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Fluorine in PDB 4qj5: Structure of A Fragment of Human Phospholipase C-BETA3 DELTA472-581, Bound to IP3 and in Complex with Galphaq

Enzymatic activity of Structure of A Fragment of Human Phospholipase C-BETA3 DELTA472-581, Bound to IP3 and in Complex with Galphaq

All present enzymatic activity of Structure of A Fragment of Human Phospholipase C-BETA3 DELTA472-581, Bound to IP3 and in Complex with Galphaq:
3.1.4.11;

Protein crystallography data

The structure of Structure of A Fragment of Human Phospholipase C-BETA3 DELTA472-581, Bound to IP3 and in Complex with Galphaq, PDB code: 4qj5 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) 29.34 / 3.41
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 205.918, 89.869, 93.261, 90.00, 101.80, 90.00
R / Rfree (%) 21.2 / 27.7

Other elements in 4qj5:

The structure of Structure of A Fragment of Human Phospholipase C-BETA3 DELTA472-581, Bound to IP3 and 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 DELTA472-581, Bound to IP3 and in Complex with Galphaq (pdb code 4qj5). 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 DELTA472-581, Bound to IP3 and in Complex with Galphaq, PDB code: 4qj5:
Jump to Fluorine binding site number: 1; 2; 3; 4;

Fluorine binding site 1 out of 4 in 4qj5

Go back to Fluorine Binding Sites List in 4qj5
Fluorine binding site 1 out of 4 in the Structure of A Fragment of Human Phospholipase C-BETA3 DELTA472-581, Bound to IP3 and 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 DELTA472-581, Bound to IP3 and in Complex with Galphaq within 5.0Å range:
probe atom residue distance (Å) B Occ
A:F401

b:59.0
occ:1.00
 F1 A:ALF401 0.0 59.0 1.0
AL A:ALF401 1.8 59.0 1.0
MG A:MG402 2.2 58.8 1.0
O3B A:GDP400 2.3 58.1 1.0
F3 A:ALF401 2.6 59.3 1.0
F4 A:ALF401 2.6 59.0 1.0
O A:HOH501 2.6 26.7 1.0
OG1 A:THR186 2.6 59.9 1.0
N A:THR186 2.8 60.0 1.0
CB A:THR186 3.0 60.5 1.0
NH1 A:ARG183 3.3 56.3 1.0
PB A:GDP400 3.4 57.8 1.0
O2B A:GDP400 3.4 58.2 1.0
CA A:THR186 3.4 60.8 1.0
O A:HOH502 3.5 12.7 1.0
F2 A:ALF401 3.6 59.3 1.0
C A:PRO185 3.6 59.6 1.0
O2A A:GDP400 3.7 57.1 1.0
CA A:PRO185 3.7 58.9 1.0
O A:VAL184 3.9 58.1 1.0
O A:THR186 4.2 61.8 1.0
CZ A:ARG183 4.2 56.4 1.0
OG A:SER53 4.3 59.0 1.0
C A:THR186 4.3 61.7 1.0
O3A A:GDP400 4.4 57.3 1.0
CG2 A:THR186 4.4 61.0 1.0
NH2 A:ARG183 4.5 56.7 1.0
O1B A:GDP400 4.6 58.0 1.0
N A:PRO185 4.7 58.5 1.0
C A:VAL184 4.7 58.0 1.0
PA A:GDP400 4.7 57.0 1.0
O A:PRO185 4.8 60.0 1.0
CB A:PRO185 4.9 59.1 1.0

Fluorine binding site 2 out of 4 in 4qj5

Go back to Fluorine Binding Sites List in 4qj5
Fluorine binding site 2 out of 4 in the Structure of A Fragment of Human Phospholipase C-BETA3 DELTA472-581, Bound to IP3 and 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 DELTA472-581, Bound to IP3 and in Complex with Galphaq within 5.0Å range:
probe atom residue distance (Å) B Occ
A:F401

b:59.3
occ:1.00
 F2 A:ALF401 0.0 59.3 1.0
AL A:ALF401 1.8 59.0 1.0
F4 A:ALF401 2.5 59.0 1.0
O A:HOH501 2.5 26.7 1.0
F3 A:ALF401 2.6 59.3 1.0
O3B A:GDP400 2.8 58.1 1.0
N A:GLY208 3.1 66.1 1.0
N A:GLU49 3.1 59.0 1.0
CA A:GLY48 3.3 60.3 1.0
CA A:GLY208 3.3 66.1 1.0
NE2 A:GLN209 3.4 65.9 1.0
O1B A:GDP400 3.5 58.0 1.0
PB A:GDP400 3.6 57.8 1.0
F1 A:ALF401 3.6 59.0 1.0
C A:GLY48 3.7 59.5 1.0
O A:THR47 3.8 60.8 1.0
OE1 A:GLN209 3.8 65.6 1.0
C A:GLY208 3.9 66.4 1.0
CD A:GLN209 4.0 66.1 1.0
NZ A:LYS52 4.1 59.1 1.0
N A:GLY48 4.2 60.9 1.0
CE A:LYS52 4.2 59.0 1.0
C A:GLY207 4.2 66.7 1.0
CA A:GLU49 4.3 58.5 1.0
N A:GLN209 4.3 67.0 1.0
C A:THR47 4.4 61.2 1.0
O A:GLY208 4.5 66.4 1.0
O2B A:GDP400 4.5 58.2 1.0
CA A:GLY207 4.6 66.8 1.0
NH1 A:ARG183 4.8 56.3 1.0
O3A A:GDP400 4.9 57.3 1.0
O A:GLY48 4.9 59.5 1.0
CG A:GLU49 5.0 58.6 1.0

Fluorine binding site 3 out of 4 in 4qj5

Go back to Fluorine Binding Sites List in 4qj5
Fluorine binding site 3 out of 4 in the Structure of A Fragment of Human Phospholipase C-BETA3 DELTA472-581, Bound to IP3 and 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 DELTA472-581, Bound to IP3 and in Complex with Galphaq within 5.0Å range:
probe atom residue distance (Å) B Occ
A:F401

b:59.3
occ:1.00
 F3 A:ALF401 0.0 59.3 1.0
AL A:ALF401 1.8 59.0 1.0
O A:HOH502 2.5 12.7 1.0
F1 A:ALF401 2.6 59.0 1.0
F2 A:ALF401 2.6 59.3 1.0
O3B A:GDP400 2.6 58.1 1.0
O A:HOH501 2.7 26.7 1.0
O2B A:GDP400 2.7 58.2 1.0
PB A:GDP400 2.8 57.8 1.0
MG A:MG402 3.0 58.8 1.0
O1B A:GDP400 3.2 58.0 1.0
O A:VAL206 3.2 66.5 1.0
CE A:LYS52 3.3 59.0 1.0
F4 A:ALF401 3.6 59.0 1.0
N A:GLY208 3.7 66.1 1.0
CB A:THR186 3.8 60.5 1.0
OG1 A:THR186 4.0 59.9 1.0
CA A:GLY207 4.0 66.8 1.0
NZ A:LYS52 4.1 59.1 1.0
C A:GLY207 4.3 66.7 1.0
C A:VAL206 4.3 67.0 1.0
OG A:SER53 4.3 59.0 1.0
O3A A:GDP400 4.4 57.3 1.0
CD A:LYS52 4.4 59.1 1.0
O A:THR186 4.6 61.8 1.0
CA A:GLY208 4.6 66.1 1.0
N A:GLY207 4.6 67.2 1.0
CG2 A:THR186 4.6 61.0 1.0
N A:THR186 4.7 60.0 1.0
CB A:LYS52 4.7 58.7 1.0
CA A:THR186 4.8 60.8 1.0
N A:GLU49 5.0 59.0 1.0
CG A:LYS52 5.0 58.8 1.0
O2A A:GDP400 5.0 57.1 1.0

Fluorine binding site 4 out of 4 in 4qj5

Go back to Fluorine Binding Sites List in 4qj5
Fluorine binding site 4 out of 4 in the Structure of A Fragment of Human Phospholipase C-BETA3 DELTA472-581, Bound to IP3 and 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 DELTA472-581, Bound to IP3 and in Complex with Galphaq within 5.0Å range:
probe atom residue distance (Å) B Occ
A:F401

b:59.0
occ:1.00
 F4 A:ALF401 0.0 59.0 1.0
AL A:ALF401 1.8 59.0 1.0
O A:HOH501 2.5 26.7 1.0
F2 A:ALF401 2.5 59.3 1.0
O3B A:GDP400 2.5 58.1 1.0
F1 A:ALF401 2.6 59.0 1.0
NH1 A:ARG183 2.7 56.3 1.0
NH2 A:ARG183 2.8 56.7 1.0
CZ A:ARG183 3.1 56.4 1.0
OE1 A:GLN209 3.6 65.6 1.0
NE2 A:GLN209 3.6 65.9 1.0
F3 A:ALF401 3.6 59.3 1.0
N A:GLU49 3.8 59.0 1.0
PB A:GDP400 4.0 57.8 1.0
CD A:GLN209 4.0 66.1 1.0
CG A:GLU49 4.0 58.6 1.0
N A:THR186 4.2 60.0 1.0
CA A:PRO185 4.2 58.9 1.0
CA A:GLU49 4.3 58.5 1.0
NE A:ARG183 4.5 56.2 1.0
MG A:MG402 4.5 58.8 1.0
CA A:GLY48 4.6 60.3 1.0
C A:GLY48 4.6 59.5 1.0
CB A:PRO185 4.7 59.1 1.0
O1B A:GDP400 4.7 58.0 1.0
C A:PRO185 4.8 59.6 1.0
CB A:GLU49 4.8 58.4 1.0
O3A A:GDP400 4.8 57.3 1.0
O2B A:GDP400 4.9 58.2 1.0
O2A A:GDP400 4.9 57.1 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 00:26:59 2025

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