Copper in PDB 6grr: Crystal Structure of Escherichia Coli Amine Oxidase Mutant I342F/E573Q

The structure of Crystal Structure of Escherichia Coli Amine Oxidase Mutant I342F/E573Q, PDB code: 6grr was solved by T.G.Gaule, M.A.Smith, K.M.Tych, P.Pirrat, C.H.Trinh, A.R.Pearson, P.F.Knowles, M.J.Mcpherson, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	105.05 / 1.70
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	135.152, 166.836, 79.734, 90.00, 90.00, 90.00
R / Rfree (%)	16.6 / 19.3

The structure of Crystal Structure of Escherichia Coli Amine Oxidase Mutant I342F/E573Q also contains other interesting chemical elements:

Calcium

(Ca)

2 atoms

The binding sites of Copper atom in the Crystal Structure of Escherichia Coli Amine Oxidase Mutant I342F/E573Q (pdb code 6grr). 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 Escherichia Coli Amine Oxidase Mutant I342F/E573Q, PDB code: 6grr:
Jump to Copper binding site number: 1; 2;

Copper binding site 1 out of 2 in the Crystal Structure of Escherichia Coli Amine Oxidase Mutant I342F/E573Q


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 Escherichia Coli Amine Oxidase Mutant I342F/E573Q within 5.0Å range: probe atom residue distance (Å) B Occ A:Cu801 b:26.3 occ:1.00 ND1 A:HIS689 2.0 24.5 1.0 NE2 A:HIS526 2.0 23.0 1.0 NE2 A:HIS524 2.0 26.1 1.0 OH A:TYR466 2.1 31.4 1.0 CE1 A:HIS689 2.8 25.2 1.0 CE1 A:HIS524 2.9 26.9 1.0 CZ A:TYR466 2.9 30.9 1.0 CE1 A:HIS526 3.0 28.3 1.0 CD2 A:HIS526 3.0 25.4 1.0 CG A:HIS689 3.1 23.9 1.0 CD2 A:HIS524 3.1 24.2 1.0 CB A:HIS689 3.5 24.3 1.0 CE2 A:TYR466 3.5 33.7 1.0 CE1 A:TYR466 3.8 33.6 1.0 NE2 A:HIS689 4.0 25.1 1.0 ND1 A:HIS524 4.1 25.7 1.0 ND1 A:HIS526 4.1 27.3 1.0 O A:HOH1061 4.1 27.4 1.0 CG A:HIS526 4.1 24.8 1.0 CD2 A:HIS689 4.1 25.8 1.0 CG A:HIS524 4.2 24.2 1.0 CD2 A:TYR466 4.7 31.4 1.0 O A:HOH1013 4.7 45.5 1.0 CE A:MET699 4.8 32.0 1.0 SD A:MET699 4.8 32.0 1.0 CD1 A:TYR466 4.9 32.3 1.0

Copper binding site 2 out of 2 in the Crystal Structure of Escherichia Coli Amine Oxidase Mutant I342F/E573Q


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 Escherichia Coli Amine Oxidase Mutant I342F/E573Q within 5.0Å range: probe atom residue distance (Å) B Occ B:Cu801 b:26.0 occ:1.00 NE2 B:HIS526 1.9 25.4 1.0 NE2 B:HIS524 2.0 22.0 1.0 ND1 B:HIS689 2.1 25.6 1.0 OH B:TYR466 2.1 38.1 1.0 CE1 B:HIS526 2.8 32.0 1.0 CE1 B:HIS524 2.9 24.3 1.0 CZ B:TYR466 3.0 36.1 1.0 CE1 B:HIS689 3.0 25.5 1.0 CD2 B:HIS526 3.0 29.9 1.0 CD2 B:HIS524 3.1 22.7 1.0 CG B:HIS689 3.1 24.2 1.0 CE2 B:TYR466 3.5 40.2 1.0 CB B:HIS689 3.5 24.3 1.0 OE1 B:GLU490 3.9 29.8 0.5 ND1 B:HIS526 3.9 32.0 1.0 CE1 B:TYR466 3.9 37.1 1.0 ND1 B:HIS524 4.1 23.3 1.0 CG B:HIS526 4.1 26.9 1.0 NE2 B:HIS689 4.2 25.3 1.0 CG B:HIS524 4.2 23.6 1.0 OE2 B:GLU490 4.2 31.0 0.5 CD2 B:HIS689 4.2 24.6 1.0 O B:HOH1148 4.3 27.5 1.0 CD B:GLU490 4.5 28.0 0.5 CE B:MET699 4.7 33.3 1.0 CD2 B:TYR466 4.7 38.2 1.0 SD B:MET699 4.8 34.1 1.0

T.G.Gaule, M.A.Smith, K.M.Tych, P.Pirrat, C.H.Trinh, A.R.Pearson, P.F.Knowles, M.J.Mcpherson. Oxygen Activation Switch in the Copper Amine Oxidase of Escherichia Coli. Biochemistry V. 57 5301 2018.
ISSN: ISSN 1520-4995
PubMed: 30110143
DOI: 10.1021/ACS.BIOCHEM.8B00633