Fluorine in PDB 1us0: Human Aldose Reductase in Complex with Nadp+ and the Inhibitor IDD594 at 0.66 Angstrom

All present enzymatic activity of Human Aldose Reductase in Complex with Nadp+ and the Inhibitor IDD594 at 0.66 Angstrom:
1.1.1.21;

The structure of Human Aldose Reductase in Complex with Nadp+ and the Inhibitor IDD594 at 0.66 Angstrom, PDB code: 1us0 was solved by E.I.Howard, R.Sanishvili, R.E.Cachau, A.Mitschler, B.Chevrier, P.Barth, V.Lamour, M.Van Zandt, E.Sibley, C.Bon, D.Moras, T.R.Schneider, A.Joachimiak, A.Podjarny, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	20.00 / 0.66
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	49.280, 66.590, 47.260, 90.00, 92.40, 90.00
R / Rfree (%)	9.4 / 10.3

The structure of Human Aldose Reductase in Complex with Nadp+ and the Inhibitor IDD594 at 0.66 Angstrom also contains other interesting chemical elements:

Bromine

(Br)

1 atom

The binding sites of Fluorine atom in the Human Aldose Reductase in Complex with Nadp+ and the Inhibitor IDD594 at 0.66 Angstrom (pdb code 1us0). This binding sites where shown within 5.0 Angstroms radius around Fluorine atom.
In total 2 binding sites of Fluorine where determined in the Human Aldose Reductase in Complex with Nadp+ and the Inhibitor IDD594 at 0.66 Angstrom, PDB code: 1us0:
Jump to Fluorine binding site number: 1; 2;

Fluorine binding site 1 out of 2 in the Human Aldose Reductase in Complex with Nadp+ and the Inhibitor IDD594 at 0.66 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 IDD594 at 0.66 Angstrom within 5.0Å range: probe atom residue distance (Å) B Occ A:F320 b:5.2 occ:1.00 F9 A:LDT320 0.0 5.2 1.0 C5 A:LDT320 1.4 4.1 1.0 C2 A:LDT320 2.3 3.9 1.0 C6 A:LDT320 2.4 4.4 1.0 O A:VAL47 3.0 3.3 1.0 O A:HOH2131 3.5 4.9 1.0 CD1 A:TYR48 3.5 2.9 1.0 C A:VAL47 3.6 2.8 1.0 C3 A:LDT320 3.6 4.2 1.0 C4 A:LDT320 3.6 3.5 1.0 CG1 A:VAL47 3.6 3.4 1.0 O A:HOH2061 3.6 7.8 0.5 O A:HOH2062 3.8 5.7 0.5 CA A:TYR48 3.9 2.8 1.0 NE1 A:TRP20 3.9 4.2 1.0 CG2 A:VAL47 3.9 3.6 1.0 CD1 A:TRP20 3.9 3.7 1.0 N A:TYR48 3.9 2.8 1.0 C7 A:LDT320 4.1 3.7 1.0 CE1 A:TYR48 4.2 2.9 1.0 CB A:VAL47 4.2 3.0 1.0 CA A:VAL47 4.5 2.8 1.0 CG A:TYR48 4.6 2.9 1.0 O15 A:LDT320 4.7 3.8 1.0 CB A:TYR48 4.8 3.0 1.0 O A:HOH2125 4.8 5.7 1.0 C A:TYR48 4.8 3.0 1.0 CE2 A:TRP20 4.9 4.2 1.0

Fluorine binding site 2 out of 2 in the Human Aldose Reductase in Complex with Nadp+ and the Inhibitor IDD594 at 0.66 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 IDD594 at 0.66 Angstrom within 5.0Å range: probe atom residue distance (Å) B Occ A:F320 b:5.0 occ:1.00 F14 A:LDT320 0.0 5.0 1.0 C27 A:LDT320 1.4 4.2 1.0 C24 A:LDT320 2.3 4.0 1.0 C28 A:LDT320 2.3 4.5 1.0 C13 A:LDT320 2.8 4.6 1.0 C A:ALA299 3.0 5.3 1.0 CA A:ALA299 3.1 5.5 1.0 CH2 A:TRP111 3.2 4.7 1.0 N A:ALA299 3.3 5.1 1.0 N A:LEU300 3.3 5.2 1.0 O A:ALA299 3.5 6.1 1.0 CB A:LEU300 3.5 5.2 1.0 C25 A:LDT320 3.6 4.5 1.0 C26 A:LDT320 3.6 4.2 1.0 C A:CYS298 3.6 4.9 0.5 CZ2 A:TRP111 3.6 4.8 1.0 C A:CYS298 3.7 4.3 0.5 CZ3 A:TRP111 3.7 4.3 1.0 O A:CYS298 3.8 5.3 0.5 O A:CYS298 4.0 6.2 0.5 CA A:LEU300 4.0 4.9 1.0 C29 A:LDT320 4.1 4.4 1.0 N17 A:LDT320 4.2 4.2 1.0 CB A:CYS298 4.4 4.9 0.5 CA A:CYS298 4.4 5.0 0.5 CE2 A:TRP111 4.4 4.1 1.0 SG A:CYS298 4.4 4.7 0.5 OH A:TYR309 4.4 6.2 1.0 CB A:ALA299 4.5 6.9 1.0 CE3 A:TRP111 4.5 3.8 1.0 CE2 A:PHE311 4.7 6.0 0.5 CA A:CYS298 4.7 4.2 0.5 CE2 A:PHE311 4.7 5.3 0.5 CE1 A:TYR309 4.8 5.5 1.0 CD2 A:TRP111 4.9 3.6 1.0 CG A:LEU300 4.9 5.7 1.0

E.I.Howard, R.Sanishvili, R.E.Cachau, A.Mitschler, B.Chevrier, P.Barth, V.Lamour, M.Van Zandt, E.Sibley, C.Bon, D.Moras, T.R.Schneider, A.Joachimiak, A.Podjarny. Ultrahigh Resolution Drug Design I: Details of Interactions in Human Aldose Reductase-Inhibitor Complex at 0.66 A. Proteins V. 55 792 2004.
ISSN: ISSN 0887-3585
PubMed: 15146478
DOI: 10.1002/PROT.20015