Fluorine in PDB 1ef3: Fidarestat Bound to Human Aldose Reductase

All present enzymatic activity of Fidarestat Bound to Human Aldose Reductase:
1.1.1.21;

The structure of Fidarestat Bound to Human Aldose Reductase, PDB code: 1ef3 was solved by M.Oka, Y.Matsumoto, S.Sugiyama, N.Tsuruta, M.Matsushima, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	8.00 / 2.80
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	96.140, 62.560, 118.990, 90.00, 101.60, 90.00
R / Rfree (%)	18.6 / 27.8

The binding sites of Fluorine atom in the Fidarestat Bound to Human Aldose Reductase (pdb code 1ef3). This binding sites where shown within 5.0 Angstroms radius around Fluorine atom.
In total 2 binding sites of Fluorine where determined in the Fidarestat Bound to Human Aldose Reductase, PDB code: 1ef3:
Jump to Fluorine binding site number: 1; 2;

Fluorine binding site 1 out of 2 in the Fidarestat Bound to Human Aldose Reductase


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 1 of Fidarestat Bound to Human Aldose Reductase within 5.0Å range: probe atom residue distance (Å) B Occ A:F340 b:5.0 occ:1.00 F17 A:FID340 0.0 5.0 1.0 C14 A:FID340 1.3 5.0 1.0 C13 A:FID340 2.3 5.0 1.0 C15 A:FID340 2.3 5.0 1.0 O A:VAL47 3.0 5.0 1.0 NE1 A:TRP20 3.6 5.0 1.0 C12 A:FID340 3.6 5.0 1.0 C16 A:FID340 3.6 5.0 1.0 CD1 A:TRP20 3.7 5.0 1.0 C A:VAL47 3.7 5.0 1.0 CG1 A:VAL47 3.9 5.0 1.0 CG2 A:VAL47 3.9 5.0 1.0 CA A:TYR48 4.0 5.0 1.0 C11 A:FID340 4.1 5.0 1.0 CD1 A:TYR48 4.1 5.0 1.0 N A:TYR48 4.2 5.0 1.0 CB A:VAL47 4.3 5.0 1.0 CA A:VAL47 4.7 5.0 1.0 CE2 A:TRP20 4.7 5.0 1.0 CE1 A:TYR48 4.7 5.0 1.0 C7I A:FID340 4.8 5.0 1.0 CG A:TRP20 4.8 5.0 1.0 C A:TYR48 4.9 5.0 1.0 N1I A:FID340 5.0 5.0 1.0

Fluorine binding site 2 out of 2 in the Fidarestat Bound to Human Aldose Reductase


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 2 of Fidarestat Bound to Human Aldose Reductase within 5.0Å range: probe atom residue distance (Å) B Occ B:F350 b:5.0 occ:1.00 F17 B:FID350 0.0 5.0 1.0 C14 B:FID350 1.3 5.0 1.0 C13 B:FID350 2.3 5.0 1.0 C15 B:FID350 2.4 5.0 1.0 O B:VAL47 3.3 5.0 1.0 CG1 B:VAL47 3.4 5.0 1.0 NE1 B:TRP20 3.5 5.0 1.0 C12 B:FID350 3.6 5.0 1.0 CG2 B:VAL47 3.6 5.0 1.0 C16 B:FID350 3.6 5.0 1.0 C B:VAL47 3.8 5.0 1.0 CD1 B:TRP20 3.9 5.0 1.0 CB B:VAL47 4.0 5.0 1.0 C11 B:FID350 4.1 5.0 1.0 N B:TYR48 4.3 5.0 1.0 CD2 B:TYR48 4.3 5.0 1.0 CA B:TYR48 4.3 5.0 1.0 CA B:VAL47 4.5 5.0 1.0 CE2 B:TRP20 4.5 5.0 1.0 CE2 B:TYR48 4.8 5.0 1.0 C7I B:FID350 4.8 5.0 1.0 N1I B:FID350 5.0 5.0 1.0 CG B:TRP20 5.0 5.0 1.0

M.Oka, Y.Matsumoto, S.Sugiyama, N.Tsuruta, M.Matsushima. A Potent Aldose Reductase Inhibitor, (2S,4S)-6-Fluoro-2', 5'-Dioxospiro[Chroman-4,4'-Imidazolidine]-2-Carboxamide (Fidarestat): Its Absolute Configuration and Interactions with the Aldose Reductase By X-Ray Crystallography. J.Med.Chem. V. 43 2479 2000.
ISSN: ISSN 0022-2623
PubMed: 10882376
DOI: 10.1021/JM990502R