Atomistry » Fluorine » PDB 5o6j-5olv » 5oep
Atomistry »
  Fluorine »
    PDB 5o6j-5olv »
      5oep »

Fluorine in PDB 5oep: Mycobacterium Tuberculosis DPRE1 in Complex with Inhibitor TCA481

Enzymatic activity of Mycobacterium Tuberculosis DPRE1 in Complex with Inhibitor TCA481

All present enzymatic activity of Mycobacterium Tuberculosis DPRE1 in Complex with Inhibitor TCA481:
1.1.98.3;

Protein crystallography data

The structure of Mycobacterium Tuberculosis DPRE1 in Complex with Inhibitor TCA481, PDB code: 5oep was solved by K.Futterer, S.M.Batt, G.S.Besra, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 57.60 / 2.35
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 78.300, 84.540, 80.970, 90.00, 103.52, 90.00
R / Rfree (%) 19.6 / 23.3

Fluorine Binding Sites:

The binding sites of Fluorine atom in the Mycobacterium Tuberculosis DPRE1 in Complex with Inhibitor TCA481 (pdb code 5oep). This binding sites where shown within 5.0 Angstroms radius around Fluorine atom.
In total 2 binding sites of Fluorine where determined in the Mycobacterium Tuberculosis DPRE1 in Complex with Inhibitor TCA481, PDB code: 5oep:
Jump to Fluorine binding site number: 1; 2;

Fluorine binding site 1 out of 2 in 5oep

Go back to Fluorine Binding Sites List in 5oep
Fluorine binding site 1 out of 2 in the Mycobacterium Tuberculosis DPRE1 in Complex with Inhibitor TCA481


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 1 of Mycobacterium Tuberculosis DPRE1 in Complex with Inhibitor TCA481 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:F502

b:80.5
occ:1.00
F16 A:9T2502 0.0 80.5 1.0
C16 A:9T2502 1.4 73.6 1.0
C17 A:9T2502 2.4 70.2 1.0
S15 A:9T2502 2.7 74.5 1.0
CD A:LYS367 3.3 49.4 1.0
CG A:LYS367 3.3 48.1 1.0
CD2 A:HIS132 3.4 36.4 1.0
ND2 A:ASN385 3.4 42.9 1.0
CB A:LYS367 3.5 47.7 1.0
CE1 A:PHE369 3.5 39.3 1.0
C18 A:9T2502 3.6 71.2 1.0
C14 A:9T2502 3.8 72.6 1.0
NE2 A:HIS132 3.8 36.2 1.0
O A:GLY133 3.9 35.9 1.0
CZ A:PHE369 4.2 39.4 1.0
C A:GLY133 4.3 36.1 1.0
CG A:ASN385 4.4 41.2 1.0
CD1 A:PHE369 4.4 39.8 1.0
CE A:LYS367 4.6 50.5 1.0
CG A:HIS132 4.6 36.1 1.0
CA A:GLY133 4.8 35.0 1.0
CA A:LYS367 4.9 45.8 1.0
N A:LYS134 5.0 37.2 1.0
CB A:ASN385 5.0 39.9 1.0

Fluorine binding site 2 out of 2 in 5oep

Go back to Fluorine Binding Sites List in 5oep
Fluorine binding site 2 out of 2 in the Mycobacterium Tuberculosis DPRE1 in Complex with Inhibitor TCA481


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 2 of Mycobacterium Tuberculosis DPRE1 in Complex with Inhibitor TCA481 within 5.0Å range:
probe atom residue distance (Å) B Occ
B:F502

b:76.1
occ:1.00
F16 B:9T2502 0.0 76.1 1.0
C16 B:9T2502 1.4 77.3 1.0
C17 B:9T2502 2.4 76.8 1.0
S15 B:9T2502 2.8 76.7 1.0
CD2 B:HIS132 3.2 39.6 1.0
ND2 B:ASN385 3.3 49.8 1.0
CG B:LYS367 3.5 49.9 1.0
CE1 B:PHE369 3.5 39.9 1.0
NE2 B:HIS132 3.5 40.6 1.0
CD B:LYS367 3.6 52.2 1.0
C18 B:9T2502 3.6 79.2 1.0
CB B:LYS367 3.6 47.8 1.0
C14 B:9T2502 3.9 79.2 1.0
O B:GLY133 4.0 40.5 1.0
CZ B:PHE369 4.1 38.6 1.0
CG B:ASN385 4.2 51.0 1.0
C B:GLY133 4.5 41.5 1.0
CG B:HIS132 4.5 39.0 1.0
CD1 B:PHE369 4.5 39.8 1.0
NE2 B:GLN336 4.7 46.2 1.0
CE B:LYS367 4.8 50.8 1.0
CE1 B:HIS132 4.8 41.4 1.0
CB B:ASN385 4.9 50.0 1.0
OD1 B:ASN385 4.9 50.7 1.0
CA B:GLY133 4.9 42.6 1.0
C19 B:9T2502 5.0 83.3 1.0

Reference:

R.Liu, X.Lyu, S.M.Batt, M.H.Hsu, M.B.Harbut, C.Vilcheze, B.Cheng, K.Ajayi, B.Yang, Y.Yang, H.Guo, C.Lin, F.Gan, C.Wang, S.G.Franzblau, W.R.Jacobs, G.S.Besra, E.F.Johnson, M.Petrassi, A.K.Chatterjee, K.Futterer, F.Wang. Determinants of the Inhibition of DPRE1 and CYP2C9 By Antitubercular Thiophenes. Angew. Chem. Int. Ed. Engl. V. 56 13011 2017.
ISSN: ESSN 1521-3773
PubMed: 28815830
DOI: 10.1002/ANIE.201707324
Page generated: Sun Dec 13 12:29:43 2020

Last articles

Zn in 8WB0
Zn in 8WAX
Zn in 8WAU
Zn in 8WAZ
Zn in 8WAY
Zn in 8WAV
Zn in 8WAW
Zn in 8WAT
Zn in 8W7M
Zn in 8WD3
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy