Chlorine in PDB 6qxh: Crystal Structure of His-Tag Human Thymidylate Synthase (Ht-Hts) in Complex with Dump

All present enzymatic activity of Crystal Structure of His-Tag Human Thymidylate Synthase (Ht-Hts) in Complex with Dump:
2.1.1.45;

The structure of Crystal Structure of His-Tag Human Thymidylate Synthase (Ht-Hts) in Complex with Dump, PDB code: 6qxh was solved by C.Pozzi, M.Mangani, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	34.19 / 2.04
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	182.110, 61.590, 101.100, 90.00, 115.38, 90.00
R / Rfree (%)	18.7 / 23.7

The binding sites of Chlorine atom in the Crystal Structure of His-Tag Human Thymidylate Synthase (Ht-Hts) in Complex with Dump (pdb code 6qxh). 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 His-Tag Human Thymidylate Synthase (Ht-Hts) in Complex with Dump, PDB code: 6qxh:

Chlorine binding site 1 out of 1 in the Crystal Structure of His-Tag Human Thymidylate Synthase (Ht-Hts) in Complex with Dump


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 His-Tag Human Thymidylate Synthase (Ht-Hts) in Complex with Dump within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl403 b:69.6 occ:1.00 N A:PHE80 3.2 61.3 1.0 CA A:VAL79 3.7 58.9 1.0 CG1 A:VAL79 3.7 59.9 1.0 CB A:PHE80 3.8 65.8 1.0 C A:VAL79 3.9 63.2 1.0 CA A:PHE80 4.1 65.1 1.0 CD2 A:PHE225 4.1 61.2 1.0 CB A:VAL79 4.2 61.1 1.0 CB A:PHE225 4.5 57.7 1.0 O A:ARG78 4.5 64.8 1.0 CE A:LYS77 4.5 62.1 1.0 CG2 A:VAL79 4.7 60.3 1.0 CG A:PHE225 4.8 59.2 1.0 N A:VAL79 4.9 59.2 1.0 O A:LEU221 4.9 63.3 1.0

C.Pozzi, S.Ferrari, R.Luciani, G.Tassone, M.P.Costi, S.Mangani. Structural Comparison Ofenterococcus Faecalisand Human Thymidylate Synthase Complexes with the Substrate Dump and Its Analogue Fdump Provides Hints About Enzyme Conformational Variabilities. Molecules V. 24 2019.
ISSN: ESSN 1420-3049
PubMed: 30935102
DOI: 10.3390/MOLECULES24071257