Fluorine in PDB 6b21: Crystal Structure of Amtb From E. Coli Bound to Topfluor Cardiolipin

The structure of Crystal Structure of Amtb From E. Coli Bound to Topfluor Cardiolipin, PDB code: 6b21 was solved by C.D.Boone, A.Laganowsky, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	56.22 / 2.45
Space group	H 3 2
Cell size a, b, c (Å), α, β, γ (°)	138.780, 138.780, 159.140, 90.00, 90.00, 120.00
R / Rfree (%)	17 / 21.3

The binding sites of Fluorine atom in the Crystal Structure of Amtb From E. Coli Bound to Topfluor Cardiolipin (pdb code 6b21). This binding sites where shown within 5.0 Angstroms radius around Fluorine atom.
In total 2 binding sites of Fluorine where determined in the Crystal Structure of Amtb From E. Coli Bound to Topfluor Cardiolipin, PDB code: 6b21:
Jump to Fluorine binding site number: 1; 2;

Fluorine binding site 1 out of 2 in the Crystal Structure of Amtb From E. Coli Bound to Topfluor Cardiolipin


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 1 of Crystal Structure of Amtb From E. Coli Bound to Topfluor Cardiolipin within 5.0Å range: probe atom residue distance (Å) B Occ A:F501 b:0.5 occ:1.00 F96 A:C9V501 0.0 0.5 1.0 B95 A:C9V501 1.7 95.4 1.0 N94 A:C9V501 2.6 84.7 1.0 N98 A:C9V501 2.6 0.8 1.0 F97 A:C9V501 2.7 0.6 1.0 C99 A:C9V501 3.2 94.4 1.0 C92 A:C9V501 3.2 62.8 1.0 CA0 A:C9V501 3.3 88.9 1.0 C93 A:C9V501 3.3 62.0 1.0 C88 A:C9V501 3.6 70.2 1.0 CA4 A:C9V501 3.6 0.5 1.0 C87 A:C9V501 4.1 0.7 1.0 O A:HOH677 4.3 76.6 1.0 CA1 A:C9V501 4.4 92.1 1.0 C91 A:C9V501 4.4 61.2 1.0 CA2 A:C9V501 4.6 93.7 1.0 C89 A:C9V501 4.6 67.0 1.0

Fluorine binding site 2 out of 2 in the Crystal Structure of Amtb From E. Coli Bound to Topfluor Cardiolipin


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 2 of Crystal Structure of Amtb From E. Coli Bound to Topfluor Cardiolipin within 5.0Å range: probe atom residue distance (Å) B Occ A:F501 b:0.6 occ:1.00 F97 A:C9V501 0.0 0.6 1.0 B95 A:C9V501 1.7 95.4 1.0 N98 A:C9V501 2.6 0.8 1.0 N94 A:C9V501 2.6 84.7 1.0 F96 A:C9V501 2.7 0.5 1.0 C48 A:C9V501 3.2 82.0 1.0 C99 A:C9V501 3.2 94.4 1.0 C92 A:C9V501 3.2 62.8 1.0 CA0 A:C9V501 3.3 88.9 1.0 C93 A:C9V501 3.3 62.0 1.0 O A:HOH677 3.4 76.6 1.0 CA4 A:C9V501 3.7 0.5 1.0 C88 A:C9V501 3.7 70.2 1.0 C47 A:C9V501 3.8 79.0 1.0 C87 A:C9V501 4.1 0.7 1.0 C45 A:C9V501 4.2 79.9 1.0 CA1 A:C9V501 4.4 92.1 1.0 C49 A:C9V501 4.4 83.2 1.0 C91 A:C9V501 4.4 61.2 1.0 C50 A:C9V501 4.6 88.3 1.0 CA2 A:C9V501 4.6 93.7 1.0 C46 A:C9V501 4.7 82.7 1.0 C89 A:C9V501 4.7 67.0 1.0

J.W.Patrick, C.D.Boone, W.Liu, G.M.Conover, Y.Liu, X.Cong, A.Laganowsky. Allostery Revealed Within Lipid Binding Events to Membrane Proteins. Proc. Natl. Acad. Sci. V. 115 2976 2018U.S.A..
ISSN: ESSN 1091-6490
PubMed: 29507234
DOI: 10.1073/PNAS.1719813115