Chlorine in PDB 4wrx: Crystal Structure of Mycobacterium Tuberculosis Uracil-Dna Glycosylase, Form V

All present enzymatic activity of Crystal Structure of Mycobacterium Tuberculosis Uracil-Dna Glycosylase, Form V:
3.2.2.27;

The structure of Crystal Structure of Mycobacterium Tuberculosis Uracil-Dna Glycosylase, Form V, PDB code: 4wrx was solved by S.M.Arif, K.Geethanandan, P.Mishra, A.Surolia, U.Varshney, M.Vijayan, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	40.87 / 1.40
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	36.890, 45.000, 122.610, 90.00, 90.00, 90.00
R / Rfree (%)	12.4 / 14.8

The binding sites of Chlorine atom in the Crystal Structure of Mycobacterium Tuberculosis Uracil-Dna Glycosylase, Form V (pdb code 4wrx). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 3 binding sites of Chlorine where determined in the Crystal Structure of Mycobacterium Tuberculosis Uracil-Dna Glycosylase, Form V, PDB code: 4wrx:
Jump to Chlorine binding site number: 1; 2; 3;

Chlorine binding site 1 out of 3 in the Crystal Structure of Mycobacterium Tuberculosis Uracil-Dna Glycosylase, Form V


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 Mycobacterium Tuberculosis Uracil-Dna Glycosylase, Form V within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl301 b:18.0 occ:1.00 NH2 A:ARG33 3.2 19.3 1.0 O A:HOH589 3.4 19.5 1.0 CB A:ALA-1 3.5 14.4 1.0 CA A:ALA-1 3.7 13.3 1.0 CD A:ARG33 3.8 19.5 1.0 CG A:ARG33 4.0 16.7 1.0 CZ A:ARG33 4.2 19.7 1.0 N A:ALA-1 4.3 13.7 1.0 NE A:ARG33 4.4 28.2 1.0 CE A:MET-2 4.5 18.1 1.0 C A:ALA-1 4.9 13.8 1.0 CG A:MET-2 4.9 26.7 1.0

Chlorine binding site 2 out of 3 in the Crystal Structure of Mycobacterium Tuberculosis Uracil-Dna Glycosylase, Form V


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Crystal Structure of Mycobacterium Tuberculosis Uracil-Dna Glycosylase, Form V within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl302 b:24.5 occ:1.00 N A:ARG41 3.2 11.2 1.0 NE A:ARG133 3.2 24.2 1.0 O A:HOH430 3.4 24.9 1.0 O A:HOH411 3.4 33.6 1.0 O A:HOH475 3.5 17.6 1.0 CA A:ARG40 3.8 11.8 1.0 NH2 A:ARG133 3.9 29.9 1.0 CB A:ARG41 3.9 11.7 1.0 C A:ARG40 4.0 10.3 1.0 CG A:ARG133 4.0 13.0 1.0 CA A:ARG41 4.0 12.2 1.0 CZ A:ARG133 4.0 25.6 1.0 CB A:ARG40 4.0 13.7 1.0 O A:ARG41 4.1 10.8 1.0 CD A:ARG133 4.2 17.8 1.0 CD A:PRO134 4.2 14.6 1.0 CG A:ARG41 4.3 11.8 1.0 CG A:PRO134 4.4 15.9 1.0 C A:ARG41 4.5 11.2 1.0 CG A:ARG40 4.5 15.1 1.0 O A:GLY39 4.8 13.9 1.0

Chlorine binding site 3 out of 3 in the Crystal Structure of Mycobacterium Tuberculosis Uracil-Dna Glycosylase, Form V


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 3 of Crystal Structure of Mycobacterium Tuberculosis Uracil-Dna Glycosylase, Form V within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl303 b:13.1 occ:1.00 O A:HOH554 3.2 12.2 1.0 O A:HOH549 3.2 10.2 1.0 O A:HOH563 3.3 16.2 1.0 ND2 A:ASN127 3.3 8.6 1.0 N A:TYR70 3.5 8.2 1.0 N A:PHE81 3.5 9.1 1.0 CA A:PRO69 3.6 10.7 1.0 CD2 A:TYR70 3.6 9.2 1.0 CE2 A:TYR70 4.0 11.0 1.0 O A:LEU79 4.0 10.9 1.0 CA A:SER80 4.0 7.3 1.0 C A:PRO69 4.0 9.2 1.0 CG A:TYR70 4.2 10.4 1.0 CB A:PRO69 4.2 11.2 1.0 C A:SER80 4.2 8.4 1.0 CB A:ALA76 4.3 10.8 1.0 CA A:PHE81 4.3 9.8 1.0 O A:HOH580 4.3 18.5 1.0 CG A:ASN127 4.4 8.3 1.0 O A:ASP68 4.5 12.3 1.0 C A:LEU79 4.5 9.7 1.0 CA A:ALA76 4.6 10.2 1.0 CB A:TYR70 4.6 9.7 1.0 CA A:TYR70 4.6 7.8 1.0 OD1 A:ASN127 4.6 10.6 1.0 N A:SER80 4.6 9.2 1.0 O A:SER82 4.7 12.2 1.0 N A:PRO69 4.7 9.8 1.0 O A:HOH556 4.8 9.3 1.0 C A:PHE81 4.8 9.1 1.0 N A:SER82 4.8 10.2 1.0 CZ A:TYR70 4.8 10.3 1.0 C A:ASP68 5.0 10.3 1.0

S.M.Arif, K.Geethanandan, P.Mishra, A.Surolia, U.Varshney, M.Vijayan. Structural Plasticity in Mycobacterium Tuberculosis Uracil-Dna Glycosylase (Mtung) and Its Functional Implications. Acta Crystallogr.,Sect.D V. 71 1514 2015.
ISSN: ESSN 1399-0047
PubMed: 26143923
DOI: 10.1107/S1399004715009311