Fluorine in PDB 4gto: Ftase in Complex with Bms Analogue 14

All present enzymatic activity of Ftase in Complex with Bms Analogue 14:
2.5.1.58; 2.5.1.59;

The structure of Ftase in Complex with Bms Analogue 14, PDB code: 4gto was solved by Z.Guo, E.A.Stigter, R.S.Bon, H.Waldmann, W.Blankenfeldt, R.S.Goody, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	29.91 / 2.15
Space group	P 61
Cell size a, b, c (Å), α, β, γ (°)	172.704, 172.704, 69.586, 90.00, 90.00, 120.00
R / Rfree (%)	18.8 / 22.5

The structure of Ftase in Complex with Bms Analogue 14 also contains other interesting chemical elements:

Zinc

(Zn)

1 atom

The binding sites of Fluorine atom in the Ftase in Complex with Bms Analogue 14 (pdb code 4gto). This binding sites where shown within 5.0 Angstroms radius around Fluorine atom.
In total 3 binding sites of Fluorine where determined in the Ftase in Complex with Bms Analogue 14, PDB code: 4gto:
Jump to Fluorine binding site number: 1; 2; 3;

Fluorine binding site 1 out of 3 in the Ftase in Complex with Bms Analogue 14


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 1 of Ftase in Complex with Bms Analogue 14 within 5.0Å range: probe atom residue distance (Å) B Occ B:F502 b:95.8 occ:1.00 FAI B:7TO502 0.0 95.8 1.0 CBR B:7TO502 1.3 95.2 1.0 FAH B:7TO502 2.2 99.5 1.0 FAJ B:7TO502 2.2 0.9 1.0 SBS B:7TO502 2.6 85.3 1.0 OBE B:7TO502 3.0 71.8 1.0 OAE B:7TO502 3.2 82.2 1.0 CBI B:7TO502 3.3 64.6 1.0 CAP B:7TO502 3.3 64.3 1.0 CD B:ARG202 3.5 36.5 1.0 CB B:ARG202 3.7 31.4 1.0 OAD B:7TO502 3.8 86.6 1.0 SG B:CYS206 3.9 29.0 1.0 CG B:ARG202 4.0 34.0 1.0 NE B:ARG202 4.0 39.3 1.0 CZ2 B:TRP102 4.1 31.6 1.0 CAO B:7TO502 4.3 59.5 1.0 CAN B:7TO502 4.3 61.4 1.0 CH2 B:TRP102 4.5 31.1 1.0 CB B:ALA151 4.6 25.6 1.0 O B:ARG202 4.8 30.5 1.0 O B:HOH633 4.8 37.6 1.0 CA B:ARG202 4.8 31.9 1.0 O B:HOH602 4.9 31.8 1.0 C B:ARG202 5.0 30.6 1.0

Fluorine binding site 2 out of 3 in the Ftase in Complex with Bms Analogue 14


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 2 of Ftase in Complex with Bms Analogue 14 within 5.0Å range: probe atom residue distance (Å) B Occ B:F502 b:0.9 occ:1.00 FAJ B:7TO502 0.0 0.9 1.0 CBR B:7TO502 1.3 95.2 1.0 FAH B:7TO502 2.2 99.5 1.0 FAI B:7TO502 2.2 95.8 1.0 SBS B:7TO502 2.6 85.3 1.0 OAE B:7TO502 2.9 82.2 1.0 OAD B:7TO502 3.0 86.6 1.0 SG B:CYS206 3.4 29.0 1.0 CD2 B:TYR205 3.4 34.5 1.0 SG B:CYS254 3.6 32.4 1.0 O B:ARG202 3.7 30.5 1.0 CB B:ARG202 3.7 31.4 1.0 OBE B:7TO502 3.9 71.8 1.0 CG B:ARG202 4.0 34.0 1.0 CE2 B:TYR205 4.0 34.6 1.0 CA B:ARG202 4.1 31.9 1.0 CD B:ARG202 4.2 36.5 1.0 C B:ARG202 4.2 30.6 1.0 CG B:TYR205 4.5 33.9 1.0 CBI B:7TO502 4.6 64.6 1.0 NE B:ARG202 4.6 39.3 1.0 CB B:TYR205 4.7 34.3 1.0 N B:CYS206 4.7 32.6 1.0 CB B:CYS206 4.8 31.6 1.0 CB B:CYS254 5.0 31.4 1.0

Fluorine binding site 3 out of 3 in the Ftase in Complex with Bms Analogue 14


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 3 of Ftase in Complex with Bms Analogue 14 within 5.0Å range: probe atom residue distance (Å) B Occ B:F502 b:99.5 occ:1.00 FAH B:7TO502 0.0 99.5 1.0 CBR B:7TO502 1.3 95.2 1.0 FAJ B:7TO502 2.2 0.9 1.0 FAI B:7TO502 2.2 95.8 1.0 SBS B:7TO502 2.6 85.3 1.0 OAD B:7TO502 2.9 86.6 1.0 SG B:CYS206 3.1 29.0 1.0 OBE B:7TO502 3.2 71.8 1.0 CH2 B:TRP102 3.2 31.1 1.0 CZ2 B:TRP102 3.3 31.6 1.0 CD2 B:TYR154 3.6 28.4 1.0 OAE B:7TO502 3.8 82.2 1.0 CE2 B:TYR154 3.9 27.9 1.0 CG B:TYR154 4.0 28.8 1.0 CBI B:7TO502 4.1 64.6 1.0 CB B:TYR154 4.4 28.4 1.0 CAP B:7TO502 4.4 64.3 1.0 CA B:ALA151 4.6 26.5 1.0 CZ3 B:TRP102 4.6 31.6 1.0 CZ B:TYR154 4.6 28.9 1.0 CD1 B:TYR154 4.7 28.0 1.0 CE2 B:TRP102 4.7 32.6 1.0 CB B:ALA151 4.7 25.6 1.0 CD2 B:TYR205 4.7 34.5 1.0 O B:ALA151 4.8 26.3 1.0 CB B:CYS206 4.8 31.6 1.0 CE2 B:TYR205 4.9 34.6 1.0 CE1 B:TYR154 4.9 28.5 1.0

E.A.Stigter, Z.Guo, R.S.Bon, Y.W.Wu, A.Choidas, A.Wolf, S.Menninger, H.Waldmann, W.Blankenfeldt, R.S.Goody. Development of Selective, Potent Rabggtase Inhibitors J.Med.Chem. V. 55 8330 2012.
ISSN: ISSN 0022-2623
PubMed: 22963166
DOI: 10.1021/JM300624S