Atomistry » Fluorine » PDB 8jvj-8ou5 » 8oqq
Atomistry »
  Fluorine »
    PDB 8jvj-8ou5 »
      8oqq »

Fluorine in PDB 8oqq: Structure of Mycobacterium Tuberculosis Beta-Oxidation Trifunctional Enzyme in Complex with Fragment-M-79

Enzymatic activity of Structure of Mycobacterium Tuberculosis Beta-Oxidation Trifunctional Enzyme in Complex with Fragment-M-79

All present enzymatic activity of Structure of Mycobacterium Tuberculosis Beta-Oxidation Trifunctional Enzyme in Complex with Fragment-M-79:
1.1.1.35;

Protein crystallography data

The structure of Structure of Mycobacterium Tuberculosis Beta-Oxidation Trifunctional Enzyme in Complex with Fragment-M-79, PDB code: 8oqq was solved by S.Dalwani, R.K.Wierenga, R.Venkatesan, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 50.27 / 2.59
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 250.339, 134.016, 119.745, 90, 110.53, 90
R / Rfree (%) 19.1 / 23

Fluorine Binding Sites:

The binding sites of Fluorine atom in the Structure of Mycobacterium Tuberculosis Beta-Oxidation Trifunctional Enzyme in Complex with Fragment-M-79 (pdb code 8oqq). This binding sites where shown within 5.0 Angstroms radius around Fluorine atom.
In total 4 binding sites of Fluorine where determined in the Structure of Mycobacterium Tuberculosis Beta-Oxidation Trifunctional Enzyme in Complex with Fragment-M-79, PDB code: 8oqq:
Jump to Fluorine binding site number: 1; 2; 3; 4;

Fluorine binding site 1 out of 4 in 8oqq

Go back to Fluorine Binding Sites List in 8oqq
Fluorine binding site 1 out of 4 in the Structure of Mycobacterium Tuberculosis Beta-Oxidation Trifunctional Enzyme in Complex with Fragment-M-79


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 1 of Structure of Mycobacterium Tuberculosis Beta-Oxidation Trifunctional Enzyme in Complex with Fragment-M-79 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:F805

b:100.4
occ:1.00
 F A:VWE805 0.0 100.4 1.0
C2 A:VWE805 1.4 94.4 1.0
C1 A:VWE805 2.3 84.9 1.0
C3 A:VWE805 2.4 90.8 1.0
O4 A:VWE805 2.5 102.1 1.0
C6 A:VWE805 2.9 98.6 1.0
C A:VWE805 3.6 86.1 1.0
C4 A:VWE805 3.6 86.6 1.0
NH2 A:ARG175 3.7 60.7 1.0
O A:HOH924 4.0 60.5 1.0
O3 A:VWE805 4.1 108.0 1.0
C5 A:VWE805 4.1 80.8 1.0
O A:PHE303 4.1 57.4 1.0
CD2 A:LEU144 4.7 53.5 1.0
CG A:LEU144 4.9 48.0 1.0
CD1 A:LEU144 4.9 62.8 1.0
CD1 A:PHE304 5.0 73.5 1.0
CZ A:ARG175 5.0 66.0 1.0

Fluorine binding site 2 out of 4 in 8oqq

Go back to Fluorine Binding Sites List in 8oqq
Fluorine binding site 2 out of 4 in the Structure of Mycobacterium Tuberculosis Beta-Oxidation Trifunctional Enzyme in Complex with Fragment-M-79


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 2 of Structure of Mycobacterium Tuberculosis Beta-Oxidation Trifunctional Enzyme in Complex with Fragment-M-79 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:F806

b:89.7
occ:1.00
 F A:VWE806 0.0 89.7 1.0
C2 A:VWE806 1.4 89.5 1.0
C1 A:VWE806 2.3 84.6 1.0
C3 A:VWE806 2.4 87.7 1.0
O3 A:VWE806 2.8 92.1 1.0
C6 A:VWE806 2.9 86.5 1.0
O A:LEU599 3.4 75.0 1.0
C A:VWE806 3.6 93.9 1.0
C4 A:VWE806 3.6 91.8 1.0
O4 A:VWE806 4.0 73.4 1.0
CA A:LYS600 4.0 63.7 1.0
C5 A:VWE806 4.1 105.0 1.0
C A:LEU599 4.3 76.8 1.0
O A:LYS600 4.4 82.9 1.0
N A:LYS600 4.6 73.1 1.0
C A:LYS600 4.6 66.9 1.0
CB A:LYS600 5.0 67.3 1.0

Fluorine binding site 3 out of 4 in 8oqq

Go back to Fluorine Binding Sites List in 8oqq
Fluorine binding site 3 out of 4 in the Structure of Mycobacterium Tuberculosis Beta-Oxidation Trifunctional Enzyme in Complex with Fragment-M-79


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 3 of Structure of Mycobacterium Tuberculosis Beta-Oxidation Trifunctional Enzyme in Complex with Fragment-M-79 within 5.0Å range:
probe atom residue distance (Å) B Occ
B:F808

b:97.4
occ:1.00
 F B:VWE808 0.0 97.4 1.0
C2 B:VWE808 1.4 90.5 1.0
C1 B:VWE808 2.3 75.7 1.0
C3 B:VWE808 2.4 96.0 1.0
O3 B:VWE808 2.7 91.9 1.0
C6 B:VWE808 2.9 96.7 1.0
C B:VWE808 3.6 95.4 1.0
C4 B:VWE808 3.6 104.5 1.0
O B:PHE303 3.8 50.2 1.0
NH2 B:ARG175 4.0 64.6 1.0
O4 B:VWE808 4.1 100.0 1.0
C5 B:VWE808 4.1 108.3 1.0
CD2 B:LEU144 4.5 41.0 1.0
C B:PHE303 4.9 34.3 1.0
CG B:LEU144 4.9 55.3 1.0
CD1 B:PHE304 5.0 57.2 1.0
CD1 B:LEU144 5.0 43.2 1.0

Fluorine binding site 4 out of 4 in 8oqq

Go back to Fluorine Binding Sites List in 8oqq
Fluorine binding site 4 out of 4 in the Structure of Mycobacterium Tuberculosis Beta-Oxidation Trifunctional Enzyme in Complex with Fragment-M-79


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 4 of Structure of Mycobacterium Tuberculosis Beta-Oxidation Trifunctional Enzyme in Complex with Fragment-M-79 within 5.0Å range:
probe atom residue distance (Å) B Occ
B:F809

b:109.6
occ:1.00
 F B:VWE809 0.0 109.6 1.0
C2 B:VWE809 1.4 105.3 1.0
C1 B:VWE809 2.3 93.1 1.0
C3 B:VWE809 2.4 96.9 1.0
O3 B:VWE809 2.7 87.8 1.0
C6 B:VWE809 2.9 87.2 1.0
C B:VWE809 3.6 90.9 1.0
C4 B:VWE809 3.6 97.6 1.0
O B:LEU599 3.9 68.1 1.0
O4 B:VWE809 4.1 84.8 1.0
C5 B:VWE809 4.1 102.4 1.0
CA B:LYS600 4.3 69.7 1.0
O B:LYS600 4.3 79.2 1.0
C B:LYS600 4.7 67.2 1.0
C B:LEU599 4.7 73.7 1.0
N B:LYS600 4.9 74.8 1.0

Reference:

S.Dalwani, A.Metz, F.U.Huschmann, M.S.Weiss, R.K.Wierenga, R.Venkatesan. Crystallographic Fragment Binding Studies of the Mycobacterium Tuberculosis Trifunctional Enzyme Suggest Binding Pockets For the Tails of the Acyl-Coa Substrates at Its Active Sites and A Potential Substrate Channeling Path Between Them Biorxiv 2024.
ISSN: ISSN 2692-8205
DOI: 10.1101/2024.01.11.575214
Page generated: Fri Aug 2 21:12:23 2024

Last articles

Mg in 4Y52
Mg in 4Y30
Mg in 4Y2V
Mg in 4Y2X
Mg in 4Y2Y
Mg in 4Y2U
Mg in 4Y2T
Mg in 4Y2Q
Mg in 4Y2R
Mg in 4Y2S
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy