Fluorine in PDB 1q6t: The Structure of Phosphotyrosine Phosphatase 1B in Complex with Compound 11
Enzymatic activity of The Structure of Phosphotyrosine Phosphatase 1B in Complex with Compound 11
All present enzymatic activity of The Structure of Phosphotyrosine Phosphatase 1B in Complex with Compound 11:
3.1.3.48;
Protein crystallography data
The structure of The Structure of Phosphotyrosine Phosphatase 1B in Complex with Compound 11, PDB code: 1q6t
was solved by
G.Scapin,
S.B.Patel,
J.W.Becker,
Q.Wang,
C.Desponts,
D.Waddleton,
K.Skorey,
W.Cromlish,
C.Bayly,
M.Therien,
J.Y.Gauthier,
C.S.Li,
C.K.Lau,
C.Ramachandran,
B.P.Kennedy,
E.Asante-Appiah,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
12.00 /
2.30
|
Space group
|
P 21 21 21
|
Cell size a, b, c (Å), α, β, γ (°)
|
88.029,
87.828,
138.926,
90.00,
90.00,
90.00
|
R / Rfree (%)
|
n/a /
n/a
|
Other elements in 1q6t:
The structure of The Structure of Phosphotyrosine Phosphatase 1B in Complex with Compound 11 also contains other interesting chemical elements:
Fluorine Binding Sites:
The binding sites of Fluorine atom in the The Structure of Phosphotyrosine Phosphatase 1B in Complex with Compound 11
(pdb code 1q6t). This binding sites where shown within
5.0 Angstroms radius around Fluorine atom.
In total 4 binding sites of Fluorine where determined in the
The Structure of Phosphotyrosine Phosphatase 1B in Complex with Compound 11, PDB code: 1q6t:
Jump to Fluorine binding site number:
1;
2;
3;
4;
Fluorine binding site 1 out
of 4 in 1q6t
Go back to
Fluorine Binding Sites List in 1q6t
Fluorine binding site 1 out
of 4 in the The Structure of Phosphotyrosine Phosphatase 1B in Complex with Compound 11
Mono view
Stereo pair view
|
A full contact list of Fluorine with other atoms in the F binding
site number 1 of The Structure of Phosphotyrosine Phosphatase 1B in Complex with Compound 11 within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:F801
b:26.4
occ:1.00
|
F53
|
A:600801
|
0.0
|
26.4
|
1.0
|
C52
|
A:600801
|
1.4
|
26.4
|
1.0
|
F54
|
A:600801
|
2.2
|
27.9
|
1.0
|
C14
|
A:600801
|
2.3
|
24.6
|
1.0
|
P55
|
A:600801
|
2.6
|
22.2
|
1.0
|
C13
|
A:600801
|
2.8
|
24.5
|
1.0
|
O58
|
A:600801
|
3.0
|
24.7
|
1.0
|
O57
|
A:600801
|
3.0
|
25.5
|
1.0
|
O
|
A:HOH25
|
3.1
|
26.7
|
1.0
|
CB
|
A:ASP681
|
3.4
|
39.6
|
1.0
|
CE2
|
A:PHE682
|
3.6
|
28.9
|
1.0
|
NH2
|
A:ARG721
|
3.6
|
24.4
|
1.0
|
C15
|
A:600801
|
3.6
|
23.8
|
1.0
|
CZ
|
A:PHE682
|
3.7
|
27.1
|
1.0
|
N
|
A:PHE682
|
3.8
|
34.0
|
1.0
|
CD2
|
A:PHE682
|
3.8
|
28.2
|
1.0
|
CA
|
A:ASP681
|
3.8
|
36.8
|
1.0
|
O56
|
A:600801
|
3.9
|
25.5
|
1.0
|
CE1
|
A:PHE682
|
4.1
|
28.0
|
1.0
|
C12
|
A:600801
|
4.2
|
24.1
|
1.0
|
CG
|
A:PHE682
|
4.2
|
28.6
|
1.0
|
C
|
A:ASP681
|
4.2
|
35.9
|
1.0
|
CZ
|
A:ARG721
|
4.2
|
26.6
|
1.0
|
NE
|
A:ARG721
|
4.3
|
26.3
|
1.0
|
CD1
|
A:PHE682
|
4.3
|
27.8
|
1.0
|
CG
|
A:ASP681
|
4.6
|
43.3
|
1.0
|
CA
|
A:PHE682
|
4.7
|
32.2
|
1.0
|
C10
|
A:600801
|
4.7
|
23.8
|
1.0
|
OD2
|
A:ASP681
|
4.8
|
46.0
|
1.0
|
|
Fluorine binding site 2 out
of 4 in 1q6t
Go back to
Fluorine Binding Sites List in 1q6t
Fluorine binding site 2 out
of 4 in the The Structure of Phosphotyrosine Phosphatase 1B in Complex with Compound 11
Mono view
Stereo pair view
|
A full contact list of Fluorine with other atoms in the F binding
site number 2 of The Structure of Phosphotyrosine Phosphatase 1B in Complex with Compound 11 within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:F801
b:27.9
occ:1.00
|
F54
|
A:600801
|
0.0
|
27.9
|
1.0
|
C52
|
A:600801
|
1.3
|
26.4
|
1.0
|
F53
|
A:600801
|
2.2
|
26.4
|
1.0
|
C14
|
A:600801
|
2.3
|
24.6
|
1.0
|
P55
|
A:600801
|
2.6
|
22.2
|
1.0
|
O
|
A:HOH25
|
2.6
|
26.7
|
1.0
|
C15
|
A:600801
|
2.7
|
23.8
|
1.0
|
O58
|
A:600801
|
3.0
|
24.7
|
1.0
|
O56
|
A:600801
|
3.1
|
25.5
|
1.0
|
CE1
|
A:PHE682
|
3.4
|
28.0
|
1.0
|
CG
|
A:GLN762
|
3.6
|
27.7
|
1.0
|
C13
|
A:600801
|
3.6
|
24.5
|
1.0
|
CZ
|
A:PHE682
|
3.7
|
27.1
|
1.0
|
CD1
|
A:PHE682
|
3.7
|
27.8
|
1.0
|
CA
|
A:GLY720
|
3.8
|
24.3
|
1.0
|
CB
|
A:GLN762
|
3.8
|
27.2
|
1.0
|
O57
|
A:600801
|
3.8
|
25.5
|
1.0
|
N
|
A:GLY720
|
3.9
|
24.0
|
1.0
|
C10
|
A:600801
|
4.1
|
23.8
|
1.0
|
CE2
|
A:PHE682
|
4.3
|
28.9
|
1.0
|
CG
|
A:PHE682
|
4.3
|
28.6
|
1.0
|
N
|
A:PHE682
|
4.5
|
34.0
|
1.0
|
CD2
|
A:PHE682
|
4.5
|
28.2
|
1.0
|
CD
|
A:GLN762
|
4.6
|
28.2
|
1.0
|
CG1
|
A:ILE719
|
4.7
|
21.8
|
1.0
|
C12
|
A:600801
|
4.7
|
24.1
|
1.0
|
OE1
|
A:GLN762
|
4.8
|
28.8
|
1.0
|
N
|
A:ARG721
|
4.8
|
25.6
|
1.0
|
CA
|
A:PHE682
|
4.8
|
32.2
|
1.0
|
C
|
A:GLY720
|
4.8
|
25.6
|
1.0
|
C11
|
A:600801
|
4.9
|
23.6
|
1.0
|
|
Fluorine binding site 3 out
of 4 in 1q6t
Go back to
Fluorine Binding Sites List in 1q6t
Fluorine binding site 3 out
of 4 in the The Structure of Phosphotyrosine Phosphatase 1B in Complex with Compound 11
Mono view
Stereo pair view
|
A full contact list of Fluorine with other atoms in the F binding
site number 3 of The Structure of Phosphotyrosine Phosphatase 1B in Complex with Compound 11 within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:F1301
b:23.2
occ:1.00
|
F53
|
B:6001301
|
0.0
|
23.2
|
1.0
|
C52
|
B:6001301
|
1.4
|
23.6
|
1.0
|
F54
|
B:6001301
|
2.2
|
22.5
|
1.0
|
C14
|
B:6001301
|
2.3
|
20.2
|
1.0
|
P55
|
B:6001301
|
2.6
|
23.2
|
1.0
|
C13
|
B:6001301
|
2.8
|
20.5
|
1.0
|
O58
|
B:6001301
|
3.0
|
23.5
|
1.0
|
O57
|
B:6001301
|
3.0
|
22.1
|
1.0
|
O
|
B:HOH79
|
3.1
|
26.9
|
1.0
|
N
|
B:PHE1182
|
3.5
|
28.9
|
1.0
|
NH2
|
B:ARG1221
|
3.5
|
21.6
|
1.0
|
C15
|
B:6001301
|
3.6
|
19.4
|
1.0
|
CE2
|
B:PHE1182
|
3.6
|
24.4
|
1.0
|
CD2
|
B:PHE1182
|
3.7
|
24.3
|
1.0
|
CZ
|
B:PHE1182
|
3.8
|
21.8
|
1.0
|
O56
|
B:6001301
|
3.9
|
23.4
|
1.0
|
CG
|
B:PHE1182
|
3.9
|
25.3
|
1.0
|
CA
|
B:ASP1181
|
4.0
|
33.1
|
1.0
|
CE1
|
B:PHE1182
|
4.0
|
22.4
|
1.0
|
CD1
|
B:PHE1182
|
4.1
|
23.7
|
1.0
|
CB
|
B:ASP1181
|
4.1
|
34.7
|
1.0
|
C
|
B:ASP1181
|
4.2
|
31.6
|
1.0
|
CZ
|
B:ARG1221
|
4.2
|
23.9
|
1.0
|
C12
|
B:6001301
|
4.2
|
21.2
|
1.0
|
NE
|
B:ARG1221
|
4.2
|
23.9
|
1.0
|
CA
|
B:PHE1182
|
4.3
|
28.7
|
1.0
|
CD1
|
B:LEU1119
|
4.6
|
54.3
|
1.0
|
OD1
|
B:ASP1181
|
4.7
|
39.0
|
1.0
|
CB
|
B:PHE1182
|
4.7
|
26.1
|
1.0
|
C10
|
B:6001301
|
4.7
|
21.1
|
1.0
|
CG
|
B:ASP1181
|
4.9
|
38.3
|
1.0
|
|
Fluorine binding site 4 out
of 4 in 1q6t
Go back to
Fluorine Binding Sites List in 1q6t
Fluorine binding site 4 out
of 4 in the The Structure of Phosphotyrosine Phosphatase 1B in Complex with Compound 11
Mono view
Stereo pair view
|
A full contact list of Fluorine with other atoms in the F binding
site number 4 of The Structure of Phosphotyrosine Phosphatase 1B in Complex with Compound 11 within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:F1301
b:22.5
occ:1.00
|
F54
|
B:6001301
|
0.0
|
22.5
|
1.0
|
C52
|
B:6001301
|
1.4
|
23.6
|
1.0
|
F53
|
B:6001301
|
2.2
|
23.2
|
1.0
|
C14
|
B:6001301
|
2.4
|
20.2
|
1.0
|
P55
|
B:6001301
|
2.6
|
23.2
|
1.0
|
O
|
B:HOH79
|
2.7
|
26.9
|
1.0
|
C15
|
B:6001301
|
2.8
|
19.4
|
1.0
|
O58
|
B:6001301
|
3.0
|
23.5
|
1.0
|
O56
|
B:6001301
|
3.1
|
23.4
|
1.0
|
CE1
|
B:PHE1182
|
3.3
|
22.4
|
1.0
|
CG
|
B:GLN1262
|
3.4
|
26.6
|
1.0
|
CD1
|
B:PHE1182
|
3.5
|
23.7
|
1.0
|
C13
|
B:6001301
|
3.6
|
20.5
|
1.0
|
CB
|
B:GLN1262
|
3.7
|
25.8
|
1.0
|
CZ
|
B:PHE1182
|
3.7
|
21.8
|
1.0
|
CA
|
B:GLY1220
|
3.7
|
22.3
|
1.0
|
O57
|
B:6001301
|
3.8
|
22.1
|
1.0
|
N
|
B:GLY1220
|
4.0
|
23.5
|
1.0
|
CG
|
B:PHE1182
|
4.0
|
25.3
|
1.0
|
C10
|
B:6001301
|
4.1
|
21.1
|
1.0
|
CE2
|
B:PHE1182
|
4.3
|
24.4
|
1.0
|
N
|
B:PHE1182
|
4.3
|
28.9
|
1.0
|
CD2
|
B:PHE1182
|
4.4
|
24.3
|
1.0
|
CA
|
B:PHE1182
|
4.5
|
28.7
|
1.0
|
CD
|
B:GLN1262
|
4.6
|
25.5
|
1.0
|
OE1
|
B:GLN1262
|
4.7
|
27.9
|
1.0
|
N
|
B:ARG1221
|
4.8
|
24.3
|
1.0
|
C
|
B:GLY1220
|
4.8
|
23.5
|
1.0
|
C12
|
B:6001301
|
4.8
|
21.2
|
1.0
|
CG1
|
B:ILE1219
|
4.8
|
19.3
|
1.0
|
CB
|
B:PHE1182
|
4.9
|
26.1
|
1.0
|
C11
|
B:6001301
|
5.0
|
21.9
|
1.0
|
|
Reference:
G.Scapin,
S.B.Patel,
J.W.Becker,
Q.Wang,
C.Desponts,
D.Waddleton,
K.Skorey,
W.Cromlish,
C.Bayly,
M.Therien,
J.Y.Gauthier,
C.S.Li,
C.K.Lau,
C.Ramachandran,
B.P.Kennedy,
E.Asante-Appiah.
The Structural Basis For the Selectivity of Benzotriazole Inhibitors of PTP1B Biochemistry V. 42 11451 2003.
ISSN: ISSN 0006-2960
PubMed: 14516196
DOI: 10.1021/BI035098J
Page generated: Wed Jul 31 12:32:11 2024
|