Copper in PDB 5zou: Copper Amine Oxidase From Arthrobacter Globiformis Anaerobically Reduced By Ethylamine at PH6 at 288 K (1)

All present enzymatic activity of Copper Amine Oxidase From Arthrobacter Globiformis Anaerobically Reduced By Ethylamine at PH6 at 288 K (1):
1.4.3.21;

The structure of Copper Amine Oxidase From Arthrobacter Globiformis Anaerobically Reduced By Ethylamine at PH6 at 288 K (1), PDB code: 5zou 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 / 1.68
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	193.440, 64.244, 158.805, 90.00, 117.12, 90.00
R / Rfree (%)	15.4 / 17.2

The structure of Copper Amine Oxidase From Arthrobacter Globiformis Anaerobically Reduced By Ethylamine at PH6 at 288 K (1) also contains other interesting chemical elements:

Sodium

(Na)

1 atom

The binding sites of Copper atom in the Copper Amine Oxidase From Arthrobacter Globiformis Anaerobically Reduced By Ethylamine at PH6 at 288 K (1) (pdb code 5zou). 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 PH6 at 288 K (1), PDB code: 5zou:
Jump to Copper binding site number: 1; 2;

Copper binding site 1 out of 2 in the Copper Amine Oxidase From Arthrobacter Globiformis Anaerobically Reduced By Ethylamine at PH6 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 PH6 at 288 K (1) within 5.0Å range: probe atom residue distance (Å) B Occ A:Cu1001 b:19.1 occ:1.00 NE2 A:HIS431 2.0 13.9 1.0 O A:HOH1166 2.0 30.2 0.8 O A:HOH1277 2.0 23.0 0.4 NE2 A:HIS433 2.0 12.9 1.0 ND1 A:HIS592 2.1 19.1 1.0 OH A:TYQ382 2.6 24.5 0.7 CE1 A:HIS431 2.9 14.4 1.0 CD2 A:HIS431 3.0 13.1 1.0 CE1 A:HIS592 3.0 20.6 1.0 CE1 A:HIS433 3.0 16.6 1.0 CD2 A:HIS433 3.0 16.9 1.0 CG A:HIS592 3.1 16.4 1.0 CZ A:TYQ382 3.4 30.6 0.7 CB A:HIS592 3.4 14.6 1.0 O A:HOH1478 3.6 47.7 1.0 N5 A:TYQ382 4.0 48.2 0.7 CE2 A:TYQ382 4.0 37.2 0.7 ND1 A:HIS431 4.0 15.1 1.0 CG A:HIS431 4.1 15.2 1.0 ND1 A:HIS433 4.1 14.9 1.0 OZ A:TYQ382 4.1 35.9 0.3 NE2 A:HIS592 4.1 16.1 1.0 CG A:HIS433 4.2 12.7 1.0 CD2 A:HIS592 4.2 14.5 1.0 CE1 A:TYQ382 4.2 36.4 0.7 O A:HOH1104 4.3 19.7 1.0 SD A:MET602 4.9 28.6 1.0 CA A:HIS592 5.0 12.3 1.0

Copper binding site 2 out of 2 in the Copper Amine Oxidase From Arthrobacter Globiformis Anaerobically Reduced By Ethylamine at PH6 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 PH6 at 288 K (1) within 5.0Å range: probe atom residue distance (Å) B Occ B:Cu701 b:18.3 occ:1.00 O B:HOH1256 2.0 24.5 0.3 CE1 B:HIS431 2.0 10.0 1.0 CD2 B:HIS592 2.0 12.0 1.0 NE2 B:HIS433 2.1 13.4 1.0 O B:HOH996 2.1 27.5 0.7 OH B:TYQ382 2.6 24.1 0.8 NE2 B:HIS431 2.8 15.5 1.0 CG B:HIS592 3.0 14.9 1.0 CE1 B:HIS433 3.0 15.7 1.0 CD2 B:HIS433 3.1 15.6 1.0 ND1 B:HIS431 3.1 16.5 1.0 NE2 B:HIS592 3.1 25.2 1.0 CZ B:TYQ382 3.4 28.8 0.8 CB B:HIS592 3.4 16.7 1.0 O B:HOH1305 3.6 43.4 1.0 N5 B:TYQ382 3.9 51.8 0.8 CE2 B:TYQ382 4.0 39.4 0.8 CD2 B:HIS431 4.0 10.5 1.0 ND1 B:HIS433 4.1 14.7 1.0 ND1 B:HIS592 4.2 20.4 1.0 CG B:HIS431 4.2 12.4 1.0 CG B:HIS433 4.2 12.6 1.0 CE1 B:HIS592 4.2 13.5 1.0 OZ B:TYQ382 4.2 31.2 0.2 CE1 B:TYQ382 4.2 29.9 0.8 O B:HOH816 4.3 16.1 1.0 CE B:MET602 4.6 45.5 1.0 CA B:HIS592 4.9 12.7 1.0 SD B:MET602 5.0 29.2 1.0

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