Fluorine in PDB 3vhe: Crystal Structure of Human VEGFR2 Kinase Domain with A Novel Pyrrolopyrimidine Inhibitor.
Enzymatic activity of Crystal Structure of Human VEGFR2 Kinase Domain with A Novel Pyrrolopyrimidine Inhibitor.
All present enzymatic activity of Crystal Structure of Human VEGFR2 Kinase Domain with A Novel Pyrrolopyrimidine Inhibitor.:
2.7.10.1;
Protein crystallography data
The structure of Crystal Structure of Human VEGFR2 Kinase Domain with A Novel Pyrrolopyrimidine Inhibitor., PDB code: 3vhe
was solved by
Y.Oguro,
N.Miyamoto,
K.Okada,
T.Takagi,
H.Iwata,
Y.Awazu,
H.Miki,
A.Hori,
K.Kamiyama,
S.Imanura,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
19.84 /
1.55
|
Space group
|
C 1 2 1
|
Cell size a, b, c (Å), α, β, γ (°)
|
134.340,
56.270,
52.070,
90.00,
95.24,
90.00
|
R / Rfree (%)
|
n/a /
n/a
|
Fluorine Binding Sites:
The binding sites of Fluorine atom in the Crystal Structure of Human VEGFR2 Kinase Domain with A Novel Pyrrolopyrimidine Inhibitor.
(pdb code 3vhe). 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 Human VEGFR2 Kinase Domain with A Novel Pyrrolopyrimidine Inhibitor., PDB code: 3vhe:
Jump to Fluorine binding site number:
1;
2;
3;
4;
Fluorine binding site 1 out
of 4 in 3vhe
Go back to
Fluorine Binding Sites List in 3vhe
Fluorine binding site 1 out
of 4 in the Crystal Structure of Human VEGFR2 Kinase Domain with A Novel Pyrrolopyrimidine 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 Human VEGFR2 Kinase Domain with A Novel Pyrrolopyrimidine Inhibitor. within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:F1170
b:13.7
occ:1.00
|
F34
|
A:42Q1170
|
0.0
|
13.7
|
1.0
|
C22
|
A:42Q1170
|
1.3
|
12.2
|
1.0
|
C21
|
A:42Q1170
|
2.4
|
10.4
|
1.0
|
C23
|
A:42Q1170
|
2.4
|
11.2
|
1.0
|
N27
|
A:42Q1170
|
2.7
|
11.2
|
1.0
|
CG1
|
A:VAL916
|
3.5
|
10.0
|
1.0
|
CB
|
A:LYS868
|
3.5
|
11.2
|
1.0
|
C20
|
A:42Q1170
|
3.7
|
11.2
|
1.0
|
C18
|
A:42Q1170
|
3.7
|
10.1
|
1.0
|
CD
|
A:LYS868
|
3.7
|
13.8
|
1.0
|
CG2
|
A:VAL916
|
3.7
|
11.4
|
1.0
|
C28
|
A:42Q1170
|
3.8
|
11.1
|
1.0
|
C19
|
A:42Q1170
|
4.2
|
10.7
|
1.0
|
CG
|
A:LYS868
|
4.2
|
13.2
|
1.0
|
CB
|
A:VAL916
|
4.3
|
9.9
|
1.0
|
CG1
|
A:VAL914
|
4.4
|
13.1
|
1.0
|
OE2
|
A:GLU885
|
4.5
|
15.3
|
1.0
|
O31
|
A:42Q1170
|
4.5
|
11.7
|
1.0
|
O
|
A:VAL914
|
4.6
|
10.1
|
1.0
|
N29
|
A:42Q1170
|
4.6
|
11.5
|
1.0
|
CG2
|
A:VAL899
|
4.7
|
21.1
|
1.0
|
N
|
A:LYS868
|
4.7
|
9.8
|
1.0
|
CA
|
A:LYS868
|
4.7
|
10.0
|
1.0
|
O17
|
A:42Q1170
|
4.9
|
10.7
|
1.0
|
CB
|
A:VAL914
|
5.0
|
11.6
|
1.0
|
N4
|
A:42Q1170
|
5.0
|
11.7
|
1.0
|
|
Fluorine binding site 2 out
of 4 in 3vhe
Go back to
Fluorine Binding Sites List in 3vhe
Fluorine binding site 2 out
of 4 in the Crystal Structure of Human VEGFR2 Kinase Domain with A Novel Pyrrolopyrimidine 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 Human VEGFR2 Kinase Domain with A Novel Pyrrolopyrimidine Inhibitor. within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:F1170
b:23.5
occ:1.00
|
F45
|
A:42Q1170
|
0.0
|
23.5
|
1.0
|
C44
|
A:42Q1170
|
1.3
|
18.5
|
1.0
|
F47
|
A:42Q1170
|
2.2
|
21.6
|
1.0
|
F46
|
A:42Q1170
|
2.2
|
20.7
|
1.0
|
C38
|
A:42Q1170
|
2.3
|
16.4
|
1.0
|
C39
|
A:42Q1170
|
3.0
|
12.6
|
1.0
|
C37
|
A:42Q1170
|
3.4
|
16.5
|
1.0
|
CG1
|
A:VAL898
|
3.4
|
14.8
|
1.0
|
CG1
|
A:VAL899
|
4.0
|
20.1
|
1.0
|
O
|
A:ILE1044
|
4.0
|
10.2
|
1.0
|
CD1
|
A:ILE892
|
4.3
|
12.4
|
1.0
|
C30
|
A:42Q1170
|
4.3
|
13.7
|
1.0
|
CD2
|
A:LEU889
|
4.5
|
14.5
|
1.0
|
C
|
A:ILE1044
|
4.6
|
9.8
|
1.0
|
CD1
|
A:LEU1019
|
4.6
|
17.3
|
1.0
|
CA
|
A:CYS1045
|
4.6
|
9.8
|
1.0
|
CG2
|
A:ILE1044
|
4.6
|
14.3
|
1.0
|
C36
|
A:42Q1170
|
4.6
|
15.3
|
1.0
|
CB
|
A:VAL898
|
4.8
|
12.1
|
1.0
|
N
|
A:CYS1045
|
4.9
|
9.5
|
1.0
|
N
|
A:VAL899
|
4.9
|
11.0
|
1.0
|
CB
|
A:ILE1044
|
5.0
|
10.4
|
1.0
|
O31
|
A:42Q1170
|
5.0
|
11.7
|
1.0
|
|
Fluorine binding site 3 out
of 4 in 3vhe
Go back to
Fluorine Binding Sites List in 3vhe
Fluorine binding site 3 out
of 4 in the Crystal Structure of Human VEGFR2 Kinase Domain with A Novel Pyrrolopyrimidine 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 Human VEGFR2 Kinase Domain with A Novel Pyrrolopyrimidine Inhibitor. within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:F1170
b:20.7
occ:1.00
|
F46
|
A:42Q1170
|
0.0
|
20.7
|
1.0
|
C44
|
A:42Q1170
|
1.3
|
18.5
|
1.0
|
F47
|
A:42Q1170
|
2.2
|
21.6
|
1.0
|
F45
|
A:42Q1170
|
2.2
|
23.5
|
1.0
|
C38
|
A:42Q1170
|
2.3
|
16.4
|
1.0
|
C39
|
A:42Q1170
|
2.9
|
12.6
|
1.0
|
C
|
A:CYS1045
|
3.3
|
9.5
|
1.0
|
CA
|
A:CYS1045
|
3.4
|
9.8
|
1.0
|
CG2
|
A:ILE1044
|
3.4
|
14.3
|
1.0
|
C37
|
A:42Q1170
|
3.5
|
16.5
|
1.0
|
O
|
A:CYS1045
|
3.5
|
9.3
|
1.0
|
CD2
|
A:HIS1026
|
3.5
|
12.5
|
1.0
|
NE2
|
A:HIS1026
|
3.6
|
12.7
|
1.0
|
N
|
A:CYS1045
|
3.6
|
9.5
|
1.0
|
C
|
A:ILE1044
|
3.8
|
9.8
|
1.0
|
N
|
A:ASP1046
|
3.8
|
10.3
|
1.0
|
O
|
A:ILE1044
|
3.9
|
10.2
|
1.0
|
CB
|
A:ASP1046
|
4.3
|
12.6
|
1.0
|
C30
|
A:42Q1170
|
4.3
|
13.7
|
1.0
|
CB
|
A:ILE1044
|
4.3
|
10.4
|
1.0
|
O
|
A:HOH2067
|
4.4
|
26.0
|
1.0
|
O31
|
A:42Q1170
|
4.6
|
11.7
|
1.0
|
CA
|
A:ASP1046
|
4.6
|
10.4
|
1.0
|
C36
|
A:42Q1170
|
4.7
|
15.3
|
1.0
|
CE1
|
A:HIS1026
|
4.7
|
12.9
|
1.0
|
CG
|
A:HIS1026
|
4.7
|
12.5
|
1.0
|
CA
|
A:ILE1044
|
4.7
|
8.4
|
1.0
|
CB
|
A:CYS1045
|
4.8
|
10.1
|
1.0
|
CG1
|
A:VAL899
|
4.9
|
20.1
|
1.0
|
C35
|
A:42Q1170
|
5.0
|
14.9
|
1.0
|
|
Fluorine binding site 4 out
of 4 in 3vhe
Go back to
Fluorine Binding Sites List in 3vhe
Fluorine binding site 4 out
of 4 in the Crystal Structure of Human VEGFR2 Kinase Domain with A Novel Pyrrolopyrimidine 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 Human VEGFR2 Kinase Domain with A Novel Pyrrolopyrimidine Inhibitor. within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:F1170
b:21.6
occ:1.00
|
F47
|
A:42Q1170
|
0.0
|
21.6
|
1.0
|
C44
|
A:42Q1170
|
1.3
|
18.5
|
1.0
|
F45
|
A:42Q1170
|
2.2
|
23.5
|
1.0
|
F46
|
A:42Q1170
|
2.2
|
20.7
|
1.0
|
C38
|
A:42Q1170
|
2.3
|
16.4
|
1.0
|
C37
|
A:42Q1170
|
2.7
|
16.5
|
1.0
|
CD1
|
A:LEU1019
|
3.6
|
17.3
|
1.0
|
CD2
|
A:LEU1019
|
3.7
|
17.8
|
1.0
|
C39
|
A:42Q1170
|
3.7
|
12.6
|
1.0
|
O
|
A:HOH2067
|
4.0
|
26.0
|
1.0
|
CD2
|
A:HIS1026
|
4.0
|
12.5
|
1.0
|
C36
|
A:42Q1170
|
4.1
|
15.3
|
1.0
|
CD1
|
A:ILE892
|
4.2
|
12.4
|
1.0
|
CG
|
A:LEU1019
|
4.3
|
16.8
|
1.0
|
O
|
A:HOH2109
|
4.4
|
29.8
|
1.0
|
NE2
|
A:HIS1026
|
4.6
|
12.7
|
1.0
|
CG2
|
A:ILE1044
|
4.6
|
14.3
|
1.0
|
CG
|
A:HIS1026
|
4.7
|
12.5
|
1.0
|
C30
|
A:42Q1170
|
4.8
|
13.7
|
1.0
|
|
Reference:
Y.Oguro,
N.Miyamoto,
K.Okada,
T.Takagi,
H.Iwata,
Y.Awazu,
H.Miki,
A.Hori,
K.Kamiyama,
S.Imamura.
Design, Synthesis, and Evaluation of 5-Methyl-4-Phenoxy-5H-Pyrrolo[3,2-D]Pyrimidine Derivatives: Novel VEGFR2 Kinase Inhibitors Binding to Inactive Kinase Conformation. Bioorg.Med.Chem. V. 18 7260 2010.
ISSN: ISSN 0968-0896
PubMed: 20833055
DOI: 10.1016/J.BMC.2010.08.017
Page generated: Wed Jul 31 23:17:40 2024
|