Fluorine in PDB 1gfi: Structures of Active Conformations of Gi Alpha 1 and the Mechanism of Gtp Hydrolysis

The structure of Structures of Active Conformations of Gi Alpha 1 and the Mechanism of Gtp Hydrolysis, PDB code: 1gfi was solved by D.E.Coleman, A.M.Berghuis, S.R.Sprang, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	8.00 / 2.20
Space group	P 32 2 1
Cell size a, b, c (Å), α, β, γ (°)	80.500, 80.500, 106.550, 90.00, 90.00, 120.00
R / Rfree (%)	21.4 / 28.4

The structure of Structures of Active Conformations of Gi Alpha 1 and the Mechanism of Gtp Hydrolysis also contains other interesting chemical elements:

Magnesium	(Mg)	1 atom
Aluminium	(Al)	1 atom

The binding sites of Fluorine atom in the Structures of Active Conformations of Gi Alpha 1 and the Mechanism of Gtp Hydrolysis (pdb code 1gfi). This binding sites where shown within 5.0 Angstroms radius around Fluorine atom.
In total 4 binding sites of Fluorine where determined in the Structures of Active Conformations of Gi Alpha 1 and the Mechanism of Gtp Hydrolysis, PDB code: 1gfi:
Jump to Fluorine binding site number: 1; 2; 3; 4;

Fluorine binding site 1 out of 4 in the Structures of Active Conformations of Gi Alpha 1 and the Mechanism of Gtp Hydrolysis


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 1 of Structures of Active Conformations of Gi Alpha 1 and the Mechanism of Gtp Hydrolysis within 5.0Å range: probe atom residue distance (Å) B Occ A:F357 b:16.2 occ:1.00 F1 A:ALF357 0.0 16.2 1.0 AL A:ALF357 1.8 14.9 1.0 F2 A:ALF357 2.1 23.0 1.0 O A:HOH401 2.4 18.5 1.0 NE2 A:GLN204 2.6 21.4 1.0 NH2 A:ARG178 2.7 9.5 1.0 O3B A:GDP355 2.8 16.8 1.0 F4 A:ALF357 2.8 23.3 1.0 N A:GLU43 3.3 12.4 1.0 CD A:GLN204 3.3 26.8 1.0 OE1 A:GLN204 3.3 20.3 1.0 F3 A:ALF357 3.5 18.4 1.0 CA A:GLY42 3.5 14.6 1.0 CZ A:ARG178 3.5 9.0 1.0 NH1 A:ARG178 3.5 11.2 1.0 C A:GLY42 3.8 14.8 1.0 CG A:GLU43 3.9 17.0 1.0 PB A:GDP355 4.2 9.1 1.0 CA A:GLU43 4.2 14.2 1.0 O A:HOH461 4.5 21.3 1.0 CG A:LYS180 4.6 22.1 1.0 CB A:GLU43 4.7 14.1 1.0 CG A:GLN204 4.7 25.7 1.0 N A:GLY203 4.8 18.6 1.0 NE A:ARG178 4.8 3.6 1.0 O1B A:GDP355 4.8 11.2 1.0 N A:GLY42 4.9 17.7 1.0 N A:THR181 4.9 23.0 1.0 O A:GLY42 4.9 10.7 1.0 O A:HOH412 5.0 10.2 1.0 CD A:GLU43 5.0 15.4 1.0

Fluorine binding site 2 out of 4 in the Structures of Active Conformations of Gi Alpha 1 and the Mechanism of Gtp Hydrolysis


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 2 of Structures of Active Conformations of Gi Alpha 1 and the Mechanism of Gtp Hydrolysis within 5.0Å range: probe atom residue distance (Å) B Occ A:F357 b:23.0 occ:1.00 F2 A:ALF357 0.0 23.0 1.0 AL A:ALF357 1.9 14.9 1.0 F1 A:ALF357 2.1 16.2 1.0 O A:HOH401 2.2 18.5 1.0 F3 A:ALF357 2.5 18.4 1.0 O3B A:GDP355 2.8 16.8 1.0 NH2 A:ARG178 2.8 9.5 1.0 NH1 A:ARG178 2.9 11.2 1.0 N A:THR181 3.0 23.0 1.0 O A:HOH412 3.2 10.2 1.0 CZ A:ARG178 3.2 9.0 1.0 F4 A:ALF357 3.5 23.3 1.0 CA A:LYS180 3.5 20.0 1.0 MG A:MG356 3.6 14.8 1.0 C A:LYS180 3.7 21.9 1.0 CG A:LYS180 3.8 22.1 1.0 OG1 A:THR181 4.0 20.4 1.0 PB A:GDP355 4.0 9.1 1.0 CA A:THR181 4.0 21.6 1.0 CB A:THR181 4.1 20.7 1.0 O A:THR181 4.1 27.1 1.0 O A:VAL179 4.1 10.6 1.0 CB A:LYS180 4.2 18.1 1.0 NE2 A:GLN204 4.2 21.4 1.0 OE1 A:GLN204 4.2 20.3 1.0 O2B A:GDP355 4.3 13.1 1.0 NE A:ARG178 4.5 3.6 1.0 N A:LYS180 4.5 17.3 1.0 C A:THR181 4.6 24.9 1.0 O2A A:GDP355 4.7 9.1 1.0 CD A:GLN204 4.7 26.8 1.0 C A:VAL179 4.7 14.1 1.0 O3A A:GDP355 4.8 9.6 1.0 N A:GLU43 4.9 12.4 1.0 O A:LYS180 4.9 19.6 1.0 NZ A:LYS180 5.0 38.4 1.0

Fluorine binding site 3 out of 4 in the Structures of Active Conformations of Gi Alpha 1 and the Mechanism of Gtp Hydrolysis


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 3 of Structures of Active Conformations of Gi Alpha 1 and the Mechanism of Gtp Hydrolysis within 5.0Å range: probe atom residue distance (Å) B Occ A:F357 b:18.4 occ:1.00 F3 A:ALF357 0.0 18.4 1.0 AL A:ALF357 1.8 14.9 1.0 MG A:MG356 2.1 14.8 1.0 F2 A:ALF357 2.5 23.0 1.0 F4 A:ALF357 2.5 23.3 1.0 O A:HOH410 2.7 8.7 1.0 O A:HOH401 2.8 18.5 1.0 O3B A:GDP355 2.8 16.8 1.0 OG1 A:THR181 2.9 20.4 1.0 O2B A:GDP355 2.9 13.1 1.0 CB A:THR181 3.0 20.7 1.0 PB A:GDP355 3.1 9.1 1.0 O A:HOH412 3.4 10.2 1.0 F1 A:ALF357 3.5 16.2 1.0 O A:VAL201 3.6 24.3 1.0 N A:THR181 3.8 23.0 1.0 CA A:THR181 3.9 21.6 1.0 O1B A:GDP355 3.9 11.2 1.0 CA A:GLY202 4.0 17.8 1.0 CE A:LYS46 4.0 10.5 1.0 OG A:SER47 4.1 12.6 1.0 NZ A:LYS46 4.1 8.4 1.0 CG2 A:THR181 4.2 22.4 1.0 O A:THR181 4.2 27.1 1.0 N A:GLY203 4.4 18.6 1.0 C A:THR181 4.5 24.9 1.0 C A:VAL201 4.5 19.4 1.0 O3A A:GDP355 4.6 9.6 1.0 N A:GLY202 4.6 19.3 1.0 NH1 A:ARG178 4.7 11.2 1.0 C A:GLY202 4.7 19.3 1.0 C A:LYS180 5.0 21.9 1.0

Fluorine binding site 4 out of 4 in the Structures of Active Conformations of Gi Alpha 1 and the Mechanism of Gtp Hydrolysis


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 4 of Structures of Active Conformations of Gi Alpha 1 and the Mechanism of Gtp Hydrolysis within 5.0Å range: probe atom residue distance (Å) B Occ A:F357 b:23.3 occ:1.00 F4 A:ALF357 0.0 23.3 1.0 AL A:ALF357 1.8 14.9 1.0 N A:GLY203 2.4 18.6 1.0 O A:HOH401 2.5 18.5 1.0 F3 A:ALF357 2.5 18.4 1.0 F1 A:ALF357 2.8 16.2 1.0 NZ A:LYS46 3.0 8.4 1.0 O3B A:GDP355 3.2 16.8 1.0 CA A:GLY203 3.2 19.3 1.0 C A:GLY202 3.4 19.3 1.0 F2 A:ALF357 3.5 23.0 1.0 CA A:GLY42 3.5 14.6 1.0 CA A:GLY202 3.6 17.8 1.0 CE A:LYS46 3.7 10.5 1.0 OE1 A:GLN204 3.8 20.3 1.0 PB A:GDP355 3.9 9.1 1.0 O1B A:GDP355 4.0 11.2 1.0 N A:GLU43 4.0 12.4 1.0 O A:ALA41 4.0 17.1 1.0 O A:VAL201 4.1 24.3 1.0 C A:GLY203 4.1 20.3 1.0 N A:GLN204 4.2 21.0 1.0 N A:GLY42 4.2 17.7 1.0 C A:GLY42 4.3 14.8 1.0 NE2 A:GLN204 4.3 21.4 1.0 CD A:GLN204 4.4 26.8 1.0 C A:ALA41 4.4 16.5 1.0 O2B A:GDP355 4.5 13.1 1.0 O A:HOH410 4.5 8.7 1.0 MG A:MG356 4.5 14.8 1.0 O A:GLY202 4.6 20.5 1.0 N A:GLY202 4.7 19.3 1.0 O A:GLY40 4.8 19.0 1.0 C A:VAL201 4.9 19.4 1.0 O A:THR181 4.9 27.1 1.0

D.E.Coleman, A.M.Berghuis, E.Lee, M.E.Linder, A.G.Gilman, S.R.Sprang. Structures of Active Conformations of Gi Alpha 1 and the Mechanism of Gtp Hydrolysis. Science V. 265 1405 1994.
ISSN: ISSN 0036-8075
PubMed: 8073283