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Copper in PDB 5zpe: Copper Amine Oxidase From Arthrobacter Globiformis Anaerobically Reduced By Ethylamine at pH 6 at 288 K (2)

Enzymatic activity of Copper Amine Oxidase From Arthrobacter Globiformis Anaerobically Reduced By Ethylamine at pH 6 at 288 K (2)

All present enzymatic activity of Copper Amine Oxidase From Arthrobacter Globiformis Anaerobically Reduced By Ethylamine at pH 6 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 6 at 288 K (2), PDB code: 5zpe 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) 40.41 / 1.69
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 193.558, 64.465, 158.831, 90.00, 117.12, 90.00
R / Rfree (%) 15.1 / 17.3

Other elements in 5zpe:

The structure of Copper Amine Oxidase From Arthrobacter Globiformis Anaerobically Reduced By Ethylamine at pH 6 at 288 K (2) 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 288 K (2) (pdb code 5zpe). 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 288 K (2), PDB code: 5zpe:
Jump to Copper binding site number: 1; 2;

Copper binding site 1 out of 2 in 5zpe

Go back to Copper Binding Sites List in 5zpe
Copper binding site 1 out of 2 in the Copper Amine Oxidase From Arthrobacter Globiformis Anaerobically Reduced By Ethylamine at pH 6 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 6 at 288 K (2) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu1001

b:16.2
occ:1.00
 O A:HOH1161 1.9 28.5 0.9
NE2 A:HIS431 1.9 11.5 1.0
O A:HOH1282 2.0 13.1 0.2
ND1 A:HIS592 2.0 15.3 1.0
NE2 A:HIS433 2.1 13.5 1.0
OH A:TYQ382 2.5 22.4 0.7
CE1 A:HIS431 2.9 13.8 1.0
CD2 A:HIS431 2.9 12.5 1.0
CE1 A:HIS592 3.0 17.4 1.0
CE1 A:HIS433 3.0 14.7 1.0
CD2 A:HIS433 3.1 16.6 1.0
CG A:HIS592 3.1 14.3 1.0
CZ A:TYQ382 3.3 25.6 0.7
CB A:HIS592 3.4 12.5 1.0
CE2 A:TYQ382 3.9 35.2 0.7
N5 A:TYQ382 3.9 40.1 0.7
ND1 A:HIS431 4.0 14.5 1.0
CG A:HIS431 4.1 12.9 1.0
CE1 A:TYQ382 4.1 31.1 0.7
NE2 A:HIS592 4.1 15.0 1.0
ND1 A:HIS433 4.2 13.4 1.0
O A:HOH1509 4.2 15.8 0.3
CD2 A:HIS592 4.2 11.4 1.0
CG A:HIS433 4.2 12.3 1.0
OZ A:TYQ382 4.2 31.9 0.3
O A:HOH1129 4.3 17.3 1.0
SD A:MET602 4.9 24.8 1.0
CA A:HIS592 4.9 10.5 1.0

Copper binding site 2 out of 2 in 5zpe

Go back to Copper Binding Sites List in 5zpe
Copper binding site 2 out of 2 in the Copper Amine Oxidase From Arthrobacter Globiformis Anaerobically Reduced By Ethylamine at pH 6 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 6 at 288 K (2) within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cu701

b:15.1
occ:1.00
 O B:HOH1012 1.9 9.9 0.3
O B:HOH865 2.0 30.6 1.0
NE2 B:HIS431 2.0 11.1 1.0
NE2 B:HIS433 2.1 11.3 1.0
CD2 B:HIS592 2.1 14.9 1.0
OH B:TYQ382 2.7 18.5 0.7
CE1 B:HIS431 3.0 12.1 1.0
CD2 B:HIS431 3.0 12.4 1.0
CD2 B:HIS433 3.0 12.1 1.0
CG B:HIS592 3.0 14.0 1.0
CE1 B:HIS433 3.1 15.5 1.0
NE2 B:HIS592 3.3 14.6 1.0
CB B:HIS592 3.4 13.4 1.0
CZ B:TYQ382 3.5 19.9 0.7
O B:HOH1275 3.7 40.3 1.0
N5 B:TYQ382 4.0 37.0 0.7
CE2 B:TYQ382 4.1 27.1 0.7
ND1 B:HIS431 4.1 10.9 1.0
CG B:HIS431 4.1 9.8 1.0
ND1 B:HIS433 4.2 13.5 1.0
CG B:HIS433 4.2 10.9 1.0
ND1 B:HIS592 4.2 16.0 1.0
CE1 B:TYQ382 4.3 21.8 0.7
CE1 B:HIS592 4.3 19.3 1.0
O B:HOH808 4.3 14.5 1.0
OZ B:TYQ382 4.6 21.6 0.3
SD B:MET602 4.8 27.0 1.0
CA B:HIS592 4.9 10.8 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: Wed Jul 31 05:43:35 2024

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