Fluorine in PDB 7t08: Cryptococcus Neoformans Protein Farnesyltransferase in Complex with Fpp and Inhibitor 2Q
Enzymatic activity of Cryptococcus Neoformans Protein Farnesyltransferase in Complex with Fpp and Inhibitor 2Q
All present enzymatic activity of Cryptococcus Neoformans Protein Farnesyltransferase in Complex with Fpp and Inhibitor 2Q:
2.5.1.58;
Protein crystallography data
The structure of Cryptococcus Neoformans Protein Farnesyltransferase in Complex with Fpp and Inhibitor 2Q, PDB code: 7t08
was solved by
Y.Wang,
Y.Shi,
L.S.Beese,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
50.17 /
1.80
|
Space group
|
P 43 21 2
|
Cell size a, b, c (Å), α, β, γ (°)
|
141.915,
141.915,
130.226,
90,
90,
90
|
R / Rfree (%)
|
17.5 /
19.4
|
Other elements in 7t08:
The structure of Cryptococcus Neoformans Protein Farnesyltransferase in Complex with Fpp and Inhibitor 2Q also contains other interesting chemical elements:
Fluorine Binding Sites:
The binding sites of Fluorine atom in the Cryptococcus Neoformans Protein Farnesyltransferase in Complex with Fpp and Inhibitor 2Q
(pdb code 7t08). This binding sites where shown within
5.0 Angstroms radius around Fluorine atom.
In total 4 binding sites of Fluorine where determined in the
Cryptococcus Neoformans Protein Farnesyltransferase in Complex with Fpp and Inhibitor 2Q, PDB code: 7t08:
Jump to Fluorine binding site number:
1;
2;
3;
4;
Fluorine binding site 1 out
of 4 in 7t08
Go back to
Fluorine Binding Sites List in 7t08
Fluorine binding site 1 out
of 4 in the Cryptococcus Neoformans Protein Farnesyltransferase in Complex with Fpp and Inhibitor 2Q
Mono view
Stereo pair view
|
A full contact list of Fluorine with other atoms in the F binding
site number 1 of Cryptococcus Neoformans Protein Farnesyltransferase in Complex with Fpp and Inhibitor 2Q within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:F628
b:30.7
occ:1.00
|
F15
|
B:XO1628
|
0.0
|
30.7
|
1.0
|
C14
|
B:XO1628
|
1.4
|
31.2
|
1.0
|
F17
|
B:XO1628
|
2.2
|
34.7
|
1.0
|
F16
|
B:XO1628
|
2.2
|
29.2
|
1.0
|
O13
|
B:XO1628
|
2.3
|
28.2
|
1.0
|
C12
|
B:XO1628
|
2.8
|
26.6
|
1.0
|
C18
|
B:XO1628
|
2.9
|
28.5
|
1.0
|
O
|
B:HOH941
|
3.1
|
29.4
|
1.0
|
CE1
|
B:TYR409
|
3.3
|
26.5
|
1.0
|
CD1
|
B:TYR409
|
3.3
|
25.1
|
1.0
|
CZ2
|
B:TRP94
|
3.4
|
25.2
|
1.0
|
NE1
|
B:TRP94
|
3.8
|
22.3
|
1.0
|
F37
|
B:XO1628
|
3.9
|
27.1
|
1.0
|
C11
|
B:XO1628
|
3.9
|
26.7
|
1.0
|
CE2
|
B:TRP94
|
4.0
|
23.9
|
1.0
|
C08
|
B:XO1628
|
4.1
|
26.8
|
1.0
|
CZ2
|
B:TRP329
|
4.1
|
25.8
|
1.0
|
CE3
|
B:TRP90
|
4.2
|
25.0
|
1.0
|
CZ3
|
B:TRP90
|
4.3
|
25.1
|
1.0
|
CH2
|
B:TRP94
|
4.6
|
27.7
|
1.0
|
CZ
|
B:TYR409
|
4.6
|
25.3
|
1.0
|
CH2
|
B:TRP329
|
4.6
|
25.3
|
1.0
|
CD2
|
B:TRP90
|
4.7
|
24.4
|
1.0
|
CG
|
B:TYR409
|
4.7
|
25.5
|
1.0
|
CH2
|
B:TRP90
|
4.7
|
25.6
|
1.0
|
C06
|
B:XO1628
|
4.7
|
24.2
|
1.0
|
ND2
|
B:ASN413
|
4.8
|
28.7
|
1.0
|
N07
|
B:XO1628
|
4.9
|
25.2
|
1.0
|
C10
|
B:XO1628
|
4.9
|
29.1
|
1.0
|
C15
|
B:FPP629
|
5.0
|
25.9
|
1.0
|
C09
|
B:XO1628
|
5.0
|
31.2
|
1.0
|
|
Fluorine binding site 2 out
of 4 in 7t08
Go back to
Fluorine Binding Sites List in 7t08
Fluorine binding site 2 out
of 4 in the Cryptococcus Neoformans Protein Farnesyltransferase in Complex with Fpp and Inhibitor 2Q
Mono view
Stereo pair view
|
A full contact list of Fluorine with other atoms in the F binding
site number 2 of Cryptococcus Neoformans Protein Farnesyltransferase in Complex with Fpp and Inhibitor 2Q within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:F628
b:29.2
occ:1.00
|
F16
|
B:XO1628
|
0.0
|
29.2
|
1.0
|
C14
|
B:XO1628
|
1.4
|
31.2
|
1.0
|
F17
|
B:XO1628
|
2.2
|
34.7
|
1.0
|
F15
|
B:XO1628
|
2.2
|
30.7
|
1.0
|
O13
|
B:XO1628
|
2.2
|
28.2
|
1.0
|
CH2
|
B:TRP90
|
3.0
|
25.6
|
1.0
|
CZ3
|
B:TRP90
|
3.1
|
25.1
|
1.0
|
C15
|
B:FPP629
|
3.3
|
25.9
|
1.0
|
O
|
B:HOH941
|
3.4
|
29.4
|
1.0
|
C13
|
B:FPP629
|
3.5
|
24.3
|
1.0
|
C12
|
B:XO1628
|
3.6
|
26.6
|
1.0
|
CZ2
|
B:TRP90
|
3.6
|
26.0
|
1.0
|
CE3
|
B:TRP90
|
3.7
|
25.0
|
1.0
|
C14
|
B:FPP629
|
3.8
|
28.3
|
1.0
|
CH2
|
B:TRP329
|
3.8
|
25.3
|
1.0
|
CZ2
|
B:TRP329
|
4.0
|
25.8
|
1.0
|
CE2
|
B:TRP90
|
4.1
|
26.2
|
1.0
|
C12
|
B:FPP629
|
4.1
|
23.4
|
1.0
|
CD2
|
B:TRP90
|
4.2
|
24.4
|
1.0
|
C18
|
B:XO1628
|
4.2
|
28.5
|
1.0
|
C11
|
B:XO1628
|
4.6
|
26.7
|
1.0
|
C11
|
B:FPP629
|
4.7
|
28.7
|
1.0
|
F37
|
B:XO1628
|
4.8
|
27.1
|
1.0
|
NE1
|
B:TRP94
|
4.9
|
22.3
|
1.0
|
C9
|
B:FPP629
|
5.0
|
27.8
|
1.0
|
|
Fluorine binding site 3 out
of 4 in 7t08
Go back to
Fluorine Binding Sites List in 7t08
Fluorine binding site 3 out
of 4 in the Cryptococcus Neoformans Protein Farnesyltransferase in Complex with Fpp and Inhibitor 2Q
Mono view
Stereo pair view
|
A full contact list of Fluorine with other atoms in the F binding
site number 3 of Cryptococcus Neoformans Protein Farnesyltransferase in Complex with Fpp and Inhibitor 2Q within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:F628
b:34.7
occ:1.00
|
F17
|
B:XO1628
|
0.0
|
34.7
|
1.0
|
C14
|
B:XO1628
|
1.4
|
31.2
|
1.0
|
F15
|
B:XO1628
|
2.2
|
30.7
|
1.0
|
F16
|
B:XO1628
|
2.2
|
29.2
|
1.0
|
O13
|
B:XO1628
|
2.3
|
28.2
|
1.0
|
F37
|
B:XO1628
|
2.7
|
27.1
|
1.0
|
C18
|
B:XO1628
|
3.0
|
28.5
|
1.0
|
C12
|
B:XO1628
|
3.0
|
26.6
|
1.0
|
C15
|
B:FPP629
|
3.3
|
25.9
|
1.0
|
N35
|
B:XO1628
|
3.6
|
27.9
|
1.0
|
C11
|
B:FPP629
|
3.6
|
28.7
|
1.0
|
C9
|
B:FPP629
|
3.6
|
27.8
|
1.0
|
C13
|
B:FPP629
|
3.7
|
24.3
|
1.0
|
C34
|
B:XO1628
|
3.7
|
23.9
|
1.0
|
C12
|
B:FPP629
|
3.8
|
23.4
|
1.0
|
CZ2
|
B:TRP329
|
3.9
|
25.8
|
1.0
|
C36
|
B:XO1628
|
3.9
|
26.1
|
1.0
|
CH2
|
B:TRP329
|
4.2
|
25.3
|
1.0
|
CE1
|
B:TYR409
|
4.3
|
26.5
|
1.0
|
C08
|
B:XO1628
|
4.3
|
26.8
|
1.0
|
C11
|
B:XO1628
|
4.4
|
26.7
|
1.0
|
C33
|
B:XO1628
|
4.4
|
26.0
|
1.0
|
C8
|
B:FPP629
|
4.4
|
26.4
|
1.0
|
O
|
B:HOH941
|
4.6
|
29.4
|
1.0
|
C14
|
B:FPP629
|
4.7
|
28.3
|
1.0
|
CE2
|
B:TRP329
|
4.9
|
24.7
|
1.0
|
CD1
|
B:TYR409
|
4.9
|
25.1
|
1.0
|
N07
|
B:XO1628
|
5.0
|
25.2
|
1.0
|
|
Fluorine binding site 4 out
of 4 in 7t08
Go back to
Fluorine Binding Sites List in 7t08
Fluorine binding site 4 out
of 4 in the Cryptococcus Neoformans Protein Farnesyltransferase in Complex with Fpp and Inhibitor 2Q
Mono view
Stereo pair view
|
A full contact list of Fluorine with other atoms in the F binding
site number 4 of Cryptococcus Neoformans Protein Farnesyltransferase in Complex with Fpp and Inhibitor 2Q within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:F628
b:27.1
occ:1.00
|
F37
|
B:XO1628
|
0.0
|
27.1
|
1.0
|
C36
|
B:XO1628
|
1.4
|
26.1
|
1.0
|
C38
|
B:XO1628
|
2.4
|
24.8
|
1.0
|
C33
|
B:XO1628
|
2.4
|
26.0
|
1.0
|
F17
|
B:XO1628
|
2.7
|
34.7
|
1.0
|
C34
|
B:XO1628
|
2.8
|
23.9
|
1.0
|
C8
|
B:FPP629
|
3.2
|
26.4
|
1.0
|
C10
|
B:FPP629
|
3.3
|
27.9
|
1.0
|
C18
|
B:XO1628
|
3.4
|
28.5
|
1.0
|
C9
|
B:FPP629
|
3.5
|
27.8
|
1.0
|
N35
|
B:XO1628
|
3.5
|
27.9
|
1.0
|
OH
|
B:TYR409
|
3.6
|
23.5
|
1.0
|
C30
|
B:XO1628
|
3.6
|
26.8
|
1.0
|
C32
|
B:XO1628
|
3.6
|
26.1
|
1.0
|
CE1
|
B:TYR409
|
3.8
|
26.5
|
1.0
|
C7
|
B:FPP629
|
3.8
|
25.1
|
1.0
|
C06
|
B:XO1628
|
3.8
|
24.2
|
1.0
|
C14
|
B:XO1628
|
3.8
|
31.2
|
1.0
|
F15
|
B:XO1628
|
3.9
|
30.7
|
1.0
|
N07
|
B:XO1628
|
3.9
|
25.2
|
1.0
|
CZ
|
B:TYR409
|
4.0
|
25.3
|
1.0
|
C11
|
B:FPP629
|
4.1
|
28.7
|
1.0
|
C31
|
B:XO1628
|
4.1
|
29.5
|
1.0
|
C08
|
B:XO1628
|
4.2
|
26.8
|
1.0
|
C12
|
B:XO1628
|
4.4
|
26.6
|
1.0
|
C6
|
B:FPP629
|
4.4
|
22.4
|
1.0
|
O13
|
B:XO1628
|
4.5
|
28.2
|
1.0
|
C19
|
B:XO1628
|
4.6
|
28.7
|
1.0
|
N22
|
B:XO1628
|
4.7
|
27.7
|
1.0
|
CZ2
|
B:TRP329
|
4.7
|
25.8
|
1.0
|
C05
|
B:XO1628
|
4.7
|
25.1
|
1.0
|
CD1
|
B:TYR409
|
4.8
|
25.1
|
1.0
|
NE1
|
B:TRP329
|
4.8
|
22.3
|
1.0
|
F16
|
B:XO1628
|
4.8
|
29.2
|
1.0
|
C29
|
B:XO1628
|
4.9
|
25.0
|
1.0
|
CE2
|
B:TRP329
|
4.9
|
24.7
|
1.0
|
|
Reference:
Y.Wang,
F.Xu,
C.B.Nichols,
Y.Shi,
H.W.Hellinga,
J.A.Alspaugh,
M.D.Distefano,
L.S.Beese.
Structure-Guided Discovery of Potent Antifungals That Prevent Ras Signaling By Inhibiting Protein Farnesyltransferase. J.Med.Chem. V. 65 13753 2022.
ISSN: ISSN 0022-2623
PubMed: 36218371
DOI: 10.1021/ACS.JMEDCHEM.2C00902
Page generated: Fri Aug 2 13:10:59 2024
|