Arsenic in PDB 2i0k: Cholesterol Oxidase From Brevibacterium Sterolicum- HIS121ALA Mutant

All present enzymatic activity of Cholesterol Oxidase From Brevibacterium Sterolicum- HIS121ALA Mutant:
1.1.3.6;

The structure of Cholesterol Oxidase From Brevibacterium Sterolicum- HIS121ALA Mutant, PDB code: 2i0k was solved by A.Vrielink, L.Lim, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	72.55 / 1.60
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	140.635, 85.851, 78.755, 90.00, 112.48, 90.00
R / Rfree (%)	14.8 / 16.7

The structure of Cholesterol Oxidase From Brevibacterium Sterolicum- HIS121ALA Mutant also contains other interesting chemical elements:

Manganese

(Mn)

2 atoms

The binding sites of Arsenic atom in the Cholesterol Oxidase From Brevibacterium Sterolicum- HIS121ALA Mutant (pdb code 2i0k). This binding sites where shown within 5.0 Angstroms radius around Arsenic atom.
In total 2 binding sites of Arsenic where determined in the Cholesterol Oxidase From Brevibacterium Sterolicum- HIS121ALA Mutant, PDB code: 2i0k:
Jump to Arsenic binding site number: 1; 2;

Arsenic binding site 1 out of 2 in the Cholesterol Oxidase From Brevibacterium Sterolicum- HIS121ALA Mutant


Mono view


Stereo pair view

A full contact list of Arsenic with other atoms in the As binding site number 1 of Cholesterol Oxidase From Brevibacterium Sterolicum- HIS121ALA Mutant within 5.0Å range: probe atom residue distance (Å) B Occ A:As703 b:15.6 occ:1.00 AS A:CAC703 0.0 15.6 1.0 O1 A:CAC703 1.7 12.6 1.0 O2 A:CAC703 1.7 14.2 1.0 C1 A:CAC703 1.9 14.3 1.0 C2 A:CAC703 2.0 14.1 1.0 MN A:MN701 3.5 11.3 1.0 O A:HOH1068 3.6 14.2 1.0 OD1 A:ASN542 3.8 8.6 1.0 O A:HOH1060 3.8 13.4 1.0 O A:HOH1135 3.9 17.7 1.0 O A:HOH1082 4.1 14.0 1.0 O A:HOH1074 4.3 11.6 1.0 O A:ASN542 4.4 8.8 1.0 CG A:ASN542 4.6 7.9 1.0 C A:ASN542 4.6 7.8 1.0 CA A:ASN543 4.7 8.2 1.0 N A:ASN543 4.7 7.8 1.0 OE2 A:GLU579 4.7 12.6 1.0 ND2 A:ASN542 5.0 9.9 1.0

Arsenic binding site 2 out of 2 in the Cholesterol Oxidase From Brevibacterium Sterolicum- HIS121ALA Mutant


Mono view


Stereo pair view

A full contact list of Arsenic with other atoms in the As binding site number 2 of Cholesterol Oxidase From Brevibacterium Sterolicum- HIS121ALA Mutant within 5.0Å range: probe atom residue distance (Å) B Occ A:As705 b:27.4 occ:1.00 AS A:CAC705 0.0 27.4 1.0 O2 A:CAC705 1.7 25.4 1.0 O1 A:CAC705 1.8 25.8 1.0 C2 A:CAC705 2.0 27.2 1.0 C1 A:CAC705 2.0 25.4 1.0 NH2 A:ARG477 3.6 7.4 0.7 NZ A:LYS554 3.7 9.5 1.0 OE1 A:GLU432 3.7 13.7 1.0 NH2 A:ARG477 3.8 10.9 0.3 O A:HOH2319 3.9 34.5 1.0 OE1 A:GLU475 4.0 20.4 1.0 N5 A:FAD700 4.0 7.8 1.0 OE2 A:GLU432 4.1 10.9 1.0 O3 A:GOL706 4.3 42.7 1.0 CD A:GLU432 4.3 11.3 1.0 CZ A:ARG477 4.4 8.6 0.7 CZ A:ARG477 4.4 10.3 0.3 CE A:LYS554 4.5 9.5 1.0 C5X A:FAD700 4.5 7.5 1.0 C4X A:FAD700 4.5 6.1 1.0 C6 A:FAD700 4.6 8.3 1.0 O4 A:FAD700 4.7 7.7 1.0 C4 A:FAD700 4.7 7.8 1.0 O A:HOH1083 4.7 12.6 1.0 NH1 A:ARG477 4.8 8.1 0.3 CD1 A:ILE423 4.9 11.1 0.7 NE A:ARG477 5.0 7.4 0.7

L.Lim, G.Molla, N.Guinn, S.Ghisla, L.Pollegioni, A.Vrielink. Structural and Kinetic Analyses of the H121A Mutant of Cholesterol Oxidase. Biochem.J. V. 400 13 2006.
ISSN: ISSN 0264-6021
PubMed: 16856877
DOI: 10.1042/BJ20060664