Fluorine in PDB 1ah3: Aldose Reductase Complexed with Tolrestat Inhibitor

All present enzymatic activity of Aldose Reductase Complexed with Tolrestat Inhibitor:
1.1.1.21;

The structure of Aldose Reductase Complexed with Tolrestat Inhibitor, PDB code: 1ah3 was solved by D.Moras, A.Podjarny, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	6.00 / 2.30
Space group	P 43 21 2
Cell size a, b, c (Å), α, β, γ (°)	68.420, 68.420, 153.560, 90.00, 90.00, 90.00
R / Rfree (%)	20.7 / 29

The binding sites of Fluorine atom in the Aldose Reductase Complexed with Tolrestat Inhibitor (pdb code 1ah3). This binding sites where shown within 5.0 Angstroms radius around Fluorine atom.
In total 3 binding sites of Fluorine where determined in the Aldose Reductase Complexed with Tolrestat Inhibitor, PDB code: 1ah3:
Jump to Fluorine binding site number: 1; 2; 3;

Fluorine binding site 1 out of 3 in the Aldose Reductase Complexed with Tolrestat Inhibitor


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 1 of Aldose Reductase Complexed with Tolrestat Inhibitor within 5.0Å range: probe atom residue distance (Å) B Occ A:F320 b:37.5 occ:1.00 F1 A:TOL320 0.0 37.5 1.0 C1 A:TOL320 1.4 34.7 1.0 F2 A:TOL320 2.2 34.4 1.0 F3 A:TOL320 2.2 47.2 1.0 HG A:SER302 2.3 20.0 1.0 C2 A:TOL320 2.4 39.5 1.0 OG A:SER302 2.7 58.1 1.0 C11 A:TOL320 2.8 35.6 1.0 C12 A:TOL320 2.9 37.5 1.0 CD1 A:LEU300 3.2 54.3 1.0 CG A:LEU300 3.5 58.0 1.0 C3 A:TOL320 3.6 37.2 1.0 CB A:LEU300 3.8 53.6 1.0 CB A:SER302 3.8 43.5 1.0 O1 A:TOL320 3.9 37.6 1.0 O A:HOH467 4.0 64.5 1.0 C10 A:TOL320 4.1 29.6 1.0 H A:SER302 4.1 20.0 1.0 C7 A:TOL320 4.3 39.5 1.0 CA A:LEU300 4.4 55.9 1.0 H A:CYS303 4.6 20.0 1.0 C5 A:TOL320 4.7 39.0 1.0 O A:LEU300 4.7 47.8 1.0 C A:LEU300 4.7 52.6 1.0 N A:SER302 4.8 50.1 1.0 CA A:SER302 4.8 45.8 1.0 N A:CYS303 5.0 44.2 1.0 CD2 A:LEU300 5.0 61.3 1.0 C6 A:TOL320 5.0 40.2 1.0

Fluorine binding site 2 out of 3 in the Aldose Reductase Complexed with Tolrestat Inhibitor


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 2 of Aldose Reductase Complexed with Tolrestat Inhibitor within 5.0Å range: probe atom residue distance (Å) B Occ A:F320 b:34.4 occ:1.00 F2 A:TOL320 0.0 34.4 1.0 C1 A:TOL320 1.4 34.7 1.0 F1 A:TOL320 2.2 37.5 1.0 F3 A:TOL320 2.2 47.2 1.0 C2 A:TOL320 2.4 39.5 1.0 O1 A:TOL320 2.5 37.6 1.0 C3 A:TOL320 2.8 37.2 1.0 HG A:SER302 3.5 20.0 1.0 CB A:CYS303 3.6 37.6 1.0 OG A:SER302 3.6 58.1 1.0 CG2 A:VAL130 3.7 44.3 1.0 C12 A:TOL320 3.7 37.5 1.0 C4 A:TOL320 3.9 32.5 1.0 CZ A:PHE115 3.9 17.9 1.0 N A:CYS303 4.1 44.2 1.0 H A:CYS303 4.1 20.0 1.0 CB A:SER302 4.2 43.5 1.0 C11 A:TOL320 4.2 35.6 1.0 C5 A:TOL320 4.3 39.0 1.0 CB A:LEU300 4.3 53.6 1.0 CA A:CYS303 4.4 42.4 1.0 C A:SER302 4.4 44.1 1.0 SG A:CYS303 4.4 60.1 1.0 CG A:LEU300 4.5 58.0 1.0 CE2 A:PHE115 4.6 19.3 1.0 O A:LEU300 4.7 47.8 1.0 CB A:VAL130 4.7 44.4 1.0 CA A:SER302 4.8 45.8 1.0 O A:SER302 4.8 40.4 1.0 CD1 A:PHE122 4.9 28.3 1.0 C7 A:TOL320 4.9 39.5 1.0 CE1 A:PHE115 4.9 13.3 1.0 CD1 A:LEU300 4.9 54.3 1.0 H A:SER302 4.9 20.0 1.0

Fluorine binding site 3 out of 3 in the Aldose Reductase Complexed with Tolrestat Inhibitor


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 3 of Aldose Reductase Complexed with Tolrestat Inhibitor within 5.0Å range: probe atom residue distance (Å) B Occ A:F320 b:47.2 occ:1.00 F3 A:TOL320 0.0 47.2 1.0 C1 A:TOL320 1.4 34.7 1.0 F2 A:TOL320 2.2 34.4 1.0 F1 A:TOL320 2.2 37.5 1.0 C2 A:TOL320 2.4 39.5 1.0 C11 A:TOL320 2.9 35.6 1.0 C12 A:TOL320 3.0 37.5 1.0 CD1 A:PHE122 3.2 28.3 1.0 O A:HOH467 3.4 64.5 1.0 CE1 A:PHE122 3.4 39.2 1.0 HG A:SER302 3.5 20.0 1.0 C3 A:TOL320 3.5 37.2 1.0 O1 A:TOL320 3.9 37.6 1.0 CG2 A:VAL130 4.0 44.3 1.0 OG A:SER302 4.1 58.1 1.0 CG A:PHE122 4.2 31.9 1.0 C10 A:TOL320 4.2 29.6 1.0 C7 A:TOL320 4.3 39.5 1.0 CZ A:PHE122 4.5 38.3 1.0 C5 A:TOL320 4.7 39.0 1.0 CB A:SER302 4.7 43.5 1.0 CB A:PHE122 4.7 34.9 1.0 O A:HOH605 4.7 41.5 1.0 CZ A:PHE115 4.7 17.9 1.0 CE2 A:PHE115 4.7 19.3 1.0 C6 A:TOL320 5.0 40.2 1.0

A.Urzhumtsev, F.Tete-Favier, A.Mitschler, J.Barbanton, P.Barth, L.Urzhumtseva, J.F.Biellmann, A.Podjarny, D.Moras. A 'Specificity' Pocket Inferred From the Crystal Structures of the Complexes of Aldose Reductase with the Pharmaceutically Important Inhibitors Tolrestat and Sorbinil. Structure V. 5 601 1997.
ISSN: ISSN 0969-2126
PubMed: 9195881
DOI: 10.1016/S0969-2126(97)00216-5