Copper in PDB 2e2v: Substrate Schiff-Base Analogue of Copper Amine Oxidase From Arthrobacter Globiformis Formed with Benzylhydrazine

All present enzymatic activity of Substrate Schiff-Base Analogue of Copper Amine Oxidase From Arthrobacter Globiformis Formed with Benzylhydrazine:
1.4.3.6;

The structure of Substrate Schiff-Base Analogue of Copper Amine Oxidase From Arthrobacter Globiformis Formed with Benzylhydrazine, PDB code: 2e2v was solved by T.Murakawa, T.Okajima, M.Taki, Y.Yamamoto, S.Kuroda, H.Hayashi, K.Tanizawa, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	26.52 / 1.80
Space group	I 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	158.054, 62.640, 183.951, 90.00, 112.16, 90.00
R / Rfree (%)	21.7 / 25.2

The binding sites of Copper atom in the Substrate Schiff-Base Analogue of Copper Amine Oxidase From Arthrobacter Globiformis Formed with Benzylhydrazine (pdb code 2e2v). This binding sites where shown within 5.0 Angstroms radius around Copper atom.
In total 2 binding sites of Copper where determined in the Substrate Schiff-Base Analogue of Copper Amine Oxidase From Arthrobacter Globiformis Formed with Benzylhydrazine, PDB code: 2e2v:
Jump to Copper binding site number: 1; 2;

Copper binding site 1 out of 2 in the Substrate Schiff-Base Analogue of Copper Amine Oxidase From Arthrobacter Globiformis Formed with Benzylhydrazine


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 1 of Substrate Schiff-Base Analogue of Copper Amine Oxidase From Arthrobacter Globiformis Formed with Benzylhydrazine within 5.0Å range: probe atom residue distance (Å) B Occ A:Cu701 b:26.9 occ:1.00 NE2 A:HIS431 2.1 21.9 1.0 ND1 A:HIS592 2.1 27.6 1.0 NE2 A:HIS433 2.2 21.9 1.0 O A:HOH1649 2.5 38.4 1.0 O A:HOH1353 2.5 47.9 1.0 CD2 A:HIS433 3.0 22.4 1.0 CD2 A:HIS431 3.1 21.1 1.0 CG A:HIS592 3.1 25.7 1.0 CE1 A:HIS431 3.1 22.5 1.0 CE1 A:HIS592 3.1 27.2 1.0 CE1 A:HIS433 3.3 22.0 1.0 CB A:HIS592 3.3 22.4 1.0 O A:HOH1590 3.7 53.8 1.0 CG A:HIS433 4.2 21.4 1.0 CG A:HIS431 4.2 22.1 1.0 ND1 A:HIS431 4.2 22.3 1.0 NE2 A:HIS592 4.2 25.7 1.0 CD2 A:HIS592 4.2 26.9 1.0 ND1 A:HIS433 4.3 20.6 1.0 O A:HOH1254 4.4 30.6 1.0 O A:HOH1132 4.4 24.6 1.0 O2 A:3TY382 4.6 36.4 1.0 CA A:HIS592 4.9 21.5 1.0 SD A:MET602 4.9 34.5 1.0 CE A:MET602 5.0 32.7 1.0

Copper binding site 2 out of 2 in the Substrate Schiff-Base Analogue of Copper Amine Oxidase From Arthrobacter Globiformis Formed with Benzylhydrazine


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 2 of Substrate Schiff-Base Analogue of Copper Amine Oxidase From Arthrobacter Globiformis Formed with Benzylhydrazine within 5.0Å range: probe atom residue distance (Å) B Occ B:Cu701 b:22.7 occ:1.00 NE2 B:HIS431 2.1 22.7 1.0 NE2 B:HIS433 2.1 17.8 1.0 ND1 B:HIS592 2.1 22.8 1.0 O B:HOH953 2.7 34.7 1.0 CD2 B:HIS433 2.9 20.1 1.0 CE1 B:HIS431 3.0 21.3 1.0 CG B:HIS592 3.1 23.5 1.0 CD2 B:HIS431 3.1 19.8 1.0 CE1 B:HIS592 3.1 24.7 1.0 CE1 B:HIS433 3.2 20.5 1.0 CB B:HIS592 3.3 20.3 1.0 CG B:HIS433 4.1 16.8 1.0 ND1 B:HIS431 4.1 22.2 1.0 CG B:HIS431 4.2 19.8 1.0 ND1 B:HIS433 4.2 16.8 1.0 NE2 B:HIS592 4.2 23.5 1.0 CD2 B:HIS592 4.2 24.6 1.0 O B:HOH906 4.4 21.3 1.0 O2 B:3TY382 4.6 29.5 1.0 O B:HOH1006 4.6 28.1 1.0 CA B:HIS592 4.9 19.3 1.0 SD B:MET602 4.9 31.7 1.0

T.Murakawa, T.Okajima, M.Taki, Y.Yamamoto, S.Kuroda, H.Hayashi, K.Tanizawa. Catalytic Regulation Conducted By the Substrate Schiff Base and Conserved Aspartic Acid Residue in Bacterial Copper Amine Oxidase Reaction To Be Published.