Fluorine in PDB 3h9k: Structures of Thymidylate Synthase R163K with Substrates and Inhibitors Show Subunit Asymmetry

All present enzymatic activity of Structures of Thymidylate Synthase R163K with Substrates and Inhibitors Show Subunit Asymmetry:
2.1.1.45;

The structure of Structures of Thymidylate Synthase R163K with Substrates and Inhibitors Show Subunit Asymmetry, PDB code: 3h9k was solved by L.M.Gibson, L.L.Lovelace, L.Lebioda, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	50.00 / 2.65
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	200.284, 122.190, 99.828, 90.00, 115.18, 90.00
R / Rfree (%)	21.4 / 26

The binding sites of Fluorine atom in the Structures of Thymidylate Synthase R163K with Substrates and Inhibitors Show Subunit Asymmetry (pdb code 3h9k). This binding sites where shown within 5.0 Angstroms radius around Fluorine atom.
In total 3 binding sites of Fluorine where determined in the Structures of Thymidylate Synthase R163K with Substrates and Inhibitors Show Subunit Asymmetry, PDB code: 3h9k:
Jump to Fluorine binding site number: 1; 2; 3;

Fluorine binding site 1 out of 3 in the Structures of Thymidylate Synthase R163K with Substrates and Inhibitors Show Subunit Asymmetry


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 1 of Structures of Thymidylate Synthase R163K with Substrates and Inhibitors Show Subunit Asymmetry within 5.0Å range: probe atom residue distance (Å) B Occ A:F400 b:0.1 occ:0.90 F5 A:UFP400 0.0 0.1 0.9 C5 A:UFP400 1.4 0.8 0.9 C6 A:UFP400 2.4 0.4 0.9 C4 A:UFP400 2.4 0.5 0.9 O4 A:UFP400 2.7 0.8 0.9 C1 A:EDO401 3.2 80.7 1.0 O1 A:EDO401 3.3 76.6 1.0 N1 A:UFP400 3.6 0.6 0.9 N3 A:UFP400 3.7 0.9 0.9 C2 A:UFP400 4.1 0.1 0.9 C2 A:EDO401 4.3 80.8 1.0 C1' A:UFP400 4.8 95.9 0.9

Fluorine binding site 2 out of 3 in the Structures of Thymidylate Synthase R163K with Substrates and Inhibitors Show Subunit Asymmetry


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 2 of Structures of Thymidylate Synthase R163K with Substrates and Inhibitors Show Subunit Asymmetry within 5.0Å range: probe atom residue distance (Å) B Occ B:F400 b:89.7 occ:0.50 F5 B:UFP400 0.0 89.7 0.5 C5 B:UFP400 1.3 88.6 0.5 C6 B:UFP400 2.4 88.3 0.5 C4 B:UFP400 2.4 88.3 0.5 O2 B:EDO401 2.6 73.1 1.0 O4 B:UFP400 2.7 88.5 0.5 N1 B:UFP400 3.6 87.9 0.5 N3 B:UFP400 3.7 87.1 0.5 C2 B:EDO401 4.0 78.1 1.0 C2 B:UFP400 4.1 87.2 0.5 O1 B:EDO401 4.8 83.1 1.0 C1' B:UFP400 4.8 87.4 0.5

Fluorine binding site 3 out of 3 in the Structures of Thymidylate Synthase R163K with Substrates and Inhibitors Show Subunit Asymmetry


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 3 of Structures of Thymidylate Synthase R163K with Substrates and Inhibitors Show Subunit Asymmetry within 5.0Å range: probe atom residue distance (Å) B Occ D:F565 b:0.3 occ:0.77 F5 D:UFP565 0.0 0.3 0.8 C5 D:UFP565 1.4 0.3 0.8 C6 D:UFP565 2.4 98.4 0.8 C4 D:UFP565 2.4 99.3 0.8 O4 D:UFP565 2.7 98.2 0.8 N1 D:UFP565 3.7 96.1 0.8 N3 D:UFP565 3.7 96.7 0.8 O D:HOH319 4.1 50.4 1.0 C2 D:UFP565 4.2 95.3 0.8 CG2 D:ILE108 4.5 89.9 1.0 C1' D:UFP565 4.8 93.6 0.8

L.M.Gibson, L.R.Celeste, L.L.Lovelace, L.Lebioda. Structures of Human Thymidylate Synthase R163K with Dump, Fdump and Glutathione Show Asymmetric Ligand Binding. Acta Crystallogr.,Sect.D V. 67 60 2011.
ISSN: ISSN 0907-4449
PubMed: 21206062
DOI: 10.1107/S0907444910044732