Chlorine in PDB 5otn: Crystal Structure of Zebrafish MTH1 in Complex with O6-Methyl-Dgmp

The structure of Crystal Structure of Zebrafish MTH1 in Complex with O6-Methyl-Dgmp, PDB code: 5otn was solved by R.Gustafsson, L.Henriksson, A.-S.Jemth, L.Brautigam, J.Carreras Puigvert, E.Homan, U.Warpman Berglund, T.Helleday, P.Stenmark, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	28.32 / 0.99
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	44.528, 55.379, 65.920, 90.00, 90.00, 90.00
R / Rfree (%)	12.1 / 13.3

The structure of Crystal Structure of Zebrafish MTH1 in Complex with O6-Methyl-Dgmp also contains other interesting chemical elements:

Calcium

(Ca)

3 atoms

The binding sites of Chlorine atom in the Crystal Structure of Zebrafish MTH1 in Complex with O6-Methyl-Dgmp (pdb code 5otn). 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 Zebrafish MTH1 in Complex with O6-Methyl-Dgmp, PDB code: 5otn:

Chlorine binding site 1 out of 1 in the Crystal Structure of Zebrafish MTH1 in Complex with O6-Methyl-Dgmp


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 Zebrafish MTH1 in Complex with O6-Methyl-Dgmp within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl217 b:7.7 occ:0.70 O A:HOH422 3.2 13.7 1.0 CA A:GLY26 3.5 8.5 1.0 C3 A:GOL205 3.6 7.2 1.0 N A:GLY26 3.7 8.4 1.0 C1 A:GOL205 3.9 7.2 1.0 CD A:ARG25 3.9 11.2 1.0 C2 A:GOL205 4.1 6.9 1.0 CG A:ARG25 4.3 11.2 1.0 CB A:ARG25 4.4 10.1 1.0 C A:ARG25 4.4 8.1 1.0 O3 A:GOL205 4.6 6.9 1.0 NE A:ARG25 4.6 9.7 1.0 O1 A:GOL205 4.8 6.9 1.0 C A:GLY26 4.9 7.8 1.0

A.S.Jemth, R.Gustafsson, L.Brautigam, L.Henriksson, K.S.A.Vallin, A.Sarno, I.Almlof, E.Homan, A.Rasti, U.Warpman Berglund, P.Stenmark, T.Helleday. Mutt Homologue 1 (MTH1) Catalyzes the Hydrolysis of Mutagenic O6-Methyl-Dgtp. Nucleic Acids Res. V. 46 10888 2018.
ISSN: ESSN 1362-4962
PubMed: 30304478
DOI: 10.1093/NAR/GKY896