Chlorine in PDB 2uy3: SCCTS1_8-Chlorotheophylline Crystal Structure

All present enzymatic activity of SCCTS1_8-Chlorotheophylline Crystal Structure:
3.2.1.14;

The structure of SCCTS1_8-Chlorotheophylline Crystal Structure, PDB code: 2uy3 was solved by R.Hurtado-Guerrero, D.M.F.Van Aalten, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	20.00 / 1.90
Space group	P 21 21 2
Cell size a, b, c (Å), α, β, γ (°)	73.411, 112.709, 37.331, 90.00, 90.00, 90.00
R / Rfree (%)	19.8 / 25.9

The binding sites of Chlorine atom in the SCCTS1_8-Chlorotheophylline Crystal Structure (pdb code 2uy3). 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 SCCTS1_8-Chlorotheophylline Crystal Structure, PDB code: 2uy3:

Chlorine binding site 1 out of 1 in the SCCTS1_8-Chlorotheophylline Crystal Structure


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of SCCTS1_8-Chlorotheophylline Crystal Structure within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl1311 b:5.0 occ:1.00 CL A:H331311 0.0 5.0 1.0 C8 A:H331311 1.5 9.3 1.0 N9 A:H331311 2.5 9.8 1.0 N7 A:H331311 2.6 10.7 1.0 O A:HOH2129 3.0 13.7 1.0 NE2 A:GLN212 3.2 12.3 1.0 CD A:GLN212 3.4 9.5 1.0 OH A:TYR214 3.5 13.3 1.0 OD2 A:ASP155 3.6 14.2 1.0 C4 A:H331311 3.6 10.4 1.0 C3 A:H331311 3.7 10.5 1.0 CG A:GLN212 3.8 9.3 1.0 CZ A:TYR32 3.8 15.2 1.0 OD1 A:ASP155 3.8 11.1 1.0 OE1 A:GLN212 3.9 14.5 1.0 CE1 A:TYR32 3.9 15.8 1.0 OH A:TYR32 3.9 16.2 1.0 CG A:ASP155 3.9 12.8 1.0 O A:HOH2133 4.0 15.5 1.0 CB A:ALA187 4.1 11.4 1.0 OE2 A:GLU157 4.1 18.0 1.0 CE2 A:TYR32 4.4 13.8 1.0 CD1 A:TYR32 4.5 14.5 1.0 CE3 A:TRP285 4.6 7.2 1.0 CZ A:TYR214 4.8 15.2 1.0 O A:HOH2131 4.8 15.1 1.0 O A:ALA187 4.9 10.1 1.0 N5 A:H331311 5.0 9.4 1.0 CD2 A:TYR32 5.0 12.7 1.0

R.Hurtado-Guerrero, D.M.F.Van Aalten. Structure of Saccharomyces Cerevisiae Chitinase 1 and Screening-Based Discovery of Potent Inhibitors. Chem.Biol. V. 14 589 2007.
ISSN: ISSN 1074-5521
PubMed: 17524989
DOI: 10.1016/J.CHEMBIOL.2007.03.015