Copper in PDB 2cwt: Catalytic Base Deletion in Copper Amine Oxidase From Arthrobacter Globiformis

All present enzymatic activity of Catalytic Base Deletion in Copper Amine Oxidase From Arthrobacter Globiformis:
1.4.3.6;

The structure of Catalytic Base Deletion in Copper Amine Oxidase From Arthrobacter Globiformis, PDB code: 2cwt was solved by Y.C.Chiu, T.Okajima, T.Murakawa, M.Uchida, M.Taki, S.Hirota, M.Kim, H.Yamaguchi, Y.Kawano, N.Kamiya, S.Kuroda, H.Hayashi, Y.Yamamoto, K.Tanizawa, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	30.02 / 1.82
Space group	I 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	157.668, 63.840, 184.453, 90.00, 112.40, 90.00
R / Rfree (%)	19.1 / 20.4

The binding sites of Copper atom in the Catalytic Base Deletion in Copper Amine Oxidase From Arthrobacter Globiformis (pdb code 2cwt). 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 Base Deletion in Copper Amine Oxidase From Arthrobacter Globiformis, PDB code: 2cwt:
Jump to Copper binding site number: 1; 2;

Copper binding site 1 out of 2 in the Catalytic Base Deletion in 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 Base Deletion in Copper Amine Oxidase From Arthrobacter Globiformis within 5.0Å range: probe atom residue distance (Å) B Occ A:Cu1001 b:17.9 occ:1.00 NE2 A:HIS431 2.1 13.8 1.0 NE2 A:HIS433 2.1 13.2 1.0 ND1 A:HIS592 2.2 21.1 1.0 O A:HOH1147 2.4 33.0 1.0 CD2 A:HIS433 3.0 14.3 1.0 CE1 A:HIS431 3.1 14.2 1.0 CD2 A:HIS431 3.1 12.4 1.0 CG A:HIS592 3.1 21.1 1.0 CE1 A:HIS433 3.2 16.3 1.0 CE1 A:HIS592 3.2 20.6 1.0 CB A:HIS592 3.4 17.9 1.0 O A:HOH1187 3.7 36.5 1.0 ND1 A:HIS431 4.2 13.3 1.0 CG A:HIS433 4.2 14.9 1.0 CG A:HIS431 4.2 13.3 1.0 ND1 A:HIS433 4.2 15.5 1.0 O A:HOH1116 4.2 25.5 1.0 O A:HOH1032 4.3 20.5 1.0 CD2 A:HIS592 4.3 20.9 1.0 NE2 A:HIS592 4.3 22.1 1.0 O2 A:TPQ382 4.5 41.7 1.0 CE A:MET602 4.8 21.6 1.0 SD A:MET602 4.9 24.1 1.0 CA A:HIS592 4.9 15.3 1.0

Copper binding site 2 out of 2 in the Catalytic Base Deletion in 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 Base Deletion in Copper Amine Oxidase From Arthrobacter Globiformis within 5.0Å range: probe atom residue distance (Å) B Occ B:Cu1001 b:18.1 occ:1.00 NE2 B:HIS431 2.1 14.3 1.0 NE2 B:HIS433 2.1 13.5 1.0 O B:HOH1176 2.2 23.5 1.0 ND1 B:HIS592 2.2 21.4 1.0 CD2 B:HIS433 2.9 15.1 1.0 CE1 B:HIS431 3.0 15.5 1.0 CD2 B:HIS431 3.1 14.8 1.0 CG B:HIS592 3.2 22.2 1.0 CE1 B:HIS592 3.2 22.0 1.0 CE1 B:HIS433 3.3 15.6 1.0 CB B:HIS592 3.4 17.9 1.0 O B:HOH1352 4.0 33.0 1.0 CG B:HIS433 4.1 14.0 1.0 ND1 B:HIS431 4.2 14.5 1.0 CG B:HIS431 4.2 15.7 1.0 ND1 B:HIS433 4.3 15.9 1.0 CD2 B:HIS592 4.3 23.2 1.0 NE2 B:HIS592 4.3 23.5 1.0 O B:HOH1110 4.4 18.2 1.0 O2 B:TPQ382 4.6 42.2 1.0 CE B:MET602 4.7 28.0 1.0 SD B:MET602 4.8 28.5 1.0 CA B:HIS592 4.9 17.2 1.0

Y.C.Chiu, T.Okajima, T.Murakawa, M.Uchida, M.Taki, S.Hirota, M.Kim, H.Yamaguchi, Y.Kawano, N.Kamiya, S.Kuroda, H.Hayashi, Y.Yamamoto, K.Tanizawa. Kinetic and Structural Studies on the Catalytic Role of the Aspartic Acid Residue Conserved in Copper Amine Oxidase(,) Biochemistry V. 45 4105 2006.
ISSN: ISSN 0006-2960
PubMed: 16566584
DOI: 10.1021/BI052464L