Strontium 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 structure of Strontium Soaked E. Coli Copper Amine Oxidase also contains other interesting chemical elements:

Copper	(Cu)	2 atoms
Calcium	(Ca)	2 atoms

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

Strontium 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 Strontium with other atoms in the Sr binding site number 1 of Strontium Soaked E. Coli Copper Amine Oxidase within 5.0Å range: probe atom residue distance (Å) B Occ A:Sr1726 b:56.5 occ:1.00 O A:TYR667 2.4 42.9 1.0 OE1 A:GLU672 2.5 44.0 1.0 OD2 A:ASP670 2.6 44.6 1.0 OE2 A:GLU573 2.7 42.0 1.0 OE1 A:GLU573 2.7 41.8 1.0 CD A:GLU573 3.0 41.9 1.0 OD1 A:ASP670 3.1 43.7 1.0 CG A:ASP670 3.2 44.2 1.0 CD A:GLU672 3.4 43.9 1.0 CG A:GLU672 3.5 43.1 1.0 C A:TYR667 3.6 43.0 1.0 CB A:GLU672 4.4 42.6 1.0 CA A:TYR667 4.5 42.8 1.0 CD2 A:HIS644 4.5 43.9 1.0 OE1 A:GLU647 4.5 39.9 1.0 CG A:GLU573 4.6 42.1 1.0 OE2 A:GLU672 4.6 44.7 1.0 N A:SER668 4.6 43.3 1.0 N A:ARG642 4.6 40.3 1.0 NE2 A:HIS644 4.6 44.0 1.0 CA A:SER668 4.7 43.6 1.0 CB A:ASP670 4.7 44.0 1.0 CB A:ARG642 4.8 40.9 1.0 CB A:THR641 4.9 39.3 1.0 N A:GLU672 4.9 42.6 1.0 O A:HOH2332 4.9 62.4 1.0 O A:ARG642 5.0 40.6 1.0 OE2 A:GLU647 5.0 40.8 1.0 CB A:TYR667 5.0 42.8 1.0

Strontium 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 Strontium with other atoms in the Sr binding site number 2 of Strontium Soaked E. Coli Copper Amine Oxidase within 5.0Å range: probe atom residue distance (Å) B Occ B:Sr1727 b:58.4 occ:1.00 O B:TYR667 2.3 46.2 1.0 OE2 B:GLU573 2.6 39.2 1.0 OE1 B:GLU573 2.6 40.4 1.0 OE2 B:GLU672 2.7 48.0 1.0 CD B:GLU573 2.9 40.1 1.0 OD1 B:ASP670 3.0 49.0 1.0 OD2 B:ASP670 3.0 49.9 1.0 CG B:GLU672 3.2 47.8 1.0 CG B:ASP670 3.4 49.2 1.0 CD B:GLU672 3.4 48.2 1.0 C B:TYR667 3.5 46.1 1.0 CA B:SER668 4.3 47.1 1.0 CB B:GLU672 4.3 47.7 1.0 N B:SER668 4.3 46.6 1.0 CG B:GLU573 4.4 40.4 1.0 CA B:TYR667 4.5 45.7 1.0 OE1 B:GLU672 4.6 48.6 1.0 CD2 B:HIS644 4.6 47.8 1.0 NE2 B:HIS644 4.8 48.2 1.0 N B:GLU672 4.8 47.8 1.0 OE1 B:GLU647 4.8 44.7 1.0 OE2 B:GLU647 4.8 44.9 1.0 CB B:ASP670 4.8 48.8 1.0 N B:ARG642 4.9 43.6 1.0 C B:SER668 4.9 47.6 1.0 CB B:ARG642 4.9 44.3 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