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Fluorine in PDB 3fal: Humanrxr Alpha & Mouse Lxr Alpha Complexed with Retenoic Acid and GSK2186
Protein crystallography data
The structure of Humanrxr Alpha & Mouse Lxr Alpha Complexed with Retenoic Acid and GSK2186, PDB code: 3fal
was solved by
E.Y.Chao,
J.A.Caravella,
M.A.Watson,
N.Campobasso,
S.Ghisletti,
A.N.Billin,
C.Galardi,
T.M.Willson,
W.J.Zuercher,
J.L.Collins,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
| Resolution Low / High (Å) | 42.34 / 2.36 |
| Space group | C 1 2 1 |
| Cell size a, b, c (Å), α, β, γ (°) | 123.212, 90.002, 101.311, 90.00, 111.88, 90.00 |
| R / Rfree (%) | 21.9 / 27.8 |
Other elements in 3fal:
The structure of Humanrxr Alpha & Mouse Lxr Alpha Complexed with Retenoic Acid and GSK2186 also contains other interesting chemical elements:
| Chlorine | (Cl) | 2 atoms |
Fluorine Binding Sites:
Pages:
>>> Page 1 <<< Page 2, Binding sites: 11 - 12;Binding sites:
The binding sites of Fluorine atom in the Humanrxr Alpha & Mouse Lxr Alpha Complexed with Retenoic Acid and GSK2186 (pdb code 3fal). This binding sites where shown within 5.0 Angstroms radius around Fluorine atom.In total 12 binding sites of Fluorine where determined in the Humanrxr Alpha & Mouse Lxr Alpha Complexed with Retenoic Acid and GSK2186, PDB code: 3fal:
Jump to Fluorine binding site number: 1; 2; 3; 4; 5; 6; 7; 8; 9; 10;
Fluorine binding site 1 out of 12 in 3fal
Go back to
Fluorine Binding Sites List in 3fal
Fluorine binding site 1 out
of 12 in the Humanrxr Alpha & Mouse Lxr Alpha Complexed with Retenoic Acid and GSK2186
Mono view
Stereo pair view
Mono view
Stereo pair view
A full contact list of Fluorine with other atoms in the F binding
site number 1 of Humanrxr Alpha & Mouse Lxr Alpha Complexed with Retenoic Acid and GSK2186 within 5.0Å range:
|
Fluorine binding site 2 out of 12 in 3fal
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Fluorine Binding Sites List in 3fal
Fluorine binding site 2 out
of 12 in the Humanrxr Alpha & Mouse Lxr Alpha Complexed with Retenoic Acid and GSK2186
Mono view
Stereo pair view
Mono view
Stereo pair view
A full contact list of Fluorine with other atoms in the F binding
site number 2 of Humanrxr Alpha & Mouse Lxr Alpha Complexed with Retenoic Acid and GSK2186 within 5.0Å range:
|
Fluorine binding site 3 out of 12 in 3fal
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Fluorine Binding Sites List in 3fal
Fluorine binding site 3 out
of 12 in the Humanrxr Alpha & Mouse Lxr Alpha Complexed with Retenoic Acid and GSK2186
Mono view
Stereo pair view
Mono view
Stereo pair view
A full contact list of Fluorine with other atoms in the F binding
site number 3 of Humanrxr Alpha & Mouse Lxr Alpha Complexed with Retenoic Acid and GSK2186 within 5.0Å range:
|
Fluorine binding site 4 out of 12 in 3fal
Go back to
Fluorine Binding Sites List in 3fal
Fluorine binding site 4 out
of 12 in the Humanrxr Alpha & Mouse Lxr Alpha Complexed with Retenoic Acid and GSK2186
Mono view
Stereo pair view
Mono view
Stereo pair view
A full contact list of Fluorine with other atoms in the F binding
site number 4 of Humanrxr Alpha & Mouse Lxr Alpha Complexed with Retenoic Acid and GSK2186 within 5.0Å range:
|
Fluorine binding site 5 out of 12 in 3fal
Go back to
Fluorine Binding Sites List in 3fal
Fluorine binding site 5 out
of 12 in the Humanrxr Alpha & Mouse Lxr Alpha Complexed with Retenoic Acid and GSK2186
Mono view
Stereo pair view
Mono view
Stereo pair view
A full contact list of Fluorine with other atoms in the F binding
site number 5 of Humanrxr Alpha & Mouse Lxr Alpha Complexed with Retenoic Acid and GSK2186 within 5.0Å range:
|
Fluorine binding site 6 out of 12 in 3fal
Go back to
Fluorine Binding Sites List in 3fal
Fluorine binding site 6 out
of 12 in the Humanrxr Alpha & Mouse Lxr Alpha Complexed with Retenoic Acid and GSK2186
Mono view
Stereo pair view
Mono view
Stereo pair view
A full contact list of Fluorine with other atoms in the F binding
site number 6 of Humanrxr Alpha & Mouse Lxr Alpha Complexed with Retenoic Acid and GSK2186 within 5.0Å range:
|
Fluorine binding site 7 out of 12 in 3fal
Go back to
Fluorine Binding Sites List in 3fal
Fluorine binding site 7 out
of 12 in the Humanrxr Alpha & Mouse Lxr Alpha Complexed with Retenoic Acid and GSK2186
Mono view
Stereo pair view
Mono view
Stereo pair view
A full contact list of Fluorine with other atoms in the F binding
site number 7 of Humanrxr Alpha & Mouse Lxr Alpha Complexed with Retenoic Acid and GSK2186 within 5.0Å range:
|
Fluorine binding site 8 out of 12 in 3fal
Go back to
Fluorine Binding Sites List in 3fal
Fluorine binding site 8 out
of 12 in the Humanrxr Alpha & Mouse Lxr Alpha Complexed with Retenoic Acid and GSK2186
Mono view
Stereo pair view
Mono view
Stereo pair view
A full contact list of Fluorine with other atoms in the F binding
site number 8 of Humanrxr Alpha & Mouse Lxr Alpha Complexed with Retenoic Acid and GSK2186 within 5.0Å range:
|
Fluorine binding site 9 out of 12 in 3fal
Go back to
Fluorine Binding Sites List in 3fal
Fluorine binding site 9 out
of 12 in the Humanrxr Alpha & Mouse Lxr Alpha Complexed with Retenoic Acid and GSK2186
Mono view
Stereo pair view
Mono view
Stereo pair view
A full contact list of Fluorine with other atoms in the F binding
site number 9 of Humanrxr Alpha & Mouse Lxr Alpha Complexed with Retenoic Acid and GSK2186 within 5.0Å range:
|
Fluorine binding site 10 out of 12 in 3fal
Go back to
Fluorine Binding Sites List in 3fal
Fluorine binding site 10 out
of 12 in the Humanrxr Alpha & Mouse Lxr Alpha Complexed with Retenoic Acid and GSK2186
Mono view
Stereo pair view
Mono view
Stereo pair view
A full contact list of Fluorine with other atoms in the F binding
site number 10 of Humanrxr Alpha & Mouse Lxr Alpha Complexed with Retenoic Acid and GSK2186 within 5.0Å range:
|
Reference:
E.Y.Chao,
J.A.Caravella,
M.A.Watson,
N.Campobasso,
S.Ghisletti,
A.N.Billin,
C.Galardi,
P.Wang,
B.A.Laffitte,
M.A.Iannone,
B.J.Goodwin,
J.A.Nichols,
D.J.Parks,
E.Stewart,
R.W.Wiethe,
S.P.Williams,
A.Smallwood,
K.H.Pearce,
C.K.Glass,
T.M.Willson,
W.J.Zuercher,
J.L.Collins.
Structure-Guided Design of N-Phenyl Tertiary Amines As Transrepression-Selective Liver X Receptor Modulators with Anti-Inflammatory Activity. J.Med.Chem. V. 51 5758 2008.
ISSN: ISSN 0022-2623
PubMed: 18800767
DOI: 10.1021/JM800612U
Page generated: Mon Jul 14 16:13:30 2025
ISSN: ISSN 0022-2623
PubMed: 18800767
DOI: 10.1021/JM800612U
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