Arsenic in PDB 1i19: Crystal Structure of Cholesterol Oxidase From B.Sterolicum

All present enzymatic activity of Crystal Structure of Cholesterol Oxidase From B.Sterolicum:
1.1.3.6;

The structure of Crystal Structure of Cholesterol Oxidase From B.Sterolicum, PDB code: 1i19 was solved by R.Coulombe, K.Q.Yue, S.Ghisla, A.Vrielink, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	36.91 / 1.70
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	77.440, 124.470, 80.840, 90.00, 109.17, 90.00
R / Rfree (%)	18.2 / 20.1

The structure of Crystal Structure of Cholesterol Oxidase From B.Sterolicum also contains other interesting chemical elements:

Manganese

(Mn)

3 atoms

The binding sites of Arsenic atom in the Crystal Structure of Cholesterol Oxidase From B.Sterolicum (pdb code 1i19). This binding sites where shown within 5.0 Angstroms radius around Arsenic atom.
In total only one binding site of Arsenic was determined in the Crystal Structure of Cholesterol Oxidase From B.Sterolicum, PDB code: 1i19:

Arsenic binding site 1 out of 1 in the Crystal Structure of Cholesterol Oxidase From B.Sterolicum


Mono view


Stereo pair view

A full contact list of Arsenic with other atoms in the As binding site number 1 of Crystal Structure of Cholesterol Oxidase From B.Sterolicum within 5.0Å range: probe atom residue distance (Å) B Occ B:As703 b:22.6 occ:1.00 AS B:CAC703 0.0 22.6 1.0 O1 B:CAC703 1.6 22.1 1.0 O2 B:CAC703 1.6 21.7 1.0 C2 B:CAC703 1.9 22.4 1.0 C1 B:CAC703 1.9 22.2 1.0 MN B:MN702 3.5 20.0 1.0 OD1 B:ASN542 3.8 16.7 1.0 O B:HOH1180 4.0 18.8 1.0 O B:HOH1862 4.2 26.9 1.0 O B:ASN542 4.3 16.4 1.0 O B:HOH1863 4.4 18.3 1.0 C B:ASN542 4.6 16.2 1.0 CG B:ASN542 4.6 16.1 1.0 CA B:ASN543 4.6 17.3 1.0 N B:ASN543 4.7 16.7 1.0 OE2 B:GLU579 4.7 17.9 1.0 C B:ASN543 4.9 17.8 1.0 ND2 B:ASN542 5.0 16.5 1.0

R.Coulombe, K.Q.Yue, S.Ghisla, A.Vrielink. Oxygen Access to the Active Site of Cholesterol Oxidase Through A Narrow Channel Is Gated By An Arg-Glu Pair. J.Biol.Chem. V. 276 30435 2001.
ISSN: ISSN 0021-9258
PubMed: 11397813
DOI: 10.1074/JBC.M104103200