Copper in PDB 2wof: Edta Treated E. Coli Copper Amine Oxidase

All present enzymatic activity of Edta Treated E. Coli Copper Amine Oxidase:
1.4.3.6;

The structure of Edta Treated E. Coli Copper Amine Oxidase, PDB code: 2wof was solved by M.A.Smith, P.Pirrat, A.R.Pearson, P.F.Knowles, S.E.V.Phillips, M.J.Mcpherson, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	19.96 / 2.25
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	135.079, 166.880, 79.802, 90.00, 90.00, 90.00
R / Rfree (%)	16.686 / 22.041

The binding sites of Copper atom in the Edta Treated E. Coli Copper Amine Oxidase (pdb code 2wof). This binding sites where shown within 5.0 Angstroms radius around Copper atom.
In total 2 binding sites of Copper where determined in the Edta Treated E. Coli Copper Amine Oxidase, PDB code: 2wof:
Jump to Copper binding site number: 1; 2;

Copper binding site 1 out of 2 in the Edta Treated E. Coli Copper Amine Oxidase


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 1 of Edta Treated E. Coli Copper Amine Oxidase within 5.0Å range: probe atom residue distance (Å) B Occ A:Cu1726 b:40.7 occ:1.00 CE1 A:HIS526 1.9 29.9 1.0 NE2 A:HIS524 2.2 27.3 1.0 ND1 A:HIS689 2.2 32.9 1.0 O4 A:TPQ466 2.3 37.5 0.5 O A:HOH2434 2.8 24.3 0.5 NE2 A:HIS526 2.9 30.9 1.0 ND1 A:HIS526 2.9 31.2 1.0 CD2 A:HIS524 3.1 28.3 1.0 CE1 A:HIS524 3.2 29.4 1.0 CG A:HIS689 3.2 29.7 1.0 C4 A:TPQ466 3.2 38.9 0.5 CE1 A:HIS689 3.2 31.7 1.0 O5 A:TPQ466 3.4 42.8 0.5 CB A:HIS689 3.5 29.9 1.0 C5 A:TPQ466 3.7 38.8 0.5 CD2 A:HIS526 4.0 27.6 1.0 CG A:HIS526 4.1 29.7 1.0 CG A:HIS524 4.2 29.6 1.0 ND1 A:HIS524 4.2 30.9 1.0 C3 A:TPQ466 4.3 38.2 0.5 NE2 A:HIS689 4.3 30.9 1.0 CD2 A:HIS689 4.4 30.7 1.0 CE A:MET699 4.5 35.9 0.5 O2 A:TPQ466 4.7 42.8 0.5 O A:HOH2341 4.7 39.8 1.0 CE A:MET699 4.7 33.9 0.5 SD A:MET699 4.8 39.3 0.5 SD A:MET699 5.0 37.4 0.5 C6 A:TPQ466 5.0 39.1 0.5

Copper binding site 2 out of 2 in the Edta Treated E. Coli Copper Amine Oxidase


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 2 of Edta Treated E. Coli Copper Amine Oxidase within 5.0Å range: probe atom residue distance (Å) B Occ B:Cu1727 b:37.5 occ:1.00 O4 B:TPQ466 1.9 35.5 0.5 NE2 B:HIS526 2.1 31.1 1.0 NE2 B:HIS524 2.1 28.3 1.0 ND1 B:HIS689 2.2 30.8 1.0 CE1 B:HIS524 3.0 24.9 1.0 CD2 B:HIS526 3.0 28.8 1.0 C4 B:TPQ466 3.0 40.0 0.5 O B:HOH2307 3.1 15.3 0.5 CE1 B:HIS526 3.1 30.8 1.0 CD2 B:HIS524 3.2 28.3 1.0 CE1 B:HIS689 3.2 27.3 1.0 CG B:HIS689 3.2 28.6 1.0 CB B:HIS689 3.5 28.8 1.0 C5 B:TPQ466 3.9 40.2 0.5 O5 B:TPQ466 3.9 43.6 0.5 C3 B:TPQ466 3.9 38.6 0.5 ND1 B:HIS524 4.1 27.7 1.0 CG B:HIS526 4.1 28.9 1.0 ND1 B:HIS526 4.2 32.8 1.0 CG B:HIS524 4.2 29.5 1.0 NE2 B:HIS689 4.3 26.2 1.0 CD2 B:HIS689 4.3 26.9 1.0 SD B:MET699 4.5 43.6 0.5 CE B:MET699 4.5 36.7 0.5 O B:HOH2231 4.8 42.7 1.0 O2 B:TPQ466 4.8 33.9 0.5 CE B:MET699 4.8 39.6 0.5 SD B:MET699 4.9 43.3 0.5

M.A.Smith, P.Pirrat, A.R.Pearson, C.R.Kurtis, T.G.Gaule, P.F.Knowles, S.E.Phillips, M.J.Mcpherson. Exploring the Roles of the Metal Ions in Escherichia Coli Copper Amine Oxidase. Biochemistry V. 49 1268 2010.
ISSN: ISSN 0006-2960
PubMed: 20052994
DOI: 10.1021/BI901738K