Fluorine in PDB 5y2i: Phosphoglycerate Mutase 1 (PGAM1) Complexed with Its Inhibitor Pgmi- 004A

All present enzymatic activity of Phosphoglycerate Mutase 1 (PGAM1) Complexed with Its Inhibitor Pgmi- 004A:
5.4.2.11; 5.4.2.4;

The structure of Phosphoglycerate Mutase 1 (PGAM1) Complexed with Its Inhibitor Pgmi- 004A, PDB code: 5y2i was solved by L.Jiang, L.Zhou, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	43.57 / 1.92
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	82.762, 85.036, 102.480, 90.00, 90.00, 90.00
R / Rfree (%)	19.1 / 21.4

The structure of Phosphoglycerate Mutase 1 (PGAM1) Complexed with Its Inhibitor Pgmi- 004A also contains other interesting chemical elements:

Chlorine

(Cl)

1 atom

The binding sites of Fluorine atom in the Phosphoglycerate Mutase 1 (PGAM1) Complexed with Its Inhibitor Pgmi- 004A (pdb code 5y2i). This binding sites where shown within 5.0 Angstroms radius around Fluorine atom.
In total 3 binding sites of Fluorine where determined in the Phosphoglycerate Mutase 1 (PGAM1) Complexed with Its Inhibitor Pgmi- 004A, PDB code: 5y2i:
Jump to Fluorine binding site number: 1; 2; 3;

Fluorine binding site 1 out of 3 in the Phosphoglycerate Mutase 1 (PGAM1) Complexed with Its Inhibitor Pgmi- 004A


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 1 of Phosphoglycerate Mutase 1 (PGAM1) Complexed with Its Inhibitor Pgmi- 004A within 5.0Å range: probe atom residue distance (Å) B Occ B:F301 b:52.9 occ:1.00 F01 B:8KX301 0.0 52.9 1.0 C B:8KX301 1.3 38.8 1.0 F02 B:8KX301 2.1 37.2 1.0 F B:8KX301 2.3 54.4 1.0 C18 B:8KX301 2.3 46.6 1.0 O B:HOH467 2.5 32.5 1.0 C17 B:8KX301 2.6 50.6 1.0 CD2 B:PHE22 3.0 30.3 1.0 N B:PHE22 3.0 22.1 1.0 CE2 B:PHE22 3.1 32.2 1.0 CG B:PHE22 3.2 29.5 1.0 O B:ASN20 3.4 24.5 1.0 CZ B:PHE22 3.4 36.3 1.0 C B:ASN20 3.5 29.4 1.0 CD1 B:PHE22 3.5 31.2 1.0 N B:ARG21 3.6 24.0 1.0 CE1 B:PHE22 3.6 37.7 1.0 O B:HOH540 3.6 38.6 1.0 C19 B:8KX301 3.6 49.9 1.0 C B:ARG21 3.7 27.4 1.0 CA B:PHE22 3.8 25.5 1.0 CA B:ARG21 3.8 23.6 1.0 CB B:PHE22 4.0 23.6 1.0 C16 B:8KX301 4.0 56.9 1.0 CA B:ASN20 4.2 27.1 1.0 O B:LEU98 4.4 24.9 1.0 O B:HOH539 4.5 48.1 1.0 O B:GLU19 4.6 29.0 1.0 O B:HOH446 4.7 44.0 1.0 C20 B:8KX301 4.7 56.4 1.0 O B:ARG21 4.8 22.4 1.0 C15 B:8KX301 4.9 59.4 1.0

Fluorine binding site 2 out of 3 in the Phosphoglycerate Mutase 1 (PGAM1) Complexed with Its Inhibitor Pgmi- 004A


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 2 of Phosphoglycerate Mutase 1 (PGAM1) Complexed with Its Inhibitor Pgmi- 004A within 5.0Å range: probe atom residue distance (Å) B Occ B:F301 b:37.2 occ:1.00 F02 B:8KX301 0.0 37.2 1.0 C B:8KX301 1.3 38.8 1.0 F B:8KX301 2.1 54.4 1.0 F01 B:8KX301 2.1 52.9 1.0 C18 B:8KX301 2.4 46.6 1.0 O B:GLU19 2.5 29.0 1.0 C B:ASN20 3.0 29.4 1.0 CA B:ASN20 3.0 27.1 1.0 N B:ARG21 3.1 24.0 1.0 N B:PHE22 3.1 22.1 1.0 C19 B:8KX301 3.2 49.9 1.0 C B:GLU19 3.2 28.4 1.0 C17 B:8KX301 3.3 50.6 1.0 N B:ASN20 3.5 25.9 1.0 O B:ASN20 3.6 24.5 1.0 CA B:PHE22 3.9 25.5 1.0 O B:HOH446 3.9 44.0 1.0 CA B:ARG21 3.9 23.6 1.0 C B:ARG21 4.0 27.4 1.0 O B:HOH467 4.2 32.5 1.0 CB B:ASN20 4.4 28.4 1.0 C20 B:8KX301 4.4 56.4 1.0 CA B:GLU19 4.4 23.4 1.0 O B:LEU18 4.5 25.1 1.0 CG B:PHE22 4.5 29.5 1.0 C16 B:8KX301 4.5 56.9 1.0 OD1 B:ASN20 4.6 31.8 1.0 CD1 B:PHE22 4.7 31.2 1.0 CD2 B:PHE22 4.8 30.3 1.0 CB B:PHE22 4.8 23.6 1.0 CG B:ASN20 5.0 30.8 1.0 C15 B:8KX301 5.0 59.4 1.0

Fluorine binding site 3 out of 3 in the Phosphoglycerate Mutase 1 (PGAM1) Complexed with Its Inhibitor Pgmi- 004A


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 3 of Phosphoglycerate Mutase 1 (PGAM1) Complexed with Its Inhibitor Pgmi- 004A within 5.0Å range: probe atom residue distance (Å) B Occ B:F301 b:54.4 occ:1.00 F B:8KX301 0.0 54.4 1.0 C B:8KX301 1.3 38.8 1.0 F02 B:8KX301 2.1 37.2 1.0 F01 B:8KX301 2.3 52.9 1.0 C18 B:8KX301 2.3 46.6 1.0 C19 B:8KX301 2.7 49.9 1.0 CD1 B:PHE22 2.8 31.2 1.0 CA B:PHE22 2.9 25.5 1.0 N B:PHE22 2.9 22.1 1.0 CG B:PHE22 3.0 29.5 1.0 CE1 B:PHE22 3.3 37.7 1.0 C17 B:8KX301 3.5 50.6 1.0 CB B:PHE22 3.5 23.6 1.0 CD2 B:PHE22 3.8 30.3 1.0 CZ B:PHE22 4.0 36.3 1.0 C20 B:8KX301 4.1 56.4 1.0 O B:GLU19 4.2 29.0 1.0 CE2 B:PHE22 4.2 32.2 1.0 C B:ARG21 4.2 27.4 1.0 C B:PHE22 4.3 25.6 1.0 CE2 B:TYR92 4.4 28.1 1.0 CZ B:TYR92 4.5 34.8 1.0 N B:ARG21 4.5 24.0 1.0 C16 B:8KX301 4.6 56.9 1.0 O B:HOH461 4.6 34.3 1.0 N B:SER23 4.6 26.0 1.0 O B:HOH467 4.7 32.5 1.0 CD2 B:TYR92 4.7 25.8 1.0 C B:ASN20 4.8 29.4 1.0 OH B:TYR92 4.8 33.2 1.0 CA B:ARG21 4.8 23.6 1.0 C15 B:8KX301 4.9 59.4 1.0 CE1 B:TYR92 4.9 31.2 1.0 C B:GLU19 4.9 28.4 1.0

L.Jiang, L.Zhou. Phosphoglycerate Mutase 1 (PGAM1) Complexed with Its Inhibitor Pgmi-004A To Be Published.