Fluorine in PDB 1z3n: Human Aldose Reductase in Complex with Nadp+ and the Inhibitor Lidorestat at 1.04 Angstrom

All present enzymatic activity of Human Aldose Reductase in Complex with Nadp+ and the Inhibitor Lidorestat at 1.04 Angstrom:
1.1.1.21;

The structure of Human Aldose Reductase in Complex with Nadp+ and the Inhibitor Lidorestat at 1.04 Angstrom, PDB code: 1z3n was solved by M.C.Van Zandt, M.L.Jones, D.E.Gunn, L.S.Geraci, J.H.Jones, D.R.Sawicki, J.Sredy, J.L.Jacot, A.T.Dicioccio, T.Petrova, A.Mitschler, A.D.Podjarny, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	10.00 / 1.04
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	50.140, 67.340, 47.880, 90.00, 92.50, 90.00
R / Rfree (%)	9.7 / 12.5

The binding sites of Fluorine atom in the Human Aldose Reductase in Complex with Nadp+ and the Inhibitor Lidorestat at 1.04 Angstrom (pdb code 1z3n). This binding sites where shown within 5.0 Angstroms radius around Fluorine atom.
In total 3 binding sites of Fluorine where determined in the Human Aldose Reductase in Complex with Nadp+ and the Inhibitor Lidorestat at 1.04 Angstrom, PDB code: 1z3n:
Jump to Fluorine binding site number: 1; 2; 3;

Fluorine binding site 1 out of 3 in the Human Aldose Reductase in Complex with Nadp+ and the Inhibitor Lidorestat at 1.04 Angstrom


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 1 of Human Aldose Reductase in Complex with Nadp+ and the Inhibitor Lidorestat at 1.04 Angstrom within 5.0Å range: probe atom residue distance (Å) B Occ A:F320 b:12.4 occ:1.00 F19 A:3NA320 0.0 12.4 1.0 C28 A:3NA320 1.3 10.0 1.0 C27 A:3NA320 2.4 9.3 1.0 C25 A:3NA320 2.4 10.9 1.0 S14 A:3NA320 3.1 10.3 1.0 CH2 A:TRP79 3.4 10.4 1.0 CD1 A:TRP111 3.5 9.0 1.0 SG A:CYS80 3.5 9.1 1.0 CZ A:PHE115 3.5 12.6 1.0 CG A:TRP111 3.5 7.7 1.0 C29 A:3NA320 3.6 11.4 1.0 C24 A:3NA320 3.6 10.1 1.0 NE1 A:TRP111 3.8 9.7 1.0 CZ2 A:TRP79 3.9 10.2 1.0 CD2 A:TRP111 3.9 8.1 1.0 CE2 A:PHE115 3.9 11.8 1.0 CE2 A:PHE122 4.0 16.8 1.0 CE2 A:TRP111 4.0 8.6 1.0 CB A:TRP111 4.1 8.0 1.0 C26 A:3NA320 4.1 11.5 1.0 CZ3 A:TRP79 4.2 9.4 1.0 OG1 A:THR113 4.2 10.0 1.0 CZ A:PHE122 4.4 16.4 1.0 C13 A:3NA320 4.6 9.7 1.0 CE1 A:PHE115 4.6 11.7 1.0 CE3 A:TRP111 4.7 8.7 1.0 SG A:CYS303 4.7 18.4 1.0 F23 A:3NA320 4.7 14.7 1.0 N36 A:3NA320 4.7 10.4 1.0 CB A:CYS80 4.8 8.5 1.0 CZ2 A:TRP111 4.9 9.8 1.0 CD2 A:PHE122 4.9 14.4 1.0 CE2 A:TRP79 5.0 9.0 1.0

Fluorine binding site 2 out of 3 in the Human Aldose Reductase in Complex with Nadp+ and the Inhibitor Lidorestat at 1.04 Angstrom


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 2 of Human Aldose Reductase in Complex with Nadp+ and the Inhibitor Lidorestat at 1.04 Angstrom within 5.0Å range: probe atom residue distance (Å) B Occ A:F320 b:14.4 occ:1.00 F22 A:3NA320 0.0 14.4 1.0 C26 A:3NA320 1.3 11.5 1.0 C29 A:3NA320 2.4 11.4 1.0 C24 A:3NA320 2.4 10.1 1.0 F23 A:3NA320 2.7 14.7 1.0 N36 A:3NA320 2.9 10.4 1.0 N A:LEU300 3.4 14.4 1.0 CE1 A:TYR309 3.4 15.0 1.0 CA A:ALA299 3.6 11.7 0.4 C27 A:3NA320 3.6 9.3 1.0 C25 A:3NA320 3.6 10.9 1.0 CZ3 A:TRP111 3.6 10.5 1.0 CA A:ALA299 3.7 13.1 0.6 C A:ALA299 3.9 14.4 0.6 C A:ALA299 3.9 10.3 0.4 CD1 A:TYR309 4.0 13.5 1.0 CH2 A:TRP111 4.0 10.9 1.0 C28 A:3NA320 4.1 10.0 1.0 C13 A:3NA320 4.2 9.7 1.0 CB A:ALA299 4.2 14.1 0.4 CE3 A:TRP111 4.2 8.7 1.0 CE2 A:PHE311 4.2 12.6 1.0 CB A:CYS303 4.2 15.0 1.0 O A:LEU300 4.3 16.5 1.0 CB A:LEU300 4.3 19.7 1.0 CZ A:TYR309 4.4 15.9 1.0 CA A:LEU300 4.4 14.3 1.0 OH A:TYR309 4.5 20.8 1.0 CD2 A:PHE311 4.5 13.1 1.0 CB A:ALA299 4.5 17.5 0.6 N A:ALA299 4.7 11.0 0.6 N A:ALA299 4.8 12.6 0.4 SG A:CYS303 4.8 18.4 1.0 C A:LEU300 4.8 15.4 1.0 CZ2 A:TRP111 4.9 9.8 1.0 O A:CYS298 4.9 9.3 0.6 S14 A:3NA320 4.9 10.3 1.0

Fluorine binding site 3 out of 3 in the Human Aldose Reductase in Complex with Nadp+ and the Inhibitor Lidorestat at 1.04 Angstrom


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 3 of Human Aldose Reductase in Complex with Nadp+ and the Inhibitor Lidorestat at 1.04 Angstrom within 5.0Å range: probe atom residue distance (Å) B Occ A:F320 b:14.7 occ:1.00 F23 A:3NA320 0.0 14.7 1.0 C29 A:3NA320 1.4 11.4 1.0 C25 A:3NA320 2.3 10.9 1.0 C26 A:3NA320 2.4 11.5 1.0 F22 A:3NA320 2.7 14.4 1.0 CD1 A:TYR309 3.4 13.5 1.0 CB A:CYS303 3.5 15.0 1.0 C28 A:3NA320 3.6 10.0 1.0 C24 A:3NA320 3.6 10.1 1.0 CG2 A:THR113 3.8 11.2 1.0 CD A:PRO310 3.8 10.4 1.0 CE1 A:TYR309 3.8 15.0 1.0 CE3 A:TRP111 3.9 8.7 1.0 OG1 A:THR113 4.0 10.0 1.0 C27 A:3NA320 4.1 9.3 1.0 SG A:CYS303 4.2 18.4 1.0 CZ3 A:TRP111 4.2 10.5 1.0 CG A:TYR309 4.5 11.8 1.0 CB A:THR113 4.5 9.6 1.0 CA A:TYR309 4.6 11.1 1.0 CG A:PRO310 4.6 11.4 1.0 O A:CYS303 4.7 14.1 1.0 CD2 A:TRP111 4.7 8.1 1.0 F19 A:3NA320 4.7 12.4 1.0 N36 A:3NA320 4.8 10.4 1.0 CA A:CYS303 4.9 13.6 1.0 CB A:TYR309 4.9 12.8 1.0 N A:PRO310 5.0 10.0 1.0 C A:CYS303 5.0 13.3 1.0

M.C.Van Zandt, M.L.Jones, D.E.Gunn, L.S.Geraci, J.H.Jones, D.R.Sawicki, J.Sredy, J.L.Jacot, A.T.Dicioccio, T.Petrova, A.Mitschler, A.D.Podjarny. Discovery of 3-[(4,5,7-Trifluorobenzothiazol-2-Yl)Methyl]Indole- N-Acetic Acid (Lidorestat) and Congeners As Highly Potent and Selective Inhibitors of Aldose Reductase For Treatment of Chronic Diabetic Complications J.Med.Chem. V. 48 3141 2005.
ISSN: ISSN 0022-2623
PubMed: 15857120
DOI: 10.1021/JM0492094