Copper in PDB 7wis: Catalytic Intermediate Structure of N381A Mutant of Copper Amine Oxidase From Arthrobacter Globiformis

All present enzymatic activity of Catalytic Intermediate Structure of N381A Mutant of Copper Amine Oxidase From Arthrobacter Globiformis:
1.4.3.21;

The structure of Catalytic Intermediate Structure of N381A Mutant of Copper Amine Oxidase From Arthrobacter Globiformis, PDB code: 7wis was solved by T.Murakawa, T.Okajima, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	26.36 / 1.90
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	191.934, 63.472, 158.1, 90, 117.3, 90
R / Rfree (%)	16.3 / 19.7

The binding sites of Copper atom in the Catalytic Intermediate Structure of N381A Mutant of Copper Amine Oxidase From Arthrobacter Globiformis (pdb code 7wis). This binding sites where shown within 5.0 Angstroms radius around Copper atom.
In total 2 binding sites of Copper where determined in the Catalytic Intermediate Structure of N381A Mutant of Copper Amine Oxidase From Arthrobacter Globiformis, PDB code: 7wis:
Jump to Copper binding site number: 1; 2;

Copper binding site 1 out of 2 in the Catalytic Intermediate Structure of N381A Mutant of Copper Amine Oxidase From Arthrobacter Globiformis


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 1 of Catalytic Intermediate Structure of N381A Mutant of Copper Amine Oxidase From Arthrobacter Globiformis within 5.0Å range: probe atom residue distance (Å) B Occ A:Cu701 b:22.0 occ:1.00 O A:HOH876 1.9 33.1 1.0 NE2 A:HIS431 1.9 16.0 1.0 ND1 A:HIS592 2.1 17.4 0.7 NE2 A:HIS433 2.1 21.7 1.0 ND1 A:HIS592 2.2 20.5 0.3 O A:HOH1232 2.5 37.7 1.0 CE1 A:HIS431 2.9 19.7 1.0 CD2 A:HIS431 2.9 18.3 1.0 CD2 A:HIS433 3.0 19.2 1.0 CG A:HIS592 3.0 20.6 0.3 CG A:HIS592 3.0 19.3 0.7 CE1 A:HIS592 3.1 16.0 0.7 CE1 A:HIS592 3.1 17.9 0.3 CE1 A:HIS433 3.2 18.4 1.0 CB A:HIS592 3.3 21.3 0.7 CB A:HIS592 3.3 20.4 0.3 ND1 A:HIS431 4.0 18.2 1.0 CG A:HIS431 4.1 15.8 1.0 CD2 A:HIS592 4.1 21.6 0.3 NE2 A:HIS592 4.1 19.9 0.3 CD2 A:HIS592 4.2 17.6 0.7 NE2 A:HIS592 4.2 15.7 0.7 CG A:HIS433 4.2 20.2 1.0 ND1 A:HIS433 4.3 17.6 1.0 O A:HOH1078 4.3 36.8 1.0 O A:HOH1113 4.4 22.5 1.0 CA A:HIS592 4.8 19.0 0.7 CA A:HIS592 4.8 19.4 0.3 SD A:MET602 4.8 30.4 0.5

Copper binding site 2 out of 2 in the Catalytic Intermediate Structure of N381A Mutant of Copper Amine Oxidase From Arthrobacter Globiformis


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 2 of Catalytic Intermediate Structure of N381A Mutant of Copper Amine Oxidase From Arthrobacter Globiformis within 5.0Å range: probe atom residue distance (Å) B Occ B:Cu701 b:22.7 occ:1.00 NE2 B:HIS431 2.0 20.2 1.0 ND1 B:HIS592 2.0 14.3 0.7 NE2 B:HIS433 2.1 16.5 1.0 CD2 B:HIS592 2.5 22.3 0.3 CE1 B:HIS431 2.9 16.9 1.0 CD2 B:HIS433 2.9 18.6 1.0 CE1 B:HIS592 3.0 16.4 0.7 CD2 B:HIS431 3.0 17.4 1.0 CG B:HIS592 3.0 19.7 0.7 CG B:HIS592 3.2 23.6 0.3 CE1 B:HIS433 3.3 18.4 1.0 CB B:HIS592 3.3 22.6 0.7 CB B:HIS592 3.4 22.0 0.3 NE2 B:HIS592 3.6 18.9 0.3 ND1 B:HIS431 4.1 15.9 1.0 NE2 B:HIS592 4.1 17.5 0.7 CG B:HIS431 4.1 14.4 1.0 CD2 B:HIS592 4.1 17.9 0.7 CG B:HIS433 4.2 15.9 1.0 ND1 B:HIS433 4.3 15.7 1.0 ND1 B:HIS592 4.4 26.2 0.3 O B:HOH1126 4.5 20.6 1.0 CE1 B:HIS592 4.6 23.6 0.3 O B:HOH922 4.8 27.8 1.0 CA B:HIS592 4.9 21.1 0.7 SD B:MET602 4.9 34.7 1.0 CA B:HIS592 4.9 20.9 0.3 O B:HOH1042 4.9 46.2 1.0

M.Shoji, T.Murakawa, S.Nakanishi, M.Boero, Y.Shigeta, H.Hayashi, T.Okajima. Molecular Mechanism of A Large Conformational Change of the Quinone Cofactor in the Semiquinone Intermediate of Bacterial Copper Amine Oxidase. Chem Sci V. 13 10923 2022.
ISSN: ISSN 2041-6520
PubMed: 36320691
DOI: 10.1039/D2SC01356H