Fluorine in PDB 7yxd: Crystal Structure of Wt ANCGR2-Lbd Bound to Dexamethasone and Shp Coregulator Fragment
Protein crystallography data
The structure of Crystal Structure of Wt ANCGR2-Lbd Bound to Dexamethasone and Shp Coregulator Fragment, PDB code: 7yxd
was solved by
A.Jimenez-Panizo,
E.Estebanez-Perpina,
P.Fuentes-Prior,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
76.81 /
2.30
|
Space group
|
P 31
|
Cell size a, b, c (Å), α, β, γ (°)
|
107.599,
107.599,
135.641,
90,
90,
120
|
R / Rfree (%)
|
17.7 /
22.1
|
Other elements in 7yxd:
The structure of Crystal Structure of Wt ANCGR2-Lbd Bound to Dexamethasone and Shp Coregulator Fragment also contains other interesting chemical elements:
Fluorine Binding Sites:
The binding sites of Fluorine atom in the Crystal Structure of Wt ANCGR2-Lbd Bound to Dexamethasone and Shp Coregulator Fragment
(pdb code 7yxd). 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 Wt ANCGR2-Lbd Bound to Dexamethasone and Shp Coregulator Fragment, PDB code: 7yxd:
Jump to Fluorine binding site number:
1;
2;
3;
4;
Fluorine binding site 1 out
of 4 in 7yxd
Go back to
Fluorine Binding Sites List in 7yxd
Fluorine binding site 1 out
of 4 in the Crystal Structure of Wt ANCGR2-Lbd Bound to Dexamethasone and Shp Coregulator Fragment
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 Wt ANCGR2-Lbd Bound to Dexamethasone and Shp Coregulator Fragment within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:F1001
b:25.0
occ:1.00
|
F1
|
A:DEX1001
|
0.0
|
25.0
|
1.0
|
C9
|
A:DEX1001
|
1.4
|
26.8
|
1.0
|
C11
|
A:DEX1001
|
2.3
|
23.1
|
1.0
|
C10
|
A:DEX1001
|
2.3
|
26.1
|
1.0
|
C8
|
A:DEX1001
|
2.3
|
24.3
|
1.0
|
C5
|
A:DEX1001
|
2.6
|
26.3
|
1.0
|
C7
|
A:DEX1001
|
2.7
|
25.6
|
1.0
|
C1
|
A:DEX1001
|
2.7
|
31.3
|
1.0
|
C12
|
A:DEX1001
|
2.8
|
24.3
|
1.0
|
C14
|
A:DEX1001
|
2.8
|
26.8
|
1.0
|
C6
|
A:DEX1001
|
3.3
|
21.6
|
1.0
|
CE1
|
A:PHE623
|
3.3
|
36.3
|
1.0
|
C4
|
A:DEX1001
|
3.3
|
26.0
|
1.0
|
C13
|
A:DEX1001
|
3.4
|
28.3
|
1.0
|
O2
|
A:DEX1001
|
3.6
|
26.6
|
1.0
|
C2
|
A:DEX1001
|
3.6
|
27.6
|
1.0
|
C3
|
A:DEX1001
|
3.7
|
30.3
|
1.0
|
C19
|
A:DEX1001
|
3.8
|
29.7
|
1.0
|
CB
|
A:LEU563
|
4.0
|
25.5
|
1.0
|
CD1
|
A:PHE623
|
4.2
|
39.2
|
1.0
|
CZ
|
A:PHE623
|
4.2
|
26.8
|
1.0
|
C15
|
A:DEX1001
|
4.3
|
32.5
|
1.0
|
O3
|
A:DEX1001
|
4.4
|
29.3
|
1.0
|
C18
|
A:DEX1001
|
4.5
|
23.1
|
1.0
|
C17
|
A:DEX1001
|
4.6
|
29.5
|
1.0
|
O1
|
A:DEX1001
|
4.6
|
27.8
|
1.0
|
O
|
A:LEU563
|
4.6
|
23.8
|
1.0
|
CD1
|
A:LEU563
|
4.7
|
28.4
|
1.0
|
CG
|
A:LEU563
|
4.7
|
27.9
|
1.0
|
SD
|
A:MET646
|
4.7
|
58.5
|
1.0
|
CD2
|
A:LEU563
|
4.8
|
33.1
|
1.0
|
C
|
A:LEU563
|
4.8
|
22.6
|
1.0
|
CA
|
A:LEU563
|
4.9
|
29.4
|
1.0
|
|
Fluorine binding site 2 out
of 4 in 7yxd
Go back to
Fluorine Binding Sites List in 7yxd
Fluorine binding site 2 out
of 4 in the Crystal Structure of Wt ANCGR2-Lbd Bound to Dexamethasone and Shp Coregulator Fragment
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 Wt ANCGR2-Lbd Bound to Dexamethasone and Shp Coregulator Fragment within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
D:F1001
b:29.7
occ:1.00
|
F1
|
D:DEX1001
|
0.0
|
29.7
|
1.0
|
C9
|
D:DEX1001
|
1.4
|
29.5
|
1.0
|
C8
|
D:DEX1001
|
2.3
|
26.8
|
1.0
|
C10
|
D:DEX1001
|
2.3
|
26.6
|
1.0
|
C11
|
D:DEX1001
|
2.4
|
29.4
|
1.0
|
C7
|
D:DEX1001
|
2.6
|
25.4
|
1.0
|
C5
|
D:DEX1001
|
2.6
|
21.1
|
1.0
|
C14
|
D:DEX1001
|
2.7
|
31.8
|
1.0
|
C1
|
D:DEX1001
|
2.8
|
31.7
|
1.0
|
C12
|
D:DEX1001
|
2.9
|
26.2
|
1.0
|
C6
|
D:DEX1001
|
3.2
|
25.7
|
1.0
|
C2
|
D:DEX1001
|
3.2
|
26.2
|
1.0
|
CE1
|
D:PHE623
|
3.2
|
31.3
|
1.0
|
C4
|
D:DEX1001
|
3.3
|
27.0
|
1.0
|
C13
|
D:DEX1001
|
3.5
|
30.6
|
1.0
|
O2
|
D:DEX1001
|
3.6
|
28.2
|
1.0
|
C3
|
D:DEX1001
|
3.7
|
30.0
|
1.0
|
C19
|
D:DEX1001
|
3.8
|
21.2
|
1.0
|
CB
|
D:LEU563
|
4.0
|
32.8
|
1.0
|
CD1
|
D:PHE623
|
4.1
|
33.2
|
1.0
|
CZ
|
D:PHE623
|
4.1
|
28.5
|
1.0
|
C15
|
D:DEX1001
|
4.1
|
32.5
|
1.0
|
O3
|
D:DEX1001
|
4.4
|
38.2
|
1.0
|
SD
|
D:MET646
|
4.4
|
59.2
|
1.0
|
C18
|
D:DEX1001
|
4.5
|
30.8
|
1.0
|
CD1
|
D:LEU563
|
4.5
|
44.1
|
1.0
|
C17
|
D:DEX1001
|
4.6
|
33.9
|
1.0
|
CG
|
D:LEU563
|
4.6
|
33.5
|
1.0
|
O
|
D:LEU563
|
4.7
|
30.4
|
1.0
|
CD2
|
D:LEU563
|
4.7
|
37.0
|
1.0
|
C
|
D:LEU563
|
4.9
|
25.4
|
1.0
|
CA
|
D:LEU563
|
4.9
|
24.1
|
1.0
|
CE
|
D:MET646
|
4.9
|
62.5
|
1.0
|
O1
|
D:DEX1001
|
4.9
|
26.8
|
1.0
|
|
Fluorine binding site 3 out
of 4 in 7yxd
Go back to
Fluorine Binding Sites List in 7yxd
Fluorine binding site 3 out
of 4 in the Crystal Structure of Wt ANCGR2-Lbd Bound to Dexamethasone and Shp Coregulator Fragment
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 Wt ANCGR2-Lbd Bound to Dexamethasone and Shp Coregulator Fragment within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
H:F1001
b:22.1
occ:1.00
|
F1
|
H:DEX1001
|
0.0
|
22.1
|
1.0
|
C9
|
H:DEX1001
|
1.4
|
23.5
|
1.0
|
C8
|
H:DEX1001
|
2.3
|
23.8
|
1.0
|
C10
|
H:DEX1001
|
2.4
|
26.4
|
1.0
|
C11
|
H:DEX1001
|
2.4
|
19.3
|
1.0
|
C7
|
H:DEX1001
|
2.6
|
21.9
|
1.0
|
C5
|
H:DEX1001
|
2.7
|
25.4
|
1.0
|
C14
|
H:DEX1001
|
2.7
|
22.0
|
1.0
|
C1
|
H:DEX1001
|
2.8
|
35.1
|
1.0
|
CE1
|
H:PHE623
|
3.0
|
33.2
|
1.0
|
C6
|
H:DEX1001
|
3.1
|
23.9
|
1.0
|
C12
|
H:DEX1001
|
3.1
|
20.0
|
1.0
|
C13
|
H:DEX1001
|
3.5
|
25.6
|
1.0
|
O2
|
H:DEX1001
|
3.5
|
22.9
|
1.0
|
C4
|
H:DEX1001
|
3.6
|
31.4
|
1.0
|
C2
|
H:DEX1001
|
3.7
|
36.2
|
1.0
|
CZ
|
H:PHE623
|
3.8
|
28.2
|
1.0
|
C19
|
H:DEX1001
|
3.8
|
24.8
|
1.0
|
CD1
|
H:PHE623
|
3.9
|
31.2
|
1.0
|
C3
|
H:DEX1001
|
4.0
|
32.2
|
1.0
|
C15
|
H:DEX1001
|
4.1
|
24.0
|
1.0
|
CB
|
H:LEU563
|
4.1
|
25.8
|
1.0
|
O3
|
H:DEX1001
|
4.1
|
25.5
|
1.0
|
SD
|
H:MET646
|
4.3
|
38.0
|
1.0
|
CD1
|
H:LEU563
|
4.4
|
37.5
|
1.0
|
C17
|
H:DEX1001
|
4.4
|
29.2
|
1.0
|
CD2
|
H:LEU563
|
4.6
|
39.1
|
1.0
|
CG
|
H:LEU563
|
4.6
|
32.5
|
1.0
|
C18
|
H:DEX1001
|
4.6
|
22.1
|
1.0
|
CE
|
H:MET646
|
4.8
|
31.5
|
1.0
|
O1
|
H:DEX1001
|
4.9
|
42.0
|
1.0
|
O
|
H:LEU563
|
4.9
|
36.7
|
1.0
|
C16
|
H:DEX1001
|
5.0
|
27.6
|
1.0
|
|
Fluorine binding site 4 out
of 4 in 7yxd
Go back to
Fluorine Binding Sites List in 7yxd
Fluorine binding site 4 out
of 4 in the Crystal Structure of Wt ANCGR2-Lbd Bound to Dexamethasone and Shp Coregulator Fragment
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 Wt ANCGR2-Lbd Bound to Dexamethasone and Shp Coregulator Fragment within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
L:F1001
b:21.3
occ:1.00
|
F1
|
L:DEX1001
|
0.0
|
21.3
|
1.0
|
C9
|
L:DEX1001
|
1.4
|
28.9
|
1.0
|
C10
|
L:DEX1001
|
2.3
|
26.2
|
1.0
|
C11
|
L:DEX1001
|
2.3
|
34.8
|
1.0
|
C8
|
L:DEX1001
|
2.3
|
28.1
|
1.0
|
C5
|
L:DEX1001
|
2.7
|
34.5
|
1.0
|
C7
|
L:DEX1001
|
2.7
|
24.7
|
1.0
|
C1
|
L:DEX1001
|
2.7
|
32.6
|
1.0
|
C14
|
L:DEX1001
|
2.8
|
24.7
|
1.0
|
C12
|
L:DEX1001
|
2.9
|
23.4
|
1.0
|
C6
|
L:DEX1001
|
3.2
|
29.7
|
1.0
|
CE1
|
L:PHE623
|
3.3
|
46.9
|
1.0
|
O2
|
L:DEX1001
|
3.5
|
31.5
|
1.0
|
C13
|
L:DEX1001
|
3.5
|
26.2
|
1.0
|
C4
|
L:DEX1001
|
3.5
|
33.2
|
1.0
|
C2
|
L:DEX1001
|
3.6
|
30.7
|
1.0
|
C19
|
L:DEX1001
|
3.7
|
25.1
|
1.0
|
C3
|
L:DEX1001
|
3.9
|
34.0
|
1.0
|
CZ
|
L:PHE623
|
4.1
|
40.3
|
1.0
|
CB
|
L:LEU563
|
4.1
|
26.8
|
1.0
|
C15
|
L:DEX1001
|
4.2
|
23.5
|
1.0
|
CD1
|
L:PHE623
|
4.3
|
46.1
|
1.0
|
O3
|
L:DEX1001
|
4.3
|
22.6
|
1.0
|
CD1
|
L:LEU563
|
4.6
|
26.1
|
1.0
|
C17
|
L:DEX1001
|
4.6
|
26.2
|
1.0
|
SD
|
L:MET646
|
4.6
|
60.2
|
1.0
|
C18
|
L:DEX1001
|
4.7
|
19.1
|
1.0
|
CG
|
L:LEU563
|
4.7
|
24.9
|
1.0
|
CD2
|
L:LEU563
|
4.8
|
30.6
|
1.0
|
O
|
L:LEU563
|
5.0
|
40.2
|
1.0
|
|
Reference:
A.Jimenez-Panizo,
A.Alegre-Marti,
T.T.Tettey,
G.Fettweis,
M.Abella,
R.Anton,
T.A.Johnson,
S.Kim,
R.L.Schiltz,
I.Nunez-Barrios,
J.Font-Diaz,
C.Caelles,
A.F.Valledor,
P.Perez,
A.M.Rojas,
J.Fernandez-Recio,
D.M.Presman,
G.L.Hager,
P.Fuentes-Prior,
E.Estebanez-Perpina.
The Multivalency of the Glucocorticoid Receptor Ligand-Binding Domain Explains Its Manifold Physiological Activities. Nucleic Acids Res. 2022.
ISSN: ESSN 1362-4962
PubMed: 36464162
DOI: 10.1093/NAR/GKAC1119
Page generated: Fri Aug 2 15:54:19 2024
|