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Fluorine in PDB 4rlo: Human P70S6K1 with Ruthenium-Based Inhibitor EM5

Enzymatic activity of Human P70S6K1 with Ruthenium-Based Inhibitor EM5

All present enzymatic activity of Human P70S6K1 with Ruthenium-Based Inhibitor EM5:
2.7.11.1;

Protein crystallography data

The structure of Human P70S6K1 with Ruthenium-Based Inhibitor EM5, PDB code: 4rlo was solved by J.F.Domsic, J.Barber-Rotenberg, J.Salami, J.Qin, R.Marmorstein, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 49.03 / 2.53
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 78.515, 62.882, 86.718, 90.00, 94.02, 90.00
R / Rfree (%) 19.2 / 22.2

Other elements in 4rlo:

The structure of Human P70S6K1 with Ruthenium-Based Inhibitor EM5 also contains other interesting chemical elements:

Ruthenium (Ru) 1 atom
Chlorine (Cl) 6 atoms

Fluorine Binding Sites:

The binding sites of Fluorine atom in the Human P70S6K1 with Ruthenium-Based Inhibitor EM5 (pdb code 4rlo). This binding sites where shown within 5.0 Angstroms radius around Fluorine atom.
In total only one binding site of Fluorine was determined in the Human P70S6K1 with Ruthenium-Based Inhibitor EM5, PDB code: 4rlo:

Fluorine binding site 1 out of 1 in 4rlo

Go back to Fluorine Binding Sites List in 4rlo
Fluorine binding site 1 out of 1 in the Human P70S6K1 with Ruthenium-Based Inhibitor EM5


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 1 of Human P70S6K1 with Ruthenium-Based Inhibitor EM5 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:F401

b:53.8
occ:1.00
F4 A:3T3401 0.0 53.8 1.0
C35 A:3T3401 1.3 47.2 1.0
C34 A:3T3401 2.4 39.0 1.0
C36 A:3T3401 2.4 44.1 1.0
HA A:ASP236 2.8 71.7 1.0
HD2 A:LYS123 3.0 68.8 1.0
HZ2 A:LYS123 3.1 77.5 1.0
HB2 A:ASP236 3.6 73.8 1.0
C33 A:3T3401 3.6 39.9 1.0
N20 A:3T3401 3.6 41.3 1.0
CA A:ASP236 3.7 59.8 1.0
CG A:ASP236 3.8 64.7 1.0
HG21 A:VAL105 3.8 55.6 1.0
OE2 A:GLU143 3.8 58.7 1.0
CB A:ASP236 3.8 61.5 1.0
OD1 A:ASP236 3.9 66.5 1.0
CD A:LYS123 3.9 57.3 1.0
NZ A:LYS123 4.0 64.6 1.0
O A:THR235 4.0 68.0 1.0
C37 A:3T3401 4.0 38.1 1.0
HE3 A:LYS123 4.2 72.5 1.0
H A:PHE237 4.2 82.4 1.0
OD2 A:ASP236 4.3 61.7 1.0
N A:ASP236 4.3 57.8 1.0
CE A:LYS123 4.3 60.4 1.0
HZ3 A:LYS123 4.3 77.5 1.0
C A:THR235 4.4 58.3 1.0
HD3 A:LYS123 4.4 68.8 1.0
HZ1 A:LYS123 4.5 77.5 1.0
HG22 A:VAL105 4.5 55.6 1.0
CG2 A:VAL105 4.6 46.3 1.0
HD13 A:LEU172 4.6 50.4 1.0
HG21 A:THR235 4.7 61.9 1.0
HB2 A:LYS123 4.7 55.5 1.0
CD A:GLU143 4.7 65.7 1.0
OE1 A:GLU143 4.7 67.0 1.0
C A:ASP236 4.8 65.3 1.0
N A:PHE237 4.8 68.7 1.0
OG1 A:THR235 4.8 56.9 1.0
C32 A:3T3401 4.8 38.3 1.0
HB3 A:ASP236 4.8 73.8 1.0
H A:ASP236 4.8 69.4 1.0
HG3 A:LYS123 4.8 61.2 1.0
HG23 A:VAL105 4.8 55.6 1.0
CG A:LYS123 4.9 51.0 1.0
HD11 A:LEU172 5.0 50.4 1.0

Reference:

J.Qin, R.Rajaratnam, L.Feng, J.Salami, J.S.Barber-Rotenberg, J.Domsic, P.Reyes-Uribe, H.Liu, W.Dang, S.L.Berger, J.Villanueva, E.Meggers, R.Marmorstein. Development of Organometallic S6K1 Inhibitors. J.Med.Chem. V. 58 305 2015.
ISSN: ISSN 0022-2623
PubMed: 25356520
DOI: 10.1021/JM5011868
Page generated: Sun Dec 13 12:12:07 2020

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