Fluorine in PDB 6qxg: Crystal Structure of His-Tag Human Thymidylate Synthase (Ht-Hts) in Complex with Fdump

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

The structure of Crystal Structure of His-Tag Human Thymidylate Synthase (Ht-Hts) in Complex with Fdump, PDB code: 6qxg 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)	32.36 / 2.08
Space group	I 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	103.220, 61.980, 169.363, 90.00, 98.96, 90.00
R / Rfree (%)	18.1 / 22.5

The binding sites of Fluorine atom in the Crystal Structure of His-Tag Human Thymidylate Synthase (Ht-Hts) in Complex with Fdump (pdb code 6qxg). This binding sites where shown within 5.0 Angstroms radius around Fluorine atom.
In total 3 binding sites of Fluorine where determined in the Crystal Structure of His-Tag Human Thymidylate Synthase (Ht-Hts) in Complex with Fdump, PDB code: 6qxg:
Jump to Fluorine binding site number: 1; 2; 3;

Fluorine binding site 1 out of 3 in the Crystal Structure of His-Tag Human Thymidylate Synthase (Ht-Hts) in Complex with Fdump


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 1 of Crystal Structure of His-Tag Human Thymidylate Synthase (Ht-Hts) in Complex with Fdump within 5.0Å range: probe atom residue distance (Å) B Occ A:F401 b:0.4 occ:1.00 F5 A:UFP401 0.0 0.4 1.0 C5 A:UFP401 1.3 75.4 1.0 C6 A:UFP401 2.4 74.4 1.0 C4 A:UFP401 2.4 68.7 1.0 O4 A:UFP401 2.7 68.8 1.0 O A:HOH505 2.9 81.3 1.0 O A:HOH594 3.2 86.0 1.0 N1 A:UFP401 3.6 70.0 1.0 SG A:CYS195 3.6 90.5 1.0 N3 A:UFP401 3.6 64.3 1.0 O A:HOH610 3.7 78.9 1.0 O A:HOH625 3.8 87.4 1.0 C2 A:UFP401 4.1 69.0 1.0 CB A:CYS195 4.1 71.0 1.0 O A:HOH604 4.4 90.7 1.0 O A:HOH607 4.6 80.0 1.0 O4' A:UFP401 4.6 67.1 1.0 C1' A:UFP401 4.8 69.0 1.0

Fluorine binding site 2 out of 3 in the Crystal Structure of His-Tag Human Thymidylate Synthase (Ht-Hts) in Complex with Fdump


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 2 of Crystal Structure of His-Tag Human Thymidylate Synthase (Ht-Hts) in Complex with Fdump within 5.0Å range: probe atom residue distance (Å) B Occ B:F401 b:0.0 occ:1.00 F5 B:UFP401 0.0 0.0 1.0 C5 B:UFP401 1.3 81.3 1.0 C4 B:UFP401 2.4 82.1 1.0 C6 B:UFP401 2.4 76.1 1.0 O4 B:UFP401 2.7 76.7 1.0 O B:HOH613 3.0 93.8 1.0 O B:HOH508 3.0 80.1 1.0 SG B:CYS195 3.4 94.7 1.0 N3 B:UFP401 3.6 68.8 1.0 N1 B:UFP401 3.6 73.1 1.0 O B:HOH568 3.6 81.1 1.0 CB B:CYS195 3.9 78.2 1.0 O B:HOH626 4.0 92.6 1.0 C2 B:UFP401 4.1 70.4 1.0 N B:CYS195 4.7 73.0 1.0 O4' B:UFP401 4.7 69.1 1.0 O B:HOH596 4.8 83.2 1.0 C1' B:UFP401 4.8 67.4 1.0 CA B:CYS195 5.0 75.8 1.0 CE1 B:HIS196 5.0 87.8 1.0 OH B:TYR135 5.0 68.6 1.0

Fluorine binding site 3 out of 3 in the Crystal Structure of His-Tag Human Thymidylate Synthase (Ht-Hts) in Complex with Fdump


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 3 of Crystal Structure of His-Tag Human Thymidylate Synthase (Ht-Hts) in Complex with Fdump within 5.0Å range: probe atom residue distance (Å) B Occ C:F401 b:0.0 occ:1.00 F5 C:UFP401 0.0 0.0 1.0 C5 C:UFP401 1.4 89.2 1.0 C6 C:UFP401 2.5 77.0 1.0 C4 C:UFP401 2.5 73.9 1.0 O4 C:UFP401 2.7 76.6 1.0 O C:HOH506 2.9 72.1 1.0 O C:HOH616 3.5 84.6 1.0 SG C:CYS195 3.6 0.1 1.0 N1 C:UFP401 3.7 73.2 1.0 N3 C:UFP401 3.7 70.2 1.0 C2 C:UFP401 4.1 65.2 1.0 O C:HOH639 4.2 0.1 1.0 O C:HOH618 4.3 79.7 1.0 O C:HOH632 4.4 91.7 1.0 CB C:CYS195 4.4 79.3 1.0 O4' C:UFP401 4.8 66.7 1.0 C1' C:UFP401 4.9 68.2 1.0 N C:CYS195 5.0 72.3 1.0 O C:HOH619 5.0 80.2 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