Fluorine in PDB 4dv8: Anthrax Lethal Factor Metalloproteinase in Complex with the Hydroxamic Acid Based Small Molecule PT8421

All present enzymatic activity of Anthrax Lethal Factor Metalloproteinase in Complex with the Hydroxamic Acid Based Small Molecule PT8421:
3.4.24.83;

The structure of Anthrax Lethal Factor Metalloproteinase in Complex with the Hydroxamic Acid Based Small Molecule PT8421, PDB code: 4dv8 was solved by S.A.Margosiak, B.Sankaran, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	44.18 / 1.63
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	57.090, 74.253, 139.530, 90.00, 90.00, 90.00
R / Rfree (%)	17.9 / 20.4

The structure of Anthrax Lethal Factor Metalloproteinase in Complex with the Hydroxamic Acid Based Small Molecule PT8421 also contains other interesting chemical elements:

Zinc

(Zn)

1 atom

The binding sites of Fluorine atom in the Anthrax Lethal Factor Metalloproteinase in Complex with the Hydroxamic Acid Based Small Molecule PT8421 (pdb code 4dv8). This binding sites where shown within 5.0 Angstroms radius around Fluorine atom.
In total 2 binding sites of Fluorine where determined in the Anthrax Lethal Factor Metalloproteinase in Complex with the Hydroxamic Acid Based Small Molecule PT8421, PDB code: 4dv8:
Jump to Fluorine binding site number: 1; 2;

Fluorine binding site 1 out of 2 in the Anthrax Lethal Factor Metalloproteinase in Complex with the Hydroxamic Acid Based Small Molecule PT8421


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 1 of Anthrax Lethal Factor Metalloproteinase in Complex with the Hydroxamic Acid Based Small Molecule PT8421 within 5.0Å range: probe atom residue distance (Å) B Occ A:F802 b:35.1 occ:1.00 F18 A:0LX802 0.0 35.1 1.0 C15 A:0LX802 1.3 38.1 1.0 C16 A:0LX802 2.4 33.0 1.0 C14 A:0LX802 2.4 31.4 1.0 CG2 A:VAL660 3.4 14.7 1.0 O A:HOH1214 3.4 37.9 1.0 CD2 A:LEU658 3.5 18.5 1.0 C17 A:0LX802 3.6 30.4 1.0 C13 A:0LX802 3.6 29.2 1.0 CG A:GLN642 3.7 18.3 1.0 CG A:GLN646 3.8 30.4 1.0 CD A:GLN646 3.8 34.9 1.0 OE1 A:GLN642 3.9 17.5 1.0 CG A:LEU658 3.9 16.8 1.0 CD A:GLN642 4.1 15.3 1.0 CG1 A:VAL660 4.1 13.6 1.0 OE1 A:GLN646 4.1 40.7 1.0 C12 A:0LX802 4.1 23.9 1.0 CB A:VAL660 4.2 14.5 1.0 NE2 A:GLN646 4.2 27.5 1.0 CD1 A:LEU658 4.5 20.5 1.0 CA A:VAL660 4.5 14.3 1.0 CB A:GLN642 4.5 17.4 1.0 O A:TYR659 4.7 16.1 1.0 CA A:GLN642 4.9 15.1 1.0 O A:HOH1510 4.9 52.8 1.0

Fluorine binding site 2 out of 2 in the Anthrax Lethal Factor Metalloproteinase in Complex with the Hydroxamic Acid Based Small Molecule PT8421


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 2 of Anthrax Lethal Factor Metalloproteinase in Complex with the Hydroxamic Acid Based Small Molecule PT8421 within 5.0Å range: probe atom residue distance (Å) B Occ A:F802 b:31.1 occ:1.00 F29 A:0LX802 0.0 31.1 1.0 C26 A:0LX802 1.3 32.7 1.0 C25 A:0LX802 2.4 25.4 1.0 C27 A:0LX802 2.4 26.5 1.0 CB A:GLU676 3.1 45.1 1.0 N A:GLU676 3.3 33.2 1.0 O A:HOH1412 3.4 40.2 1.0 CA A:GLU676 3.4 37.6 1.0 CG A:LEU677 3.4 29.1 1.0 C A:GLU676 3.4 35.7 1.0 CD2 A:LEU677 3.6 29.0 1.0 C24 A:0LX802 3.6 22.4 1.0 C28 A:0LX802 3.6 19.6 1.0 N A:LEU677 3.7 29.6 1.0 O A:GLU676 3.8 36.2 1.0 C23 A:0LX802 4.1 19.1 1.0 OE1 A:GLU739 4.1 23.5 1.0 CG A:GLU676 4.2 48.1 1.0 CD1 A:LEU677 4.3 28.5 1.0 NH2 A:ARG742 4.4 32.7 1.0 OE1 A:GLU676 4.4 32.2 1.0 CB A:LEU677 4.4 25.1 1.0 CA A:LEU677 4.5 28.9 1.0 C A:VAL675 4.6 34.8 1.0 CD A:GLU676 4.6 45.2 1.0 O A:HOH1494 4.7 39.0 1.0 N A:VAL675 4.7 28.8 1.0 OE2 A:GLU739 4.7 20.1 1.0 CD A:GLU739 4.7 18.8 1.0 CB A:TYR728 4.8 21.0 1.0 C A:GLY674 4.9 29.8 1.0 CZ A:ARG742 4.9 23.2 1.0

G.S.Jiao, S.Kim, M.Moayeri, D.Crown, A.Thai, L.Cregar-Hernandez, L.Mckasson, B.Sankaran, A.Lehrer, T.Wong, L.Johns, S.A.Margosiak, S.H.Leppla, A.T.Johnson. Antidotes to Anthrax Lethal Factor Intoxication. Part 3: Evaluation of Core Structures and Further Modifications to the C2-Side Chain. Bioorg.Med.Chem.Lett. V. 22 2242 2012.
ISSN: ISSN 0960-894X
PubMed: 22342144
DOI: 10.1016/J.BMCL.2012.01.095