Chlorine in PDB 4o1u: Crystal Structure of Human Thymidylate Synthase Mutant Y202C

All present enzymatic activity of Crystal Structure of Human Thymidylate Synthase Mutant Y202C:
2.1.1.45;

The structure of Crystal Structure of Human Thymidylate Synthase Mutant Y202C, PDB code: 4o1u was solved by C.Pozzi, S.Mangani, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	48.12 / 2.26
Space group	P 31
Cell size a, b, c (Å), α, β, γ (°)	96.230, 96.230, 83.770, 90.00, 90.00, 120.00
R / Rfree (%)	17.2 / 21

The binding sites of Chlorine atom in the Crystal Structure of Human Thymidylate Synthase Mutant Y202C (pdb code 4o1u). 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 Human Thymidylate Synthase Mutant Y202C, PDB code: 4o1u:
Jump to Chlorine binding site number: 1; 2; 3;

Chlorine binding site 1 out of 3 in the Crystal Structure of Human Thymidylate Synthase Mutant Y202C


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 Human Thymidylate Synthase Mutant Y202C within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl405 b:61.8 occ:1.00 O A:HOH554 3.4 46.0 1.0 N A:PHE80 3.7 48.2 1.0 CB A:PHE80 4.2 50.4 1.0 CG1 A:VAL79 4.2 42.9 1.0 CA A:VAL79 4.2 43.9 1.0 CD2 A:PHE225 4.3 52.9 1.0 C A:VAL79 4.5 46.6 1.0 CA A:PHE80 4.6 48.4 1.0 O A:HOH518 4.6 49.0 1.0 CB A:VAL79 4.6 42.7 1.0 O A:ARG78 4.8 46.4 1.0 CG2 A:VAL79 4.9 41.6 1.0 CB A:PHE225 4.9 41.7 1.0 CE A:LYS77 4.9 41.3 1.0

Chlorine binding site 2 out of 3 in the Crystal Structure of Human Thymidylate Synthase Mutant Y202C


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 Human Thymidylate Synthase Mutant Y202C within 5.0Å range: probe atom residue distance (Å) B Occ B:Cl406 b:47.8 occ:1.00 O B:HOH522 3.1 44.4 1.0 N B:ASP218 3.2 34.8 1.0 CA B:GLY217 3.8 35.3 1.0 CB B:ASP218 3.8 36.5 1.0 CA B:GLY222 3.8 35.0 1.0 OD1 B:ASN226 4.0 45.7 1.0 C B:GLY217 4.1 35.6 1.0 CA B:ASP218 4.1 34.2 1.0 C B:GLY222 4.2 34.2 1.0 O B:HOH590 4.3 56.1 1.0 O B:ASP218 4.3 32.4 1.0 O B:SER216 4.4 35.4 1.0 N B:VAL223 4.6 32.9 1.0 C B:ASP218 4.6 33.4 1.0 O B:GLY222 4.8 35.6 1.0 N B:GLY222 4.8 36.0 1.0 NE2 B:GLN214 4.8 41.6 1.0 OE1 B:GLN214 4.8 41.3 1.0 N B:GLY217 4.9 34.7 1.0

Chlorine binding site 3 out of 3 in the Crystal Structure of Human Thymidylate Synthase Mutant Y202C


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 Human Thymidylate Synthase Mutant Y202C within 5.0Å range: probe atom residue distance (Å) B Occ B:Cl407 b:59.2 occ:1.00 O B:HOH520 3.2 43.8 1.0 N B:PHE80 3.8 49.3 1.0 CG1 B:VAL79 4.1 46.9 1.0 CA B:VAL79 4.1 45.6 1.0 CD2 B:PHE225 4.4 47.7 1.0 CB B:PHE80 4.4 53.7 1.0 C B:VAL79 4.5 47.2 1.0 O B:HOH516 4.6 52.1 1.0 CB B:VAL79 4.6 44.4 1.0 CA B:PHE80 4.7 49.9 1.0 CE B:LYS77 4.7 40.1 1.0 O B:ARG78 4.8 47.1 1.0 CB B:PHE225 4.9 39.6 1.0 NZ B:LYS77 4.9 39.0 1.0 CG2 B:VAL79 5.0 42.5 1.0

S.Ferrari, S.Mangani, C.Pozzi, M.P.Costi. Tethering the Dimer-Dimer Interface of Human Thymidylate Synthase To Be Published.