Copper in PDB 1ivu: Crystal Structure of Copper Amine Oxidase From Arthrobacter Globiformis: Initial Intermediate in Topaquinone Biogenesis

All present enzymatic activity of Crystal Structure of Copper Amine Oxidase From Arthrobacter Globiformis: Initial Intermediate in Topaquinone Biogenesis:
1.4.3.6;

The structure of Crystal Structure of Copper Amine Oxidase From Arthrobacter Globiformis: Initial Intermediate in Topaquinone Biogenesis, PDB code: 1ivu was solved by M.Kim, T.Okajima, S.Kishishita, M.Yoshimura, A.Kawamori, K.Tanizawa, H.Yamaguchi, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	7.00 / 1.90
Space group	I 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	157.878, 63.176, 184.279, 90.00, 111.81, 90.00
R / Rfree (%)	19.9 / 25.8

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

Copper binding site 1 out of 2 in the Crystal Structure of Copper Amine Oxidase From Arthrobacter Globiformis: Initial Intermediate in Topaquinone Biogenesis


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 1 of Crystal Structure of Copper Amine Oxidase From Arthrobacter Globiformis: Initial Intermediate in Topaquinone Biogenesis within 5.0Å range: probe atom residue distance (Å) B Occ A:Cu1001 b:19.1 occ:1.00 NE2 A:HIS431 1.8 2.0 1.0 ND1 A:HIS592 2.1 21.3 0.3 NE2 A:HIS433 2.1 23.0 1.0 ND1 A:HIS592 2.2 18.9 0.7 OH A:TYR382 2.6 27.3 1.0 CE1 A:HIS431 2.8 9.2 1.0 CD2 A:HIS431 2.8 6.2 1.0 CD2 A:HIS433 3.0 18.9 1.0 CE1 A:HIS592 3.0 26.2 0.3 CE1 A:HIS592 3.1 22.3 0.7 CG A:HIS592 3.2 28.0 0.3 CG A:HIS592 3.2 24.8 0.7 CE1 A:HIS433 3.2 17.3 1.0 CZ A:TYR382 3.3 21.0 1.0 CB A:HIS592 3.5 21.9 1.0 ND1 A:HIS431 3.9 7.0 1.0 CE2 A:TYR382 3.9 23.6 1.0 CG A:HIS431 4.0 6.3 1.0 CE1 A:TYR382 4.0 19.2 1.0 NE2 A:HIS592 4.2 24.4 0.3 CG A:HIS433 4.2 20.5 1.0 NE2 A:HIS592 4.2 18.3 0.7 O A:HOH1002 4.3 13.2 1.0 CD2 A:HIS592 4.3 22.7 0.7 CD2 A:HIS592 4.3 28.2 0.3 ND1 A:HIS433 4.3 17.9 1.0 SD A:MET602 4.9 33.0 1.0

Copper binding site 2 out of 2 in the Crystal Structure of Copper Amine Oxidase From Arthrobacter Globiformis: Initial Intermediate in Topaquinone Biogenesis


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 2 of Crystal Structure of Copper Amine Oxidase From Arthrobacter Globiformis: Initial Intermediate in Topaquinone Biogenesis within 5.0Å range: probe atom residue distance (Å) B Occ B:Cu1002 b:19.5 occ:1.00 NE2 B:HIS431 2.0 10.9 1.0 ND1 B:HIS592 2.0 23.1 0.7 NE2 B:HIS433 2.1 23.5 1.0 ND1 B:HIS592 2.5 26.2 0.3 CD2 B:HIS431 2.7 13.3 1.0 OH B:TYR382 2.8 22.5 1.0 CD2 B:HIS433 2.9 22.2 1.0 CG B:HIS592 3.0 18.0 0.7 CE1 B:HIS592 3.0 23.8 0.7 CE1 B:HIS431 3.1 10.5 1.0 CE1 B:HIS433 3.2 17.4 1.0 CG B:HIS592 3.3 23.3 0.3 CB B:HIS592 3.3 26.9 1.0 CE1 B:HIS592 3.6 24.4 0.3 CZ B:TYR382 3.6 20.6 1.0 CG B:HIS431 3.9 8.2 1.0 ND1 B:HIS431 4.0 13.1 1.0 NE2 B:HIS592 4.1 23.2 0.7 CD2 B:HIS592 4.1 23.4 0.7 CG B:HIS433 4.1 18.5 1.0 ND1 B:HIS433 4.2 14.7 1.0 CE2 B:TYR382 4.2 18.9 1.0 CE1 B:TYR382 4.3 20.0 1.0 O B:HOH1104 4.5 19.2 1.0 CD2 B:HIS592 4.5 25.3 0.3 NE2 B:HIS592 4.6 24.2 0.3 CA B:HIS592 4.8 19.2 1.0 CE B:MET602 4.8 28.7 1.0 SD B:MET602 4.9 29.6 1.0

M.Kim, T.Okajima, S.Kishishita, M.Yoshimura, A.Kawamori, K.Tanizawa, H.Yamaguchi. X-Ray Snapshots of Quinone Cofactor Biogenesis in Bacterial Copper Amine Oxidase. Nat.Struct.Biol. V. 9 591 2002.
ISSN: ISSN 1072-8368
PubMed: 12134140
DOI: 10.1038/NSB824