 0.3
CE1 A:HIS592 4.2 12.4 1.0
O A:HOH1110 4.3 17.1 1.0
CE A:MET602 4.7 19.5 0.3
CA A:HIS592 4.9 10.0 1.0
SD A:MET602 4.9 20.1 0.7
CE A:MET602 4.9 20.8 0.7
CE1 A:TYQ382 5.0 37.3 0.3
SD A:MET602 5.0 20.4 0.3

Copper binding site 2 out of 2 in 5zpi

Go back to Copper Binding Sites List in 5zpi
Copper binding site 2 out of 2 in the Copper Amine Oxidase From Arthrobacter Globiformis Anaerobically Reduced By Ethylamine at pH 6 at 293 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 293 K (3) within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cu701

b:15.6
occ:1.00
 O B:HOH909 1.8 15.6 0.4
NE2 B:HIS431 1.9 9.5 1.0
O B:HOH831 2.1 18.3 0.7
ND1 B:HIS592 2.1 13.3 1.0
NE2 B:HIS433 2.1 14.0 1.0
OH B:TYQ382 2.7 19.1 0.8
CD2 B:HIS431 2.9 9.5 1.0
CE1 B:HIS431 2.9 10.4 1.0
CD2 B:HIS433 3.0 13.7 1.0
CE1 B:HIS592 3.0 14.5 1.0
CG B:HIS592 3.1 14.6 1.0
CE1 B:HIS433 3.1 15.0 1.0
CB B:HIS592 3.4 11.1 1.0
CZ B:TYQ382 3.4 21.2 0.8
N5 B:TYQ382 3.8 42.1 0.8
CE2 B:TYQ382 3.9 33.8 0.8
ND1 B:HIS431 4.0 10.2 1.0
CG B:HIS431 4.1 9.6 1.0
NE2 B:HIS592 4.2 14.5 1.0
CG B:HIS433 4.2 12.4 1.0
ND1 B:HIS433 4.2 12.9 1.0
CD2 B:HIS592 4.2 14.2 1.0
OZ B:TYQ382 4.2 27.1 0.2
CE1 B:TYQ382 4.3 26.0 0.8
O B:HOH810 4.3 13.7 1.0
SD B:MET602 4.9 24.9 1.0
CA B:HIS592 4.9 10.0 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: Mon Jul 14 05:50:47 2025

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