Fluorine in PDB 4y24: Complex of Human Galectin-1 and Td-139

The structure of Complex of Human Galectin-1 and Td-139, PDB code: 4y24 was solved by H.Y.Lin, T.J.Hsieh, C.H.Lin, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	29.54 / 2.32
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	43.578, 58.242, 110.976, 90.00, 90.00, 90.00
R / Rfree (%)	20 / 24.8

The binding sites of Fluorine atom in the Complex of Human Galectin-1 and Td-139 (pdb code 4y24). This binding sites where shown within 5.0 Angstroms radius around Fluorine atom.
In total 4 binding sites of Fluorine where determined in the Complex of Human Galectin-1 and Td-139, PDB code: 4y24:
Jump to Fluorine binding site number: 1; 2; 3; 4;

Fluorine binding site 1 out of 4 in the Complex of Human Galectin-1 and Td-139


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 1 of Complex of Human Galectin-1 and Td-139 within 5.0Å range: probe atom residue distance (Å) B Occ A:F201 b:57.4 occ:1.00 F18 A:TD2201 0.0 57.4 1.0 C14 A:TD2201 1.3 60.0 1.0 C15 A:TD2201 2.3 63.6 1.0 C13 A:TD2201 2.4 58.3 1.0 C16 A:TD2201 3.5 62.4 1.0 C12 A:TD2201 3.6 55.5 1.0 C17 A:TD2201 4.1 58.9 1.0 OD1 A:ASP54 4.5 58.1 1.0 NH1 A:ARG73 4.7 31.8 1.0 C9 A:TD2201 4.9 50.4 1.0

Fluorine binding site 2 out of 4 in the Complex of Human Galectin-1 and Td-139


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 2 of Complex of Human Galectin-1 and Td-139 within 5.0Å range: probe atom residue distance (Å) B Occ A:F201 b:50.2 occ:1.00 F28 A:TD2201 0.0 50.2 1.0 C26 A:TD2201 1.3 47.5 1.0 C25 A:TD2201 2.3 44.8 1.0 C27 A:TD2201 2.4 47.0 1.0 OG A:SER29 3.2 36.1 1.0 C24 A:TD2201 3.6 43.9 1.0 C22 A:TD2201 3.6 46.0 1.0 CA A:GLY124 3.6 27.0 1.0 CA A:PHE30 3.6 18.5 1.0 O A:SER29 3.6 28.3 1.0 C A:SER29 3.7 27.3 1.0 CG2 A:VAL31 3.8 16.4 1.0 N A:PHE30 3.8 20.8 1.0 C A:PHE30 3.9 17.8 1.0 C23 A:TD2201 4.0 44.4 1.0 CB A:SER29 4.1 34.1 1.0 N A:GLY124 4.1 25.3 1.0 ND2 A:ASN46 4.2 23.1 1.0 N A:VAL31 4.3 17.2 1.0 O A:PHE30 4.4 14.2 1.0 O A:ASP123 4.5 28.5 1.0 CB A:VAL31 4.5 15.3 1.0 CA A:SER29 4.5 30.1 1.0 C A:ASP123 4.5 27.9 1.0 C A:GLY124 4.9 27.2 1.0 C10 A:TD2201 4.9 44.6 1.0 CB A:PHE30 5.0 20.6 1.0

Fluorine binding site 3 out of 4 in the Complex of Human Galectin-1 and Td-139


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 3 of Complex of Human Galectin-1 and Td-139 within 5.0Å range: probe atom residue distance (Å) B Occ B:F201 b:50.4 occ:1.00 F18 B:TD2201 0.0 50.4 1.0 C14 B:TD2201 1.3 54.9 1.0 C15 B:TD2201 2.3 61.2 1.0 C13 B:TD2201 2.4 54.4 1.0 C16 B:TD2201 3.5 64.7 1.0 C12 B:TD2201 3.6 58.5 1.0 CD B:ARG73 3.7 29.5 1.0 NE B:ARG73 4.0 31.1 1.0 C17 B:TD2201 4.0 63.7 1.0 CZ B:ARG73 4.5 32.3 1.0 NH1 B:ARG73 4.6 42.1 1.0 C9 B:TD2201 4.9 57.4 1.0

Fluorine binding site 4 out of 4 in the Complex of Human Galectin-1 and Td-139


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 4 of Complex of Human Galectin-1 and Td-139 within 5.0Å range: probe atom residue distance (Å) B Occ B:F201 b:66.2 occ:1.00 F28 B:TD2201 0.0 66.2 1.0 C26 B:TD2201 1.3 63.7 1.0 C25 B:TD2201 2.3 63.2 1.0 C27 B:TD2201 2.4 60.6 1.0 OG B:SER29 3.1 28.9 1.0 O B:SER29 3.2 34.0 1.0 C B:SER29 3.4 32.4 1.0 CA B:PHE30 3.5 25.4 1.0 CA B:GLY124 3.5 31.8 1.0 C24 B:TD2201 3.6 60.6 1.0 C22 B:TD2201 3.6 58.4 1.0 N B:PHE30 3.7 26.2 1.0 C B:PHE30 3.8 23.9 1.0 CG2 B:VAL31 3.9 28.9 1.0 C23 B:TD2201 4.0 58.8 1.0 CB B:SER29 4.1 30.0 1.0 N B:VAL31 4.1 23.4 1.0 N B:GLY124 4.1 32.1 1.0 ND2 B:ASN46 4.2 23.2 1.0 O B:ASP123 4.3 34.9 1.0 CA B:SER29 4.3 31.9 1.0 O B:PHE30 4.4 23.6 1.0 C B:ASP123 4.5 32.1 1.0 CB B:VAL31 4.5 24.2 1.0 C B:GLY124 4.8 32.2 1.0 CB B:PHE30 4.8 20.3 1.0 C10 B:TD2201 4.9 56.6 1.0 N B:ASP125 4.9 30.6 1.0 CA B:VAL31 4.9 23.4 1.0 N B:SER29 4.9 31.7 1.0

T.J.Hsieh, H.Y.Lin, Z.Tu, T.C.Lin, S.C.Wu, Y.Y.Tseng, F.T.Liu, S.T.Hsu, C.H.Lin. Dual Thio-Digalactoside-Binding Modes of Human Galectins As the Structural Basis For the Design of Potent and Selective Inhibitors. Sci Rep V. 6 29457 2016.
ISSN: ESSN 2045-2322
PubMed: 27416897
DOI: 10.1038/SREP29457