Fluorine in PDB 1ah0: Pig Aldose Reductase Complexed with Sorbinil

All present enzymatic activity of Pig Aldose Reductase Complexed with Sorbinil:
1.1.1.21;

The structure of Pig Aldose Reductase Complexed with Sorbinil, PDB code: 1ah0 was solved by D.Moras, A.D.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 (°)	67.920, 67.920, 152.800, 90.00, 90.00, 90.00
R / Rfree (%)	19.2 / 26.3

The binding sites of Fluorine atom in the Pig Aldose Reductase Complexed with Sorbinil (pdb code 1ah0). 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 Pig Aldose Reductase Complexed with Sorbinil, PDB code: 1ah0:

Fluorine binding site 1 out of 1 in the Pig Aldose Reductase Complexed with Sorbinil


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 1 of Pig Aldose Reductase Complexed with Sorbinil within 5.0Å range: probe atom residue distance (Å) B Occ A:F320 b:64.4 occ:1.00 F1 A:SBI320 0.0 64.4 1.0 C1 A:SBI320 1.3 62.3 1.0 C11 A:SBI320 2.4 54.4 1.0 C2 A:SBI320 2.4 63.8 1.0 HE1 A:TRP20 2.7 20.0 1.0 O A:HOH505 3.1 72.7 1.0 NE1 A:TRP20 3.5 25.4 1.0 C3 A:SBI320 3.6 58.2 1.0 C10 A:SBI320 3.7 59.5 1.0 O A:HOH755 3.7 50.3 0.7 O A:VAL47 3.8 21.2 1.0 CD1 A:TRP20 4.1 25.0 1.0 CG2 A:VAL47 4.1 15.8 1.0 CG1 A:VAL47 4.1 14.2 1.0 C4 A:SBI320 4.1 59.9 1.0 CE2 A:TRP20 4.4 21.6 1.0 C A:VAL47 4.5 13.3 1.0 CB A:VAL47 4.7 13.7 1.0 CD1 A:TYR48 4.7 18.6 1.0 CE1 A:PHE122 4.8 30.6 1.0 CZ2 A:TRP20 4.8 25.6 1.0 C7 A:SBI320 4.9 56.9 1.0 CZ A:PHE122 5.0 36.1 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