Fluorine in PDB 4qxi: Crystal Structure of Human Ar Complexed with Nadp+ and AK198

All present enzymatic activity of Crystal Structure of Human Ar Complexed with Nadp+ and AK198:
1.1.1.21;

The structure of Crystal Structure of Human Ar Complexed with Nadp+ and AK198, PDB code: 4qxi was solved by A.Cousido-Siah, A.Mitschler, F.X.Ruiz, J.Fanfrlik, P.Hobza, A.D.Podjarny, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	27.59 / 0.87
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	49.403, 66.542, 47.311, 90.00, 92.34, 90.00
R / Rfree (%)	13.4 / 14.5

The structure of Crystal Structure of Human Ar Complexed with Nadp+ and AK198 also contains other interesting chemical elements:

Chlorine

(Cl)

1 atom

The binding sites of Fluorine atom in the Crystal Structure of Human Ar Complexed with Nadp+ and AK198 (pdb code 4qxi). This binding sites where shown within 5.0 Angstroms radius around Fluorine atom.
In total only one binding site of Fluorine was determined in the Crystal Structure of Human Ar Complexed with Nadp+ and AK198, PDB code: 4qxi:

Fluorine binding site 1 out of 1 in the Crystal Structure of Human Ar Complexed with Nadp+ and AK198


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 Human Ar Complexed with Nadp+ and AK198 within 5.0Å range: probe atom residue distance (Å) B Occ A:F402 b:8.7 occ:0.56 F A:I98402 0.0 8.7 0.6 C15 A:I98402 1.3 7.9 0.6 CB A:LEU300 1.5 16.1 0.4 N A:LEU300 1.7 15.0 0.4 CA A:LEU300 1.7 16.2 0.4 C22 A:I98402 2.3 7.2 0.6 C11 A:I98402 2.4 8.6 0.6 C A:ALA299 2.6 13.7 0.4 C19 A:I98402 2.7 7.2 0.6 CG A:LEU300 2.8 15.3 0.4 CD1 A:LEU300 3.0 15.4 0.4 CH2 A:TRP111 3.2 8.2 1.0 C A:LEU300 3.2 17.6 0.4 N A:LEU300 3.2 10.2 0.6 C A:ALA299 3.2 10.8 0.6 CA A:ALA299 3.3 10.6 0.6 O A:ALA299 3.3 13.1 0.4 CA A:ALA299 3.5 12.3 0.4 CB A:LEU300 3.6 10.2 0.6 CZ3 A:TRP111 3.6 7.5 1.0 N A:ALA299 3.6 9.8 0.6 C13 A:I98402 3.6 7.5 0.6 N A:ALA299 3.6 10.8 0.4 C18 A:I98402 3.6 8.9 0.6 CZ2 A:TRP111 3.7 8.1 1.0 CD2 A:LEU300 3.7 14.9 0.4 O A:LEU300 3.8 17.9 0.4 O A:ALA299 3.9 11.6 0.6 C A:CYS298 3.9 8.6 0.6 C A:CYS298 4.0 9.6 0.4 CA A:LEU300 4.0 9.8 0.6 O A:CYS298 4.1 9.0 0.6 N A:LEU301 4.1 19.2 0.4 C17 A:I98402 4.1 8.3 0.6 N21 A:I98402 4.2 6.6 0.6 O A:CYS298 4.2 9.0 0.4 OH A:TYR309 4.2 10.8 0.5 CE1 A:TYR309 4.3 10.2 0.5 CE3 A:TRP111 4.4 6.6 1.0 CE2 A:TRP111 4.4 7.1 1.0 CE2 A:PHE311 4.6 11.2 1.0 CB A:ALA299 4.7 11.1 0.6 CZ A:TYR309 4.7 10.4 0.5 N2 A:I98402 4.7 9.8 0.6 CA A:CYS298 4.7 8.9 0.4 CA A:CYS298 4.7 8.6 0.6 CD2 A:TRP111 4.8 6.3 1.0 CB A:CYS298 4.8 10.3 0.6 CB A:CYS298 4.9 9.2 0.4 CB A:ALA299 4.9 12.2 0.4 CG A:LEU300 5.0 10.6 0.6

J.Fanfrlik, F.X.Ruiz, A.Kadlcikova, J.Rezac, A.Cousido-Siah, A.Mitschler, S.Haldar, M.Lepsik, M.H.Kolar, P.Majer, A.D.Podjarny, P.Hobza. The Effect of Halogen-to-Hydrogen Bond Substitution on Human Aldose Reductase Inhibition Acs Chem.Biol. 2015.
ISSN: ESSN 1554-8937
PubMed: 25919404
DOI: 10.1021/ACSCHEMBIO.5B00151