Chlorine in PDB 2vfv: Alditol Oxidase From Streptomyces Coelicolor A3(2): Complex with Sulphite

All present enzymatic activity of Alditol Oxidase From Streptomyces Coelicolor A3(2): Complex with Sulphite:
1.1.3.41;

The structure of Alditol Oxidase From Streptomyces Coelicolor A3(2): Complex with Sulphite, PDB code: 2vfv was solved by F.Forneris, A.Mattevi, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	19.51 / 1.72
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	105.561, 68.455, 57.965, 90.00, 95.19, 90.00
R / Rfree (%)	15.2 / 18.4

The binding sites of Chlorine atom in the Alditol Oxidase From Streptomyces Coelicolor A3(2): Complex with Sulphite (pdb code 2vfv). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total only one binding site of Chlorine was determined in the Alditol Oxidase From Streptomyces Coelicolor A3(2): Complex with Sulphite, PDB code: 2vfv:

Chlorine binding site 1 out of 1 in the Alditol Oxidase From Streptomyces Coelicolor A3(2): Complex with Sulphite


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Alditol Oxidase From Streptomyces Coelicolor A3(2): Complex with Sulphite within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl1419 b:9.7 occ:1.00 O A:HOH2320 3.2 15.6 1.0 N A:LEU192 3.2 6.5 1.0 N A:ALA193 3.2 7.0 1.0 CB A:PRO219 3.6 8.1 1.0 C A:PRO219 3.7 7.7 1.0 CA A:PRO191 3.7 7.6 1.0 CB A:ALA193 3.8 7.0 1.0 N A:GLY220 3.8 8.1 1.0 CB A:PRO191 3.8 7.9 1.0 O A:PRO219 3.9 8.3 1.0 C A:PRO191 3.9 6.4 1.0 CA A:GLY220 3.9 6.9 1.0 CA A:LEU192 4.0 6.5 1.0 C A:LEU192 4.1 6.7 1.0 CA A:ALA193 4.1 7.2 1.0 CB A:LEU192 4.2 5.8 1.0 CA A:PRO219 4.3 8.1 1.0 O A:HOH2321 4.5 17.9 1.0 O A:HOH2127 4.7 23.6 1.0 CG A:PRO219 5.0 8.5 1.0

F.Forneris, D.P.H.M.Heuts, M.Delvecchio, S.Rovida, M.W.Fraaije, A.Mattevi. Structural Analysis of the Catalytic Mechanism and Stereoselectivity in Streptomyces Coelicolor Alditol Oxidase. Biochemistry V. 47 978 2008.
ISSN: ISSN 0006-2960
PubMed: 18154360
DOI: 10.1021/BI701886T