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Fluorine in PDB 3ejl: Replacement of VAL3 in Human Thymidylate Synthase Affects Its Kinetic Properties and Intracellular Stability

Enzymatic activity of Replacement of VAL3 in Human Thymidylate Synthase Affects Its Kinetic Properties and Intracellular Stability

All present enzymatic activity of Replacement of VAL3 in Human Thymidylate Synthase Affects Its Kinetic Properties and Intracellular Stability:
2.1.1.45;

Protein crystallography data

The structure of Replacement of VAL3 in Human Thymidylate Synthase Affects Its Kinetic Properties and Intracellular Stability, PDB code: 3ejl was solved by X.Huang, L.M.Gibson, B.J.Bell, L.L.Lovelace, M.M.Pena, F.G.Berger, S.H.Berger, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 50.00 / 3.20
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 157.435, 94.642, 131.988, 90.00, 122.35, 90.00
R / Rfree (%) 23.2 / 25.7

Fluorine Binding Sites:

The binding sites of Fluorine atom in the Replacement of VAL3 in Human Thymidylate Synthase Affects Its Kinetic Properties and Intracellular Stability (pdb code 3ejl). This binding sites where shown within 5.0 Angstroms radius around Fluorine atom.
In total only one binding site of Fluorine was determined in the Replacement of VAL3 in Human Thymidylate Synthase Affects Its Kinetic Properties and Intracellular Stability, PDB code: 3ejl:

Fluorine binding site 1 out of 1 in 3ejl

Go back to Fluorine Binding Sites List in 3ejl
Fluorine binding site 1 out of 1 in the Replacement of VAL3 in Human Thymidylate Synthase Affects Its Kinetic Properties and Intracellular Stability


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 1 of Replacement of VAL3 in Human Thymidylate Synthase Affects Its Kinetic Properties and Intracellular Stability within 5.0Å range:
probe atom residue distance (Å) B Occ
D:F314

b:97.0
occ:1.00
 F5 D:UFP314 0.0 97.0 1.0
C5 D:UFP314 1.4 95.1 1.0
C6 D:UFP314 2.4 93.8 1.0
C4 D:UFP314 2.4 95.2 1.0
O4 D:UFP314 2.7 96.1 1.0
NH1 C:ARG163 3.4 21.3 1.0
N1 D:UFP314 3.7 91.9 1.0
CG C:ARG176 3.7 94.5 1.0
N3 D:UFP314 3.7 93.2 1.0
O C:ARG176 4.0 70.4 1.0
C2 D:UFP314 4.2 92.0 1.0
CD C:ARG176 4.3 0.2 1.0
CB C:ARG176 4.3 80.3 1.0
CZ C:ARG163 4.5 21.3 1.0
NE C:ARG176 4.5 0.6 1.0
C1' D:UFP314 4.9 89.2 1.0
C C:ARG176 5.0 62.2 1.0
CD1 D:LEU187 5.0 0.8 1.0
C2' D:UFP314 5.0 87.8 1.0

Reference:

X.Huang, L.M.Gibson, B.J.Bell, L.L.Lovelace, M.M.Pena, F.G.Berger, S.H.Berger, L.Lebioda. Replacement of VAL3 in Human Thymidylate Synthase Affects Its Kinetic Properties and Intracellular Stability . Biochemistry V. 49 2475 2010.
ISSN: ISSN 0006-2960
PubMed: 20151707
DOI: 10.1021/BI901457E
Page generated: Mon Jul 14 16:06:30 2025

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