Fluorine in PDB 4xty: Mycobacterium Tuberculosis Biotin Ligase Complexed with Bisubstrate Inhibitor 63 with Fluorine in Place of 2'Oh

All present enzymatic activity of Mycobacterium Tuberculosis Biotin Ligase Complexed with Bisubstrate Inhibitor 63 with Fluorine in Place of 2'Oh:
6.3.4.15;

The structure of Mycobacterium Tuberculosis Biotin Ligase Complexed with Bisubstrate Inhibitor 63 with Fluorine in Place of 2'Oh, PDB code: 4xty was solved by T.De La Mora-Rey, B.C.Finzel, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	36.14 / 1.80
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	63.408, 68.731, 114.488, 90.00, 90.00, 90.00
R / Rfree (%)	17.7 / 21.2

The binding sites of Fluorine atom in the Mycobacterium Tuberculosis Biotin Ligase Complexed with Bisubstrate Inhibitor 63 with Fluorine in Place of 2'Oh (pdb code 4xty). 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 Biotin Ligase Complexed with Bisubstrate Inhibitor 63 with Fluorine in Place of 2'Oh, PDB code: 4xty:
Jump to Fluorine binding site number: 1; 2;

Fluorine binding site 1 out of 2 in the Mycobacterium Tuberculosis Biotin Ligase Complexed with Bisubstrate Inhibitor 63 with Fluorine in Place of 2'Oh


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 1 of Mycobacterium Tuberculosis Biotin Ligase Complexed with Bisubstrate Inhibitor 63 with Fluorine in Place of 2'Oh within 5.0Å range: probe atom residue distance (Å) B Occ A:F301 b:20.7 occ:1.00 F1 A:44L301 0.0 20.7 1.0 CAM A:44L301 1.4 16.3 1.0 CBG A:44L301 2.3 11.8 1.0 CAL A:44L301 2.3 15.2 1.0 OAL A:44L301 2.6 19.0 1.0 CBE A:44L301 2.8 13.5 1.0 OD1 A:ASP167 2.9 31.7 1.0 O A:HOH519 2.9 28.8 1.0 OAX A:44L301 3.0 15.4 1.0 O A:HOH537 3.2 39.5 1.0 O A:HOH563 3.6 36.1 1.0 N9 A:44L301 3.6 17.1 1.0 CG A:ASP167 3.8 24.8 1.0 C8 A:44L301 4.2 15.1 1.0 CAN A:44L301 4.3 15.5 1.0 OD2 A:ASP167 4.4 28.8 1.0 O A:HOH498 4.6 22.4 1.0 O A:HOH538 4.6 30.4 1.0 C4 A:44L301 4.7 14.1 1.0 O A:HOH470 4.7 21.3 1.0 CB A:ASP167 4.7 23.4 1.0 O A:HOH482 4.9 21.4 1.0

Fluorine binding site 2 out of 2 in the Mycobacterium Tuberculosis Biotin Ligase Complexed with Bisubstrate Inhibitor 63 with Fluorine in Place of 2'Oh


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 2 of Mycobacterium Tuberculosis Biotin Ligase Complexed with Bisubstrate Inhibitor 63 with Fluorine in Place of 2'Oh within 5.0Å range: probe atom residue distance (Å) B Occ B:F301 b:19.8 occ:1.00 F1 B:44L301 0.0 19.8 1.0 CAM B:44L301 1.4 21.2 1.0 CAL B:44L301 2.4 16.3 1.0 CBG B:44L301 2.4 16.5 1.0 OAL B:44L301 2.7 19.7 1.0 CBE B:44L301 2.9 15.1 1.0 OD1 B:ASP167 3.0 33.0 1.0 OAX B:44L301 3.0 16.2 1.0 O B:HOH443 3.2 32.5 1.0 O B:HOH407 3.5 35.6 1.0 N9 B:44L301 3.6 16.2 1.0 CG B:ASP167 4.0 28.6 1.0 C8 B:44L301 4.3 16.3 1.0 CAN B:44L301 4.4 14.7 1.0 CB B:ASP167 4.7 25.5 1.0 O B:HOH423 4.7 16.4 1.0 C4 B:44L301 4.7 16.2 1.0 O B:HOH421 4.8 22.9 1.0 OD2 B:ASP167 4.8 29.9 1.0 O B:HOH518 4.9 20.6 1.0

M.R.Bockman, A.S.Kalinda, R.Petrelli, T.De La Mora-Rey, D.Tiwari, F.Liu, S.Dawadi, M.Nandakumar, K.Y.Rhee, D.Schnappinger, B.C.Finzel, C.C.Aldrich. Targeting Mycobacterium Tuberculosis Biotin Protein Ligase (Mtbpl) with Nucleoside-Based Bisubstrate Adenylation Inhibitors. J.Med.Chem. V. 58 7349 2015.
ISSN: ISSN 0022-2623
PubMed: 26299766
DOI: 10.1021/ACS.JMEDCHEM.5B00719