Chlorine in PDB 2jhq: Crystal Structure of Uracil Dna-Glycosylase From Vibrio Cholerae

All present enzymatic activity of Crystal Structure of Uracil Dna-Glycosylase From Vibrio Cholerae:
3.2.2.3;

The structure of Crystal Structure of Uracil Dna-Glycosylase From Vibrio Cholerae, PDB code: 2jhq was solved by I.L.U.Raeder, E.Moe, N.P.Willassen, A.O.Smalas, I.Leiros, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	15.31 / 1.50
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	60.140, 60.440, 61.330, 90.00, 90.00, 90.00
R / Rfree (%)	17.5 / 21

The binding sites of Chlorine atom in the Crystal Structure of Uracil Dna-Glycosylase From Vibrio Cholerae (pdb code 2jhq). 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 Crystal Structure of Uracil Dna-Glycosylase From Vibrio Cholerae, PDB code: 2jhq:

Chlorine binding site 1 out of 1 in the Crystal Structure of Uracil Dna-Glycosylase From Vibrio Cholerae


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Crystal Structure of Uracil Dna-Glycosylase From Vibrio Cholerae within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl1227 b:11.9 occ:1.00 OG A:SER88 3.1 7.5 1.0 O A:HOH2059 3.1 25.9 1.0 N A:SER88 3.2 6.3 1.0 CB A:SER88 3.5 7.0 1.0 CD A:PRO87 3.7 7.8 1.0 CE1 A:TYR66 3.8 9.8 1.0 CA A:SER88 3.9 6.9 1.0 N A:PRO87 3.9 6.9 1.0 CB A:PRO87 4.1 7.9 1.0 C A:PRO87 4.2 6.5 1.0 CG A:PRO87 4.3 8.1 1.0 CB A:PRO86 4.3 6.8 1.0 CA A:PRO87 4.3 7.1 1.0 CD1 A:TYR66 4.5 9.2 1.0 C A:PRO86 4.5 6.0 1.0 O A:HOH2050 4.7 30.5 1.0 OH A:TYR66 4.8 9.1 1.0 CZ A:TYR66 4.8 9.1 1.0 CA A:PRO86 5.0 6.8 1.0

I.L.U.Raeder, E.Moe, N.P.Willassen, A.O.Smalas, I.Leiros. Structure of Uracil-Dna N-Glycosylase (Ung) From Vibrio Cholerae. Mapping Temperature Adaptation Through Structural and Mutational Analysis. Acta Crystallogr.,Sect.F V. 66 130 2010.
ISSN: ISSN 1744-3091
PubMed: 20124707
DOI: 10.1107/S1744309109052063