Fluorine in PDB 2y1w: Crystal Structure of Coactivator Associated Arginine Methyltransferase 1 (CARM1) in Complex with Sinefungin and Indole Inhibitor
Enzymatic activity of Crystal Structure of Coactivator Associated Arginine Methyltransferase 1 (CARM1) in Complex with Sinefungin and Indole Inhibitor
All present enzymatic activity of Crystal Structure of Coactivator Associated Arginine Methyltransferase 1 (CARM1) in Complex with Sinefungin and Indole Inhibitor:
2.1.1.125;
Protein crystallography data
The structure of Crystal Structure of Coactivator Associated Arginine Methyltransferase 1 (CARM1) in Complex with Sinefungin and Indole Inhibitor, PDB code: 2y1w
was solved by
J.S.Sack,
S.Thieffine,
T.Bandiera,
M.Fasolini,
G.J.Duke,
L.Jayaraman,
K.F.Kish,
H.E.Klei,
A.V.Purandare,
P.Rosettani,
S.Troiani,
D.Xie,
J.A.Bertrand,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
29.88 /
2.10
|
Space group
|
P 21 21 2
|
Cell size a, b, c (Å), α, β, γ (°)
|
74.896,
98.471,
207.184,
90.00,
90.00,
90.00
|
R / Rfree (%)
|
20.5 /
24.4
|
Fluorine Binding Sites:
The binding sites of Fluorine atom in the Crystal Structure of Coactivator Associated Arginine Methyltransferase 1 (CARM1) in Complex with Sinefungin and Indole Inhibitor
(pdb code 2y1w). 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 Coactivator Associated Arginine Methyltransferase 1 (CARM1) in Complex with Sinefungin and Indole Inhibitor, PDB code: 2y1w:
Jump to Fluorine binding site number:
1;
2;
3;
4;
Fluorine binding site 1 out
of 4 in 2y1w
Go back to
Fluorine Binding Sites List in 2y1w
Fluorine binding site 1 out
of 4 in the Crystal Structure of Coactivator Associated Arginine Methyltransferase 1 (CARM1) in Complex with Sinefungin and Indole Inhibitor
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 Coactivator Associated Arginine Methyltransferase 1 (CARM1) in Complex with Sinefungin and Indole Inhibitor within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:F1005
b:45.6
occ:1.00
|
F28
|
A:8491005
|
0.0
|
45.6
|
1.0
|
C9
|
A:8491005
|
1.4
|
43.4
|
1.0
|
C5
|
A:8491005
|
2.4
|
42.2
|
1.0
|
C8
|
A:8491005
|
2.5
|
43.9
|
1.0
|
C1
|
A:8491005
|
3.1
|
39.6
|
1.0
|
C10
|
A:8491005
|
3.2
|
44.8
|
1.0
|
CE2
|
A:TYR154
|
3.3
|
34.5
|
1.0
|
CD2
|
A:PHE153
|
3.3
|
34.3
|
1.0
|
C25
|
A:8491005
|
3.4
|
44.1
|
1.0
|
CE2
|
A:PHE153
|
3.5
|
30.2
|
1.0
|
OH
|
A:TYR154
|
3.5
|
30.9
|
1.0
|
CZ
|
A:TYR154
|
3.6
|
34.4
|
1.0
|
C6
|
A:8491005
|
3.6
|
42.5
|
1.0
|
CE1
|
A:TYR150
|
3.7
|
34.3
|
1.0
|
N7
|
A:8491005
|
3.7
|
43.9
|
1.0
|
CD1
|
A:TYR150
|
3.8
|
34.2
|
1.0
|
OE1
|
A:GLU267
|
3.9
|
34.5
|
1.0
|
CG
|
A:PHE153
|
4.0
|
34.9
|
1.0
|
CD
|
A:GLU267
|
4.0
|
32.3
|
1.0
|
CD2
|
A:TYR154
|
4.2
|
35.7
|
1.0
|
CZ
|
A:PHE153
|
4.2
|
32.3
|
1.0
|
OE2
|
A:GLU267
|
4.3
|
34.1
|
1.0
|
C21
|
A:8491005
|
4.3
|
44.7
|
1.0
|
CG
|
A:GLU267
|
4.5
|
31.0
|
1.0
|
CB
|
A:PHE153
|
4.6
|
36.4
|
1.0
|
C2
|
A:8491005
|
4.6
|
40.2
|
1.0
|
C24
|
A:8491005
|
4.6
|
46.1
|
1.0
|
CE1
|
A:TYR154
|
4.6
|
35.4
|
1.0
|
CZ
|
A:TYR150
|
4.6
|
34.4
|
1.0
|
CD1
|
A:PHE153
|
4.6
|
34.2
|
1.0
|
CE1
|
A:PHE153
|
4.7
|
33.9
|
1.0
|
CG
|
A:TYR150
|
4.8
|
33.2
|
1.0
|
O26
|
A:8491005
|
4.9
|
43.6
|
1.0
|
C4
|
A:8491005
|
4.9
|
40.2
|
1.0
|
O
|
A:TYR150
|
4.9
|
37.4
|
1.0
|
|
Fluorine binding site 2 out
of 4 in 2y1w
Go back to
Fluorine Binding Sites List in 2y1w
Fluorine binding site 2 out
of 4 in the Crystal Structure of Coactivator Associated Arginine Methyltransferase 1 (CARM1) in Complex with Sinefungin and Indole Inhibitor
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 Coactivator Associated Arginine Methyltransferase 1 (CARM1) in Complex with Sinefungin and Indole Inhibitor within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:F1005
b:46.3
occ:1.00
|
F28
|
B:8491005
|
0.0
|
46.3
|
1.0
|
C9
|
B:8491005
|
1.4
|
45.5
|
1.0
|
C5
|
B:8491005
|
2.4
|
44.6
|
1.0
|
C8
|
B:8491005
|
2.5
|
48.3
|
1.0
|
C1
|
B:8491005
|
3.1
|
42.8
|
1.0
|
C10
|
B:8491005
|
3.2
|
50.0
|
1.0
|
CE2
|
B:TYR154
|
3.3
|
30.5
|
1.0
|
CD2
|
B:PHE153
|
3.4
|
30.7
|
1.0
|
C25
|
B:8491005
|
3.5
|
50.2
|
1.0
|
CE2
|
B:PHE153
|
3.6
|
31.4
|
1.0
|
C6
|
B:8491005
|
3.6
|
45.6
|
1.0
|
CE1
|
B:TYR150
|
3.6
|
30.5
|
1.0
|
OH
|
B:TYR154
|
3.6
|
31.1
|
1.0
|
N7
|
B:8491005
|
3.7
|
45.5
|
1.0
|
CZ
|
B:TYR154
|
3.7
|
31.1
|
1.0
|
CD1
|
B:TYR150
|
3.7
|
31.5
|
1.0
|
OE1
|
B:GLU267
|
3.9
|
33.9
|
1.0
|
CD
|
B:GLU267
|
4.0
|
33.4
|
1.0
|
CG
|
B:PHE153
|
4.1
|
32.6
|
1.0
|
CD2
|
B:TYR154
|
4.1
|
30.8
|
1.0
|
C21
|
B:8491005
|
4.3
|
51.4
|
1.0
|
OE2
|
B:GLU267
|
4.3
|
33.7
|
1.0
|
CZ
|
B:PHE153
|
4.3
|
32.8
|
1.0
|
CG
|
B:GLU267
|
4.4
|
32.4
|
1.0
|
C2
|
B:8491005
|
4.5
|
43.0
|
1.0
|
CZ
|
B:TYR150
|
4.6
|
31.4
|
1.0
|
CB
|
B:PHE153
|
4.6
|
30.8
|
1.0
|
CE1
|
B:TYR154
|
4.7
|
27.8
|
1.0
|
C24
|
B:8491005
|
4.7
|
52.5
|
1.0
|
CG
|
B:TYR150
|
4.7
|
32.0
|
1.0
|
O26
|
B:8491005
|
4.7
|
50.4
|
1.0
|
CD1
|
B:PHE153
|
4.8
|
31.2
|
1.0
|
O
|
B:TYR150
|
4.8
|
32.8
|
1.0
|
C4
|
B:8491005
|
4.9
|
44.1
|
1.0
|
CE1
|
B:PHE153
|
4.9
|
35.8
|
1.0
|
|
Fluorine binding site 3 out
of 4 in 2y1w
Go back to
Fluorine Binding Sites List in 2y1w
Fluorine binding site 3 out
of 4 in the Crystal Structure of Coactivator Associated Arginine Methyltransferase 1 (CARM1) in Complex with Sinefungin and Indole Inhibitor
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 Coactivator Associated Arginine Methyltransferase 1 (CARM1) in Complex with Sinefungin and Indole Inhibitor within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
C:F1005
b:48.3
occ:1.00
|
F28
|
C:8491005
|
0.0
|
48.3
|
1.0
|
C9
|
C:8491005
|
1.4
|
48.2
|
1.0
|
C5
|
C:8491005
|
2.4
|
46.7
|
1.0
|
C8
|
C:8491005
|
2.5
|
49.4
|
1.0
|
C1
|
C:8491005
|
3.1
|
42.6
|
1.0
|
C10
|
C:8491005
|
3.2
|
50.9
|
1.0
|
CD2
|
C:PHE153
|
3.3
|
35.5
|
1.0
|
CE2
|
C:TYR154
|
3.3
|
27.6
|
1.0
|
CE2
|
C:PHE153
|
3.4
|
37.9
|
1.0
|
C25
|
C:8491005
|
3.4
|
51.6
|
1.0
|
OH
|
C:TYR154
|
3.5
|
29.8
|
1.0
|
CZ
|
C:TYR154
|
3.5
|
29.0
|
1.0
|
C6
|
C:8491005
|
3.6
|
47.0
|
1.0
|
CE1
|
C:TYR150
|
3.7
|
33.3
|
1.0
|
N7
|
C:8491005
|
3.7
|
48.9
|
1.0
|
CD1
|
C:TYR150
|
3.8
|
34.5
|
1.0
|
OE1
|
C:GLU267
|
3.9
|
30.5
|
1.0
|
CG
|
C:PHE153
|
4.0
|
36.2
|
1.0
|
CD
|
C:GLU267
|
4.0
|
33.1
|
1.0
|
CD2
|
C:TYR154
|
4.1
|
29.1
|
1.0
|
CZ
|
C:PHE153
|
4.2
|
37.2
|
1.0
|
OE2
|
C:GLU267
|
4.3
|
34.0
|
1.0
|
C21
|
C:8491005
|
4.4
|
51.8
|
1.0
|
CE1
|
C:TYR154
|
4.5
|
29.5
|
1.0
|
CB
|
C:PHE153
|
4.5
|
34.3
|
1.0
|
CG
|
C:GLU267
|
4.5
|
31.1
|
1.0
|
C2
|
C:8491005
|
4.6
|
41.2
|
1.0
|
CZ
|
C:TYR150
|
4.6
|
35.2
|
1.0
|
C24
|
C:8491005
|
4.6
|
52.0
|
1.0
|
CD1
|
C:PHE153
|
4.7
|
36.6
|
1.0
|
CE1
|
C:PHE153
|
4.8
|
37.3
|
1.0
|
O
|
C:TYR150
|
4.8
|
34.4
|
1.0
|
CG
|
C:TYR150
|
4.8
|
35.5
|
1.0
|
C4
|
C:8491005
|
4.9
|
45.5
|
1.0
|
O26
|
C:8491005
|
4.9
|
50.4
|
1.0
|
CG
|
C:TYR154
|
5.0
|
29.0
|
1.0
|
|
Fluorine binding site 4 out
of 4 in 2y1w
Go back to
Fluorine Binding Sites List in 2y1w
Fluorine binding site 4 out
of 4 in the Crystal Structure of Coactivator Associated Arginine Methyltransferase 1 (CARM1) in Complex with Sinefungin and Indole Inhibitor
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 Coactivator Associated Arginine Methyltransferase 1 (CARM1) in Complex with Sinefungin and Indole Inhibitor within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
D:F1005
b:38.5
occ:1.00
|
F28
|
D:8491005
|
0.0
|
38.5
|
1.0
|
C9
|
D:8491005
|
1.4
|
37.0
|
1.0
|
C5
|
D:8491005
|
2.5
|
35.8
|
1.0
|
C8
|
D:8491005
|
2.5
|
36.8
|
1.0
|
C1
|
D:8491005
|
3.2
|
34.2
|
1.0
|
C10
|
D:8491005
|
3.2
|
38.3
|
1.0
|
CE2
|
D:TYR154
|
3.3
|
25.0
|
1.0
|
CD1
|
D:PHE153
|
3.3
|
28.7
|
1.0
|
C25
|
D:8491005
|
3.4
|
39.2
|
1.0
|
CE1
|
D:PHE153
|
3.5
|
29.5
|
1.0
|
OH
|
D:TYR154
|
3.5
|
25.7
|
1.0
|
CZ
|
D:TYR154
|
3.6
|
27.3
|
1.0
|
C6
|
D:8491005
|
3.6
|
34.3
|
1.0
|
CE1
|
D:TYR150
|
3.6
|
30.7
|
1.0
|
N7
|
D:8491005
|
3.7
|
37.2
|
1.0
|
CD1
|
D:TYR150
|
3.8
|
27.9
|
1.0
|
OE1
|
D:GLU267
|
4.0
|
28.6
|
1.0
|
CG
|
D:PHE153
|
4.0
|
31.0
|
1.0
|
CD
|
D:GLU267
|
4.0
|
28.3
|
1.0
|
CD2
|
D:TYR154
|
4.2
|
26.4
|
1.0
|
CZ
|
D:PHE153
|
4.2
|
29.8
|
1.0
|
OE2
|
D:GLU267
|
4.4
|
29.8
|
1.0
|
C21
|
D:8491005
|
4.4
|
38.5
|
1.0
|
CG
|
D:GLU267
|
4.5
|
25.5
|
1.0
|
CB
|
D:PHE153
|
4.6
|
29.8
|
1.0
|
C2
|
D:8491005
|
4.6
|
34.5
|
1.0
|
CE1
|
D:TYR154
|
4.6
|
28.3
|
1.0
|
CZ
|
D:TYR150
|
4.6
|
30.3
|
1.0
|
C24
|
D:8491005
|
4.6
|
38.7
|
1.0
|
CD2
|
D:PHE153
|
4.7
|
30.2
|
1.0
|
CE2
|
D:PHE153
|
4.7
|
31.7
|
1.0
|
O
|
D:TYR150
|
4.8
|
28.1
|
1.0
|
CG
|
D:TYR150
|
4.8
|
28.9
|
1.0
|
C4
|
D:8491005
|
4.9
|
34.7
|
1.0
|
O26
|
D:8491005
|
4.9
|
40.8
|
1.0
|
|
Reference:
J.S.Sack,
S.Thieffine,
T.Bandiera,
M.Fasolini,
G.J.Duke,
L.Jayaraman,
K.F.Kish,
H.E.Klei,
A.V.Purandare,
P.Rosettani,
S.Troiani,
D.Xie,
J.A.Bertrand.
Structural Basis For CARM1 Inhibition By Indole and Pyrazole Inhibitors Biochem.J. V. 436 331 2011.
ISSN: ISSN 0264-6021
PubMed: 21410432
DOI: 10.1042/BJ20102161
Page generated: Wed Jul 31 16:43:45 2024
|