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Fluorine in PDB 3d7m: Crystal Structure of the G Protein Fast-Exchange Double Mutant I56C/Q333C

Protein crystallography data

The structure of Crystal Structure of the G Protein Fast-Exchange Double Mutant I56C/Q333C, PDB code: 3d7m was solved by M.A.Funk, A.M.Preininger, W.M.Oldham, S.M.Meier, H.E.Hamm, T.M.Iverson, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 50.00 / 2.90
Space group P 43 21 2
Cell size a, b, c (Å), α, β, γ (°) 79.659, 79.659, 114.587, 90.00, 90.00, 90.00
R / Rfree (%) 24.9 / 29.4

Other elements in 3d7m:

The structure of Crystal Structure of the G Protein Fast-Exchange Double Mutant I56C/Q333C also contains other interesting chemical elements:

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

Fluorine Binding Sites:

The binding sites of Fluorine atom in the Crystal Structure of the G Protein Fast-Exchange Double Mutant I56C/Q333C (pdb code 3d7m). This binding sites where shown within 5.0 Angstroms radius around Fluorine atom.
In total 4 binding sites of Fluorine where determined in the Crystal Structure of the G Protein Fast-Exchange Double Mutant I56C/Q333C, PDB code: 3d7m:
Jump to Fluorine binding site number: 1; 2; 3; 4;

Fluorine binding site 1 out of 4 in 3d7m

Go back to Fluorine Binding Sites List in 3d7m
Fluorine binding site 1 out of 4 in the Crystal Structure of the G Protein Fast-Exchange Double Mutant I56C/Q333C


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 1 of Crystal Structure of the G Protein Fast-Exchange Double Mutant I56C/Q333C within 5.0Å range:
probe atom residue distance (Å) B Occ
A:F357

b:95.9
occ:1.00
F1 A:ALF357 0.0 95.9 1.0
AL A:ALF357 1.7 95.6 1.0
F2 A:ALF357 2.4 94.7 1.0
F4 A:ALF357 2.5 97.0 1.0
NE2 A:GLN204 2.6 0.1 1.0
O3B A:GDP355 2.9 70.9 1.0
NH2 A:ARG178 3.0 64.8 1.0
N A:GLU43 3.1 74.0 1.0
F3 A:ALF357 3.4 95.8 1.0
CA A:GLY42 3.5 73.8 1.0
C A:GLY42 3.7 74.4 1.0
CD A:GLN204 3.8 0.2 1.0
NH1 A:ARG178 3.9 64.1 1.0
CZ A:ARG178 3.9 64.6 1.0
CG A:GLN204 4.2 0.2 1.0
CA A:GLU43 4.2 73.2 1.0
CG A:GLU43 4.2 72.8 1.0
PB A:GDP355 4.3 69.3 1.0
N A:GLY42 4.8 74.6 1.0
CB A:GLU43 4.8 72.3 1.0
O3A A:GDP355 4.8 66.7 1.0
OE1 A:GLN204 4.8 0.7 1.0
CG A:LYS180 4.8 81.4 1.0
O A:ALA41 4.9 77.8 1.0
N A:GLY203 4.9 0.2 1.0
NZ A:LYS46 4.9 64.8 1.0
N A:THR181 4.9 81.7 1.0
O A:GLY42 4.9 77.4 1.0
O A:GLY203 4.9 0.3 1.0

Fluorine binding site 2 out of 4 in 3d7m

Go back to Fluorine Binding Sites List in 3d7m
Fluorine binding site 2 out of 4 in the Crystal Structure of the G Protein Fast-Exchange Double Mutant I56C/Q333C


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 2 of Crystal Structure of the G Protein Fast-Exchange Double Mutant I56C/Q333C within 5.0Å range:
probe atom residue distance (Å) B Occ
A:F357

b:94.7
occ:1.00
F2 A:ALF357 0.0 94.7 1.0
AL A:ALF357 1.7 95.6 1.0
F1 A:ALF357 2.4 95.9 1.0
F3 A:ALF357 2.4 95.8 1.0
NH2 A:ARG178 2.7 64.8 1.0
N A:THR181 2.9 81.7 1.0
NH1 A:ARG178 2.9 64.1 1.0
CZ A:ARG178 3.1 64.6 1.0
O3B A:GDP355 3.1 70.9 1.0
O A:HOH412 3.1 65.5 1.0
CA A:LYS180 3.3 79.5 1.0
F4 A:ALF357 3.5 97.0 1.0
C A:LYS180 3.5 79.9 1.0
MG A:MG356 3.6 54.7 1.0
O A:VAL179 3.7 76.3 1.0
O2B A:GDP355 3.9 72.0 1.0
PB A:GDP355 3.9 69.3 1.0
CA A:THR181 4.0 85.0 1.0
CB A:THR181 4.0 84.0 1.0
CG A:LYS180 4.2 81.4 1.0
OG1 A:THR181 4.2 84.8 1.0
CB A:LYS180 4.2 80.8 1.0
N A:LYS180 4.2 77.8 1.0
O3A A:GDP355 4.3 66.7 1.0
NE A:ARG178 4.3 63.6 1.0
NE2 A:GLN204 4.3 0.1 1.0
O A:THR181 4.3 89.8 1.0
C A:VAL179 4.4 75.7 1.0
C A:THR181 4.7 88.0 1.0
O A:LYS180 4.7 80.8 1.0
N A:GLU43 4.8 74.0 1.0
O2A A:GDP355 4.8 65.7 1.0

Fluorine binding site 3 out of 4 in 3d7m

Go back to Fluorine Binding Sites List in 3d7m
Fluorine binding site 3 out of 4 in the Crystal Structure of the G Protein Fast-Exchange Double Mutant I56C/Q333C


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 3 of Crystal Structure of the G Protein Fast-Exchange Double Mutant I56C/Q333C within 5.0Å range:
probe atom residue distance (Å) B Occ
A:F357

b:95.8
occ:1.00
F3 A:ALF357 0.0 95.8 1.0
AL A:ALF357 1.7 95.6 1.0
MG A:MG356 2.1 54.7 1.0
F2 A:ALF357 2.4 94.7 1.0
F4 A:ALF357 2.4 97.0 1.0
O3B A:GDP355 2.9 70.9 1.0
CB A:THR181 3.0 84.0 1.0
O2B A:GDP355 3.1 72.0 1.0
OG1 A:THR181 3.4 84.8 1.0
PB A:GDP355 3.4 69.3 1.0
F1 A:ALF357 3.4 95.9 1.0
N A:THR181 3.5 81.7 1.0
O A:HOH412 3.6 65.5 1.0
CA A:THR181 3.8 85.0 1.0
CA A:GLY202 3.8 0.9 1.0
NZ A:LYS46 3.8 64.8 1.0
CG2 A:THR181 4.0 83.0 1.0
O A:THR181 4.0 89.8 1.0
N A:GLY203 4.0 0.2 1.0
OG A:SER47 4.1 75.7 1.0
CE A:LYS46 4.1 67.1 1.0
O A:VAL201 4.1 97.2 1.0
C A:THR181 4.3 88.0 1.0
O1B A:GDP355 4.4 68.7 1.0
C A:GLY202 4.4 0.4 1.0
O3A A:GDP355 4.6 66.7 1.0
N A:GLY202 4.7 99.8 1.0
NH1 A:ARG178 4.7 64.1 1.0
C A:LYS180 4.7 79.9 1.0
C A:VAL201 4.7 98.0 1.0

Fluorine binding site 4 out of 4 in 3d7m

Go back to Fluorine Binding Sites List in 3d7m
Fluorine binding site 4 out of 4 in the Crystal Structure of the G Protein Fast-Exchange Double Mutant I56C/Q333C


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 4 of Crystal Structure of the G Protein Fast-Exchange Double Mutant I56C/Q333C within 5.0Å range:
probe atom residue distance (Å) B Occ
A:F357

b:97.0
occ:1.00
F4 A:ALF357 0.0 97.0 1.0
AL A:ALF357 1.8 95.6 1.0
F3 A:ALF357 2.4 95.8 1.0
F1 A:ALF357 2.5 95.9 1.0
N A:GLY203 2.6 0.2 1.0
O3B A:GDP355 2.7 70.9 1.0
NZ A:LYS46 2.8 64.8 1.0
CA A:GLY203 3.4 0.6 1.0
F2 A:ALF357 3.5 94.7 1.0
CE A:LYS46 3.6 67.1 1.0
C A:GLY202 3.7 0.4 1.0
O A:ALA41 3.7 77.8 1.0
CA A:GLY42 3.7 73.8 1.0
C A:GLY203 3.8 0.2 1.0
O A:GLY203 3.8 0.3 1.0
PB A:GDP355 3.9 69.3 1.0
CA A:GLY202 3.9 0.9 1.0
N A:GLU43 4.0 74.0 1.0
NE2 A:GLN204 4.1 0.1 1.0
C A:ALA41 4.3 76.4 1.0
MG A:MG356 4.3 54.7 1.0
C A:GLY42 4.3 74.4 1.0
CG A:GLN204 4.4 0.2 1.0
O2B A:GDP355 4.4 72.0 1.0
O1B A:GDP355 4.4 68.7 1.0
N A:GLY42 4.4 74.6 1.0
O A:VAL201 4.6 97.2 1.0
CD A:GLN204 4.6 0.2 1.0
N A:GLN204 4.7 0.5 1.0
O A:GLY202 4.8 0.6 1.0

Reference:

A.M.Preininger, M.A.Funk, W.M.Oldham, S.M.Meier, C.A.Johnston, S.Adhikary, A.J.Kimple, D.P.Siderovski, H.E.Hamm, T.M.Iverson. Helix Dipole Movement and Conformational Variability Contribute to Allosteric Gdp Release in Galphai Subunits. Biochemistry V. 48 2630 2009.
ISSN: ISSN 0006-2960
PubMed: 19222191
DOI: 10.1021/BI801853A
Page generated: Mon Jul 14 15:48:32 2025

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