Copper in PDB 1d6u: Crystal Structure of E. Coli Amine Oxidase Anaerobically Reduced with Beta-Phenylethylamine

All present enzymatic activity of Crystal Structure of E. Coli Amine Oxidase Anaerobically Reduced with Beta-Phenylethylamine:
1.4.3.6;

The structure of Crystal Structure of E. Coli Amine Oxidase Anaerobically Reduced with Beta-Phenylethylamine, PDB code: 1d6u was solved by C.M.Wilmot, J.Hajdu, M.J.Mcpherson, P.F.Knowles, S.E.V.Phillips, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	30.00 / 2.40
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	135.236, 166.482, 79.628, 90.00, 90.00, 90.00
R / Rfree (%)	18.1 / 23.9

The structure of Crystal Structure of E. Coli Amine Oxidase Anaerobically Reduced with Beta-Phenylethylamine also contains other interesting chemical elements:

Calcium

(Ca)

4 atoms

The binding sites of Copper atom in the Crystal Structure of E. Coli Amine Oxidase Anaerobically Reduced with Beta-Phenylethylamine (pdb code 1d6u). 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 E. Coli Amine Oxidase Anaerobically Reduced with Beta-Phenylethylamine, PDB code: 1d6u:
Jump to Copper binding site number: 1; 2;

Copper binding site 1 out of 2 in the Crystal Structure of E. Coli Amine Oxidase Anaerobically Reduced with Beta-Phenylethylamine


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 E. Coli Amine Oxidase Anaerobically Reduced with Beta-Phenylethylamine within 5.0Å range: probe atom residue distance (Å) B Occ A:Cu801 b:26.5 occ:1.00 NE2 A:HIS526 2.1 21.9 1.0 NE2 A:HIS524 2.1 28.2 1.0 ND1 A:HIS689 2.2 22.6 1.0 CD2 A:HIS526 2.8 23.8 1.0 O A:HOH2440 2.9 27.1 1.0 CE1 A:HIS524 2.9 21.2 1.0 CG A:HIS689 3.2 19.0 1.0 CE1 A:HIS526 3.2 27.7 1.0 CE1 A:HIS689 3.2 20.2 1.0 CD2 A:HIS524 3.3 20.6 1.0 CB A:HIS689 3.4 22.6 1.0 O A:HOH2589 3.8 44.3 1.0 CG A:HIS526 4.0 21.8 1.0 ND1 A:HIS524 4.1 24.8 1.0 ND1 A:HIS526 4.2 29.4 1.0 CG A:HIS524 4.3 22.6 1.0 NE2 A:HIS689 4.3 23.6 1.0 CD2 A:HIS689 4.4 19.6 1.0 O A:HOH2756 4.6 39.6 1.0 OZ A:TYQ466 4.8 44.4 1.0 O A:HOH2448 4.8 34.4 1.0 SD A:MET699 4.8 50.8 1.0 CE A:MET699 4.9 52.3 1.0 CE1 A:HIS613 5.0 25.7 1.0 CA A:HIS689 5.0 21.2 1.0

Copper binding site 2 out of 2 in the Crystal Structure of E. Coli Amine Oxidase Anaerobically Reduced with Beta-Phenylethylamine


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 E. Coli Amine Oxidase Anaerobically Reduced with Beta-Phenylethylamine within 5.0Å range: probe atom residue distance (Å) B Occ B:Cu801 b:29.4 occ:1.00 NE2 B:HIS526 2.1 31.1 1.0 ND1 B:HIS689 2.2 19.2 1.0 NE2 B:HIS524 2.2 24.6 1.0 O B:HOH3413 2.8 21.2 1.0 CD2 B:HIS526 2.9 25.8 1.0 CE1 B:HIS524 3.0 22.3 1.0 CG B:HIS689 3.1 22.7 1.0 CE1 B:HIS526 3.2 28.6 1.0 CE1 B:HIS689 3.2 18.4 1.0 CD2 B:HIS524 3.2 26.2 1.0 CB B:HIS689 3.3 18.2 1.0 CG B:HIS526 4.1 22.6 1.0 ND1 B:HIS524 4.1 25.5 1.0 O B:HOH3179 4.2 40.8 1.0 ND1 B:HIS526 4.2 27.6 1.0 CG B:HIS524 4.3 26.4 1.0 CD2 B:HIS689 4.3 18.1 1.0 NE2 B:HIS689 4.3 23.3 1.0 SD B:MET699 4.8 53.0 1.0 O B:HOH3037 4.8 35.3 1.0 CA B:HIS689 4.9 22.4 1.0 OZ B:TYQ466 4.9 45.9 1.0 O B:HOH3695 5.0 23.4 1.0 OE2 B:GLU490 5.0 60.7 1.0

C.M.Wilmot, J.Hajdu, M.J.Mcpherson, P.F.Knowles, S.E.Phillips. Visualization of Dioxygen Bound to Copper During Enzyme Catalysis. Science V. 286 1724 1999.
ISSN: ISSN 0036-8075
PubMed: 10576737
DOI: 10.1126/SCIENCE.286.5445.1724