Fluorine in PDB 6ebr: Activation of RR02 Bound to BEF3
Protein crystallography data
The structure of Activation of RR02 Bound to BEF3, PDB code: 6ebr
was solved by
A.Riboldi-Tunnicliffe,
S.Panjikar,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
37.35 /
1.82
|
Space group
|
C 2 2 21
|
Cell size a, b, c (Å), α, β, γ (°)
|
74.705,
93.404,
37.611,
90.00,
90.00,
90.00
|
R / Rfree (%)
|
16.9 /
19.9
|
Other elements in 6ebr:
The structure of Activation of RR02 Bound to BEF3 also contains other interesting chemical elements:
Fluorine Binding Sites:
The binding sites of Fluorine atom in the Activation of RR02 Bound to BEF3
(pdb code 6ebr). This binding sites where shown within
5.0 Angstroms radius around Fluorine atom.
In total 3 binding sites of Fluorine where determined in the
Activation of RR02 Bound to BEF3, PDB code: 6ebr:
Jump to Fluorine binding site number:
1;
2;
3;
Fluorine binding site 1 out
of 3 in 6ebr
Go back to
Fluorine Binding Sites List in 6ebr
Fluorine binding site 1 out
of 3 in the Activation of RR02 Bound to BEF3
Mono view
Stereo pair view
|
A full contact list of Fluorine with other atoms in the F binding
site number 1 of Activation of RR02 Bound to BEF3 within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:F201
b:20.3
occ:1.00
|
F1
|
A:BEF201
|
0.0
|
20.3
|
1.0
|
BE
|
A:BEF201
|
1.5
|
19.5
|
1.0
|
F2
|
A:BEF201
|
2.5
|
21.6
|
1.0
|
F3
|
A:BEF201
|
2.5
|
22.5
|
1.0
|
OD1
|
A:ASP52
|
2.5
|
25.1
|
1.0
|
NZ
|
A:LYS101
|
2.9
|
23.7
|
1.0
|
N
|
A:ALA80
|
2.9
|
23.6
|
1.0
|
O
|
A:HOH402
|
3.0
|
39.2
|
1.0
|
CA
|
A:SER79
|
3.3
|
21.0
|
1.0
|
CE
|
A:LYS101
|
3.4
|
21.7
|
1.0
|
OG
|
A:SER79
|
3.5
|
22.9
|
1.0
|
C
|
A:SER79
|
3.6
|
26.9
|
1.0
|
CD
|
A:LYS101
|
3.6
|
23.0
|
1.0
|
CG
|
A:ASP52
|
3.7
|
26.5
|
1.0
|
CB
|
A:SER79
|
3.8
|
21.3
|
1.0
|
O
|
A:HOH316
|
3.9
|
41.6
|
1.0
|
CB
|
A:ALA80
|
4.0
|
25.8
|
1.0
|
O
|
A:HOH339
|
4.0
|
26.1
|
1.0
|
CA
|
A:ALA80
|
4.0
|
28.1
|
1.0
|
O
|
A:LEU78
|
4.2
|
16.7
|
1.0
|
MN
|
A:MN202
|
4.3
|
21.3
|
1.0
|
OD2
|
A:ASP52
|
4.3
|
19.5
|
1.0
|
CG
|
A:LYS101
|
4.5
|
21.1
|
1.0
|
N
|
A:SER79
|
4.5
|
17.4
|
1.0
|
O
|
A:SER79
|
4.8
|
22.6
|
1.0
|
C
|
A:LEU78
|
4.8
|
16.7
|
1.0
|
N
|
A:LEU53
|
4.8
|
19.2
|
1.0
|
CB
|
A:ASP52
|
4.8
|
17.5
|
1.0
|
N
|
A:LYS81
|
4.9
|
25.6
|
1.0
|
CG
|
A:MET54
|
4.9
|
31.7
|
1.0
|
N
|
A:MET54
|
5.0
|
21.9
|
1.0
|
OD2
|
A:ASP8
|
5.0
|
23.3
|
1.0
|
|
Fluorine binding site 2 out
of 3 in 6ebr
Go back to
Fluorine Binding Sites List in 6ebr
Fluorine binding site 2 out
of 3 in the Activation of RR02 Bound to BEF3
Mono view
Stereo pair view
|
A full contact list of Fluorine with other atoms in the F binding
site number 2 of Activation of RR02 Bound to BEF3 within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:F201
b:21.6
occ:1.00
|
F2
|
A:BEF201
|
0.0
|
21.6
|
1.0
|
BE
|
A:BEF201
|
1.6
|
19.5
|
1.0
|
MN
|
A:MN202
|
2.1
|
21.3
|
1.0
|
F3
|
A:BEF201
|
2.4
|
22.5
|
1.0
|
F1
|
A:BEF201
|
2.5
|
20.3
|
1.0
|
OD1
|
A:ASP52
|
2.5
|
25.1
|
1.0
|
OD2
|
A:ASP52
|
3.0
|
19.5
|
1.0
|
CG
|
A:ASP52
|
3.1
|
26.5
|
1.0
|
CB
|
A:MET54
|
3.1
|
27.6
|
1.0
|
O
|
A:MET54
|
3.2
|
25.1
|
1.0
|
O
|
A:HOH394
|
3.2
|
44.5
|
1.0
|
O
|
A:HOH339
|
3.2
|
26.1
|
1.0
|
N
|
A:MET54
|
3.4
|
21.9
|
1.0
|
O
|
A:HOH402
|
3.4
|
39.2
|
1.0
|
CG
|
A:MET54
|
3.5
|
31.7
|
1.0
|
CA
|
A:MET54
|
3.6
|
26.4
|
1.0
|
C
|
A:MET54
|
3.8
|
23.0
|
1.0
|
NZ
|
A:LYS101
|
4.1
|
23.7
|
1.0
|
OD1
|
A:ASP9
|
4.3
|
25.5
|
1.0
|
N
|
A:LEU53
|
4.4
|
19.2
|
1.0
|
SD
|
A:MET54
|
4.5
|
40.4
|
1.0
|
CB
|
A:ASP52
|
4.5
|
17.5
|
1.0
|
C
|
A:LEU53
|
4.6
|
22.3
|
1.0
|
O
|
A:HOH316
|
4.6
|
41.6
|
1.0
|
OG
|
A:SER79
|
4.8
|
22.9
|
1.0
|
OE1
|
A:GLU10
|
5.0
|
34.3
|
1.0
|
|
Fluorine binding site 3 out
of 3 in 6ebr
Go back to
Fluorine Binding Sites List in 6ebr
Fluorine binding site 3 out
of 3 in the Activation of RR02 Bound to BEF3
Mono view
Stereo pair view
|
A full contact list of Fluorine with other atoms in the F binding
site number 3 of Activation of RR02 Bound to BEF3 within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:F201
b:22.5
occ:1.00
|
F3
|
A:BEF201
|
0.0
|
22.5
|
1.0
|
BE
|
A:BEF201
|
1.5
|
19.5
|
1.0
|
F2
|
A:BEF201
|
2.4
|
21.6
|
1.0
|
F1
|
A:BEF201
|
2.5
|
20.3
|
1.0
|
OD1
|
A:ASP52
|
2.5
|
25.1
|
1.0
|
OG
|
A:SER79
|
2.7
|
22.9
|
1.0
|
N
|
A:MET54
|
2.8
|
21.9
|
1.0
|
N
|
A:LEU53
|
2.9
|
19.2
|
1.0
|
CB
|
A:SER79
|
3.3
|
21.3
|
1.0
|
CA
|
A:LEU53
|
3.4
|
19.8
|
1.0
|
CB
|
A:LEU53
|
3.4
|
21.4
|
1.0
|
CG
|
A:MET54
|
3.4
|
31.7
|
1.0
|
CG
|
A:ASP52
|
3.4
|
26.5
|
1.0
|
C
|
A:LEU53
|
3.5
|
22.3
|
1.0
|
CB
|
A:MET54
|
3.8
|
27.6
|
1.0
|
CA
|
A:SER79
|
3.8
|
21.0
|
1.0
|
CA
|
A:MET54
|
3.8
|
26.4
|
1.0
|
C
|
A:ASP52
|
4.0
|
20.8
|
1.0
|
OD2
|
A:ASP52
|
4.0
|
19.5
|
1.0
|
N
|
A:ALA80
|
4.1
|
23.6
|
1.0
|
MN
|
A:MN202
|
4.3
|
21.3
|
1.0
|
CG
|
A:LEU53
|
4.3
|
24.3
|
1.0
|
CA
|
A:ASP52
|
4.3
|
17.0
|
1.0
|
CB
|
A:ASP52
|
4.5
|
17.5
|
1.0
|
O
|
A:MET54
|
4.5
|
25.1
|
1.0
|
C
|
A:SER79
|
4.5
|
26.9
|
1.0
|
CG
|
A:LYS81
|
4.5
|
32.1
|
1.0
|
C
|
A:MET54
|
4.6
|
23.0
|
1.0
|
O
|
A:LEU78
|
4.6
|
16.7
|
1.0
|
O
|
A:LEU53
|
4.7
|
22.3
|
1.0
|
SD
|
A:MET54
|
4.8
|
40.4
|
1.0
|
O
|
A:HOH402
|
4.8
|
39.2
|
1.0
|
NZ
|
A:LYS101
|
4.9
|
23.7
|
1.0
|
N
|
A:LYS81
|
4.9
|
25.6
|
1.0
|
CD1
|
A:LEU53
|
4.9
|
27.6
|
1.0
|
N
|
A:SER79
|
5.0
|
17.4
|
1.0
|
|
Reference:
A.Riboldi-Tunnicliffe,
A.Riboldi-Tunnicliffe,
S.Panjikar.
N/A N/A.
Page generated: Thu Aug 1 19:29:00 2024
|