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Fluorine in PDB 4qj3: Structure of A Fragment of Human Phospholipase C-BETA3 DELTA472-559, in Complex with Galphaq

Enzymatic activity of Structure of A Fragment of Human Phospholipase C-BETA3 DELTA472-559, in Complex with Galphaq

All present enzymatic activity of Structure of A Fragment of Human Phospholipase C-BETA3 DELTA472-559, in Complex with Galphaq:
3.1.4.11;

Protein crystallography data

The structure of Structure of A Fragment of Human Phospholipase C-BETA3 DELTA472-559, in Complex with Galphaq, PDB code: 4qj3 was solved by A.M.Lyon, J.J.G.Tesmer, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 29.71 / 3.00
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 200.623, 88.761, 92.232, 90.00, 101.39, 90.00
R / Rfree (%) 19.5 / 24

Other elements in 4qj3:

The structure of Structure of A Fragment of Human Phospholipase C-BETA3 DELTA472-559, in Complex with Galphaq also contains other interesting chemical elements:

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

Fluorine Binding Sites:

The binding sites of Fluorine atom in the Structure of A Fragment of Human Phospholipase C-BETA3 DELTA472-559, in Complex with Galphaq (pdb code 4qj3). This binding sites where shown within 5.0 Angstroms radius around Fluorine atom.
In total 4 binding sites of Fluorine where determined in the Structure of A Fragment of Human Phospholipase C-BETA3 DELTA472-559, in Complex with Galphaq, PDB code: 4qj3:
Jump to Fluorine binding site number: 1; 2; 3; 4;

Fluorine binding site 1 out of 4 in 4qj3

Go back to Fluorine Binding Sites List in 4qj3
Fluorine binding site 1 out of 4 in the Structure of A Fragment of Human Phospholipase C-BETA3 DELTA472-559, in Complex with Galphaq


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 1 of Structure of A Fragment of Human Phospholipase C-BETA3 DELTA472-559, in Complex with Galphaq within 5.0Å range:
probe atom residue distance (Å) B Occ
A:F401

b:30.8
occ:1.00
 F1 A:ALF401 0.0 30.8 1.0
AL A:ALF401 1.8 30.6 1.0
O3B A:GDP400 2.5 30.0 1.0
F4 A:ALF401 2.5 30.1 1.0
F3 A:ALF401 2.5 30.9 1.0
NH1 A:ARG183 2.6 36.5 1.0
O A:HOH501 2.6 18.1 1.0
MG A:MG402 2.8 32.8 1.0
N A:THR186 3.0 37.2 1.0
NH2 A:ARG183 3.0 37.0 1.0
CZ A:ARG183 3.1 36.4 1.0
CA A:PRO185 3.3 37.2 1.0
F2 A:ALF401 3.6 31.2 1.0
C A:PRO185 3.6 37.8 1.0
PB A:GDP400 3.7 29.9 1.0
OG1 A:THR186 3.7 36.1 1.0
O2B A:GDP400 3.9 30.9 1.0
O A:VAL184 4.0 37.4 1.0
CA A:THR186 4.0 37.9 1.0
CB A:THR186 4.1 37.4 1.0
O2A A:GDP400 4.1 30.1 1.0
CB A:PRO185 4.2 37.7 1.0
N A:PRO185 4.3 37.3 1.0
NE A:ARG183 4.3 36.0 1.0
O3A A:GDP400 4.4 29.4 1.0
O A:THR186 4.4 38.8 1.0
C A:VAL184 4.5 37.3 1.0
O A:HOH508 4.5 16.3 1.0
NE2 A:GLN209 4.7 35.1 1.0
OE1 A:GLN209 4.7 36.4 1.0
C A:THR186 4.8 38.9 1.0
N A:GLU49 4.8 33.6 1.0
O A:PRO185 4.8 38.8 1.0
PA A:GDP400 4.9 29.5 1.0
OG A:SER53 4.9 33.7 1.0
O1B A:GDP400 4.9 29.9 1.0

Fluorine binding site 2 out of 4 in 4qj3

Go back to Fluorine Binding Sites List in 4qj3
Fluorine binding site 2 out of 4 in the Structure of A Fragment of Human Phospholipase C-BETA3 DELTA472-559, in Complex with Galphaq


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 2 of Structure of A Fragment of Human Phospholipase C-BETA3 DELTA472-559, in Complex with Galphaq within 5.0Å range:
probe atom residue distance (Å) B Occ
A:F401

b:31.2
occ:1.00
 F2 A:ALF401 0.0 31.2 1.0
AL A:ALF401 1.8 30.6 1.0
F3 A:ALF401 2.5 30.9 1.0
F4 A:ALF401 2.6 30.1 1.0
O3B A:GDP400 2.6 30.0 1.0
NZ A:LYS52 2.6 33.3 1.0
N A:GLY208 2.7 36.7 1.0
O A:HOH501 2.7 18.1 1.0
CE A:LYS52 3.1 34.0 1.0
CA A:GLY208 3.2 36.8 1.0
CA A:GLY48 3.4 34.8 1.0
PB A:GDP400 3.5 29.9 1.0
O1B A:GDP400 3.6 29.9 1.0
F1 A:ALF401 3.6 30.8 1.0
N A:GLU49 3.7 33.6 1.0
C A:GLY207 3.7 37.7 1.0
CA A:GLY207 4.0 38.0 1.0
C A:GLY48 4.0 33.9 1.0
N A:GLY48 4.1 35.4 1.0
O A:THR47 4.2 34.6 1.0
O2B A:GDP400 4.2 30.9 1.0
OE1 A:GLN209 4.2 36.4 1.0
O A:VAL206 4.2 37.7 1.0
O A:HOH508 4.3 16.3 1.0
C A:GLY208 4.3 37.2 1.0
NE2 A:GLN209 4.4 35.1 1.0
C A:THR47 4.4 35.1 1.0
N A:GLN209 4.5 37.7 1.0
MG A:MG402 4.5 32.8 1.0
CD A:GLN209 4.6 36.1 1.0
CD A:LYS52 4.6 34.4 1.0
O A:GLY46 4.8 36.0 1.0
O A:GLY207 4.8 38.5 1.0
CA A:GLU49 4.9 33.3 1.0
O3A A:GDP400 4.9 29.4 1.0

Fluorine binding site 3 out of 4 in 4qj3

Go back to Fluorine Binding Sites List in 4qj3
Fluorine binding site 3 out of 4 in the Structure of A Fragment of Human Phospholipase C-BETA3 DELTA472-559, in Complex with Galphaq


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 3 of Structure of A Fragment of Human Phospholipase C-BETA3 DELTA472-559, in Complex with Galphaq within 5.0Å range:
probe atom residue distance (Å) B Occ
A:F401

b:30.9
occ:1.00
 F3 A:ALF401 0.0 30.9 1.0
AL A:ALF401 1.8 30.6 1.0
O A:HOH508 2.3 16.3 1.0
MG A:MG402 2.3 32.8 1.0
F2 A:ALF401 2.5 31.2 1.0
F1 A:ALF401 2.5 30.8 1.0
O3B A:GDP400 2.6 30.0 1.0
O A:HOH501 2.6 18.1 1.0
OG1 A:THR186 2.8 36.1 1.0
O2B A:GDP400 2.8 30.9 1.0
CB A:THR186 3.0 37.4 1.0
PB A:GDP400 3.1 29.9 1.0
O A:VAL206 3.6 37.7 1.0
F4 A:ALF401 3.6 30.1 1.0
N A:THR186 3.7 37.2 1.0
OG A:SER53 3.7 33.7 1.0
CE A:LYS52 3.8 34.0 1.0
CA A:THR186 3.9 37.9 1.0
O1B A:GDP400 4.0 29.9 1.0
NZ A:LYS52 4.1 33.3 1.0
CA A:GLY207 4.1 38.0 1.0
CG2 A:THR186 4.2 38.5 1.0
N A:GLY208 4.3 36.7 1.0
O A:THR186 4.3 38.8 1.0
C A:VAL206 4.5 38.7 1.0
O3A A:GDP400 4.5 29.4 1.0
C A:THR186 4.5 38.9 1.0
NH1 A:ARG183 4.6 36.5 1.0
C A:GLY207 4.7 37.7 1.0
N A:GLY207 4.7 38.9 1.0
OD1 A:ASP205 4.9 39.3 1.0
O2A A:GDP400 4.9 30.1 1.0
C A:PRO185 4.9 37.8 1.0
CB A:SER53 4.9 33.8 1.0
CB A:LYS52 5.0 33.8 1.0

Fluorine binding site 4 out of 4 in 4qj3

Go back to Fluorine Binding Sites List in 4qj3
Fluorine binding site 4 out of 4 in the Structure of A Fragment of Human Phospholipase C-BETA3 DELTA472-559, in Complex with Galphaq


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 4 of Structure of A Fragment of Human Phospholipase C-BETA3 DELTA472-559, in Complex with Galphaq within 5.0Å range:
probe atom residue distance (Å) B Occ
A:F401

b:30.1
occ:1.00
 F4 A:ALF401 0.0 30.1 1.0
AL A:ALF401 1.8 30.6 1.0
F1 A:ALF401 2.5 30.8 1.0
F2 A:ALF401 2.6 31.2 1.0
NE2 A:GLN209 2.6 35.1 1.0
O A:HOH501 2.6 18.1 1.0
O3B A:GDP400 2.7 30.0 1.0
NH2 A:ARG183 2.9 37.0 1.0
N A:GLU49 3.1 33.6 1.0
CA A:GLY48 3.3 34.8 1.0
OE1 A:GLN209 3.3 36.4 1.0
CD A:GLN209 3.3 36.1 1.0
F3 A:ALF401 3.6 30.9 1.0
C A:GLY48 3.6 33.9 1.0
NH1 A:ARG183 3.7 36.5 1.0
CZ A:ARG183 3.8 36.4 1.0
CA A:GLU49 4.1 33.3 1.0
CG A:GLU49 4.1 35.0 1.0
PB A:GDP400 4.1 29.9 1.0
N A:GLY208 4.4 36.7 1.0
N A:GLY48 4.6 35.4 1.0
CB A:GLU49 4.7 33.9 1.0
CG A:GLN209 4.8 37.1 1.0
O1B A:GDP400 4.8 29.9 1.0
O A:GLY48 4.8 33.8 1.0
CA A:GLY208 4.8 36.8 1.0
MG A:MG402 4.8 32.8 1.0
NZ A:LYS52 4.9 33.3 1.0
O3A A:GDP400 4.9 29.4 1.0
N A:GLN209 5.0 37.7 1.0
N A:THR186 5.0 37.2 1.0

Reference:

A.M.Lyon, J.A.Begley, T.Manett, J.J.G.Tesmer. Molecular Mechanisms of Plcbeta Regulation. Structure 2014.
ISSN: ISSN 0969-2126
Page generated: Tue Jul 15 00:25:58 2025

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