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Copper in PDB 5zp1: Copper Amine Oxidase From Arthrobacter Globiformis Anaerobically Reduced By Ethylamine at pH 9 at 288 K (1)

Enzymatic activity of Copper Amine Oxidase From Arthrobacter Globiformis Anaerobically Reduced By Ethylamine at pH 9 at 288 K (1)

All present enzymatic activity of Copper Amine Oxidase From Arthrobacter Globiformis Anaerobically Reduced By Ethylamine at pH 9 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 9 at 288 K (1), PDB code: 5zp1 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) 40.49 / 1.67
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 193.665, 64.739, 158.920, 90.00, 117.16, 90.00
R / Rfree (%) 14.6 / 16.6

Other elements in 5zp1:

The structure of Copper Amine Oxidase From Arthrobacter Globiformis Anaerobically Reduced By Ethylamine at pH 9 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 9 at 288 K (1) (pdb code 5zp1). 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 9 at 288 K (1), PDB code: 5zp1:
Jump to Copper binding site number: 1; 2;

Copper binding site 1 out of 2 in 5zp1

Go back to Copper Binding Sites List in 5zp1
Copper binding site 1 out of 2 in the Copper Amine Oxidase From Arthrobacter Globiformis Anaerobically Reduced By Ethylamine at pH 9 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 9 at 288 K (1) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu701

b:18.1
occ:1.00
O A:HOH1124 1.9 21.8 0.4
CE1 A:HIS431 2.0 10.2 1.0
NE2 A:HIS433 2.1 12.4 1.0
ND1 A:HIS592 2.1 16.5 1.0
O A:HOH811 2.1 20.7 0.5
OH A:TYQ382 2.5 20.4 0.8
NE2 A:HIS431 2.8 16.3 1.0
CE1 A:HIS433 3.0 15.7 1.0
CE1 A:HIS592 3.0 19.8 1.0
CD2 A:HIS433 3.1 12.9 1.0
ND1 A:HIS431 3.1 17.1 1.0
CG A:HIS592 3.1 14.6 1.0
CZ A:TYQ382 3.3 21.4 0.8
CB A:HIS592 3.4 12.4 1.0
O A:HOH1235 3.6 52.1 1.0
N5 A:TYQ382 3.7 38.8 0.8
CE2 A:TYQ382 3.8 31.0 0.8
CD2 A:HIS431 4.1 10.8 1.0
ND1 A:HIS433 4.1 12.9 1.0
NE2 A:HIS592 4.2 15.1 1.0
CG A:HIS433 4.2 11.8 1.0
CG A:HIS431 4.2 12.6 1.0
CE1 A:TYQ382 4.2 24.1 0.8
CD2 A:HIS592 4.2 15.5 1.0
OZ A:TYQ382 4.2 25.7 0.2
O A:HOH814 4.3 16.4 1.0
CE A:MET602 4.7 29.0 0.1
SD A:MET602 4.9 24.4 0.9
CE A:MET602 4.9 26.4 0.9
CA A:HIS592 5.0 13.0 1.0
SD A:MET602 5.0 25.4 0.1

Copper binding site 2 out of 2 in 5zp1

Go back to Copper Binding Sites List in 5zp1
Copper binding site 2 out of 2 in the Copper Amine Oxidase From Arthrobacter Globiformis Anaerobically Reduced By Ethylamine at pH 9 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 9 at 288 K (1) within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cu701

b:17.6
occ:1.00
NE2 B:HIS431 2.0 13.4 1.0
CE1 B:HIS433 2.1 12.2 1.0
ND1 B:HIS592 2.1 16.3 1.0
O B:HOH802 2.1 22.1 0.5
O B:HOH1123 2.2 12.7 0.1
OH B:TYQ382 2.4 21.7 0.8
NE2 B:HIS433 2.8 19.0 1.0
CE1 B:HIS431 3.0 16.8 1.0
CE1 B:HIS592 3.0 18.3 1.0
CD2 B:HIS431 3.0 12.7 1.0
CG B:HIS592 3.1 15.6 1.0
ND1 B:HIS433 3.2 18.0 1.0
CZ B:TYQ382 3.2 16.4 0.8
N5 B:TYQ382 3.4 38.9 0.8
CB B:HIS592 3.5 12.8 1.0
CE2 B:TYQ382 3.6 26.0 0.8
O B:HOH1249 3.8 49.0 1.0
OZ B:TYQ382 4.0 22.3 0.2
ND1 B:HIS431 4.1 12.5 1.0
CD2 B:HIS433 4.1 11.1 1.0
CG B:HIS431 4.1 10.9 1.0
NE2 B:HIS592 4.1 14.4 1.0
CE1 B:TYQ382 4.2 17.4 0.8
CD2 B:HIS592 4.2 15.5 1.0
CG B:HIS433 4.3 10.0 1.0
O B:HOH811 4.3 17.3 1.0
CD2 B:TYQ382 4.9 20.7 0.8
SD B:MET602 4.9 24.4 1.0
CA B:HIS592 5.0 12.8 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: Mon Jul 14 05:48:29 2025

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