Copper in PDB 2woh: Strontium Soaked E. Coli Copper Amine Oxidase

All present enzymatic activity of Strontium Soaked E. Coli Copper Amine Oxidase:
1.4.3.6;

The structure of Strontium Soaked E. Coli Copper Amine Oxidase, PDB code: 2woh 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)	37.82 / 2.70
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	135.135, 166.911, 79.796, 90.00, 90.00, 90.00
R / Rfree (%)	18.564 / 24.28

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

Copper binding site 1 out of 2 in the Strontium Soaked 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 Strontium Soaked E. Coli Copper Amine Oxidase within 5.0Å range: probe atom residue distance (Å) B Occ A:Cu801 b:39.9 occ:1.00 NE2 A:HIS526 1.9 34.4 1.0 NE2 A:HIS524 2.1 34.5 1.0 ND1 A:HIS689 2.1 35.6 1.0 O A:HOH2260 2.7 35.3 1.0 CD2 A:HIS526 2.8 34.6 1.0 CE1 A:HIS526 2.9 34.7 1.0 CE1 A:HIS524 2.9 34.5 1.0 CG A:HIS689 3.1 35.5 1.0 CD2 A:HIS524 3.1 34.7 1.0 CE1 A:HIS689 3.1 35.7 1.0 CB A:HIS689 3.3 35.5 1.0 CG A:HIS526 3.9 34.5 1.0 ND1 A:HIS526 4.0 34.5 1.0 ND1 A:HIS524 4.0 34.3 1.0 CG A:HIS524 4.1 34.5 1.0 NE2 A:HIS689 4.2 35.4 1.0 CD2 A:HIS689 4.2 35.5 1.0 O2 A:TPQ466 4.4 45.9 1.0 CE A:MET699 4.7 38.3 1.0 SD A:MET699 4.7 38.8 1.0 CA A:HIS689 4.9 35.5 1.0 O A:HOH2101 4.9 26.8 1.0 CE1 A:HIS613 4.9 39.2 1.0 O A:HOH2199 5.0 47.0 1.0

Copper binding site 2 out of 2 in the Strontium Soaked 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 Strontium Soaked E. Coli Copper Amine Oxidase within 5.0Å range: probe atom residue distance (Å) B Occ B:Cu801 b:38.5 occ:1.00 NE2 B:HIS526 2.0 32.9 1.0 ND1 B:HIS689 2.1 36.3 1.0 NE2 B:HIS524 2.3 33.1 1.0 O B:HOH2176 2.6 37.6 1.0 CE1 B:HIS526 3.0 33.3 1.0 CG B:HIS689 3.0 35.8 1.0 CD2 B:HIS526 3.0 32.7 1.0 CE1 B:HIS689 3.1 36.5 1.0 CD2 B:HIS524 3.2 33.2 1.0 CE1 B:HIS524 3.2 33.4 1.0 CB B:HIS689 3.3 35.3 1.0 ND1 B:HIS526 4.1 32.9 1.0 CG B:HIS526 4.1 32.8 1.0 NE2 B:HIS689 4.2 36.3 1.0 CD2 B:HIS689 4.2 35.9 1.0 ND1 B:HIS524 4.3 33.2 1.0 CG B:HIS524 4.3 33.0 1.0 SD B:MET699 4.7 38.9 1.0 O2 B:TPQ466 4.7 57.0 1.0 CA B:HIS689 4.8 35.2 1.0

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