Fluorine in PDB 8bjl: Human Aldose Reductase in Complex with A Ligand with A Fluoro-Indol- Acetic-Acid Structure (SCHL44172)

All present enzymatic activity of Human Aldose Reductase in Complex with A Ligand with A Fluoro-Indol- Acetic-Acid Structure (SCHL44172):
1.1.1.21; 1.1.1.300; 1.1.1.372; 1.1.1.54;

The structure of Human Aldose Reductase in Complex with A Ligand with A Fluoro-Indol- Acetic-Acid Structure (SCHL44172), PDB code: 8bjl was solved by L.-S.Hubert, A.Heine, G.Klebe, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	27.09 / 0.97
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	47.073, 66.28, 49.342, 90, 92.66, 90
R / Rfree (%)	11.7 / 12.6

The binding sites of Fluorine atom in the Human Aldose Reductase in Complex with A Ligand with A Fluoro-Indol- Acetic-Acid Structure (SCHL44172) (pdb code 8bjl). 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 A Ligand with A Fluoro-Indol- Acetic-Acid Structure (SCHL44172), PDB code: 8bjl:
Jump to Fluorine binding site number: 1; 2; 3;

Fluorine binding site 1 out of 3 in the Human Aldose Reductase in Complex with A Ligand with A Fluoro-Indol- Acetic-Acid Structure (SCHL44172)


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 A Ligand with A Fluoro-Indol- Acetic-Acid Structure (SCHL44172) within 5.0Å range: probe atom residue distance (Å) B Occ A:F402 b:11.7 occ:0.64 F A:QXO402 0.0 11.7 0.6 C7 A:QXO402 1.4 11.3 0.6 H A:LEU300 2.3 15.4 1.0 C8 A:QXO402 2.4 11.5 0.6 C6 A:QXO402 2.4 10.5 0.6 HB3 A:CYS298 2.7 12.2 1.0 HA A:CYS298 2.8 11.7 1.0 N A:LEU300 3.1 12.8 1.0 HA A:LEU300 3.2 16.1 1.0 C2 A:QXO402 3.2 11.3 0.4 CA A:CYS298 3.3 9.7 1.0 CB A:CYS298 3.4 10.1 1.0 H A:ALA299 3.4 13.6 1.0 C3 A:QXO402 3.4 11.7 0.4 HZ2 A:TRP111 3.5 11.9 1.0 C A:CYS298 3.5 10.1 1.0 N A:ALA299 3.5 11.3 1.0 HH2 A:TRP111 3.6 11.8 1.0 C9 A:QXO402 3.6 11.7 0.6 C5 A:QXO402 3.6 10.7 0.6 CA A:LEU300 3.6 13.4 1.0 HB2 A:LEU300 3.7 16.3 1.0 O A:QXO403 3.7 23.0 0.8 HD12 A:LEU300 3.7 17.8 1.0 CZ2 A:TRP111 3.9 9.9 1.0 HD13 A:LEU300 3.9 17.8 1.0 CH2 A:TRP111 4.0 9.9 1.0 HH2 A:TRP219 4.0 15.6 1.0 SG A:CYS298 4.0 10.3 1.0 O A:HOH545 4.0 16.0 1.0 HZ2 A:TRP219 4.1 14.6 1.0 C4 A:QXO402 4.1 11.3 0.6 CB A:LEU300 4.1 13.5 1.0 C A:ALA299 4.2 12.9 1.0 O A:CYS298 4.2 10.8 1.0 HB2 A:CYS298 4.2 12.2 1.0 CD1 A:LEU300 4.3 14.8 1.0 CH2 A:TRP219 4.4 13.0 1.0 CA A:ALA299 4.4 12.5 1.0 CZ2 A:TRP219 4.4 12.1 1.0 N A:QXO402 4.6 10.8 0.4 C A:QXO403 4.6 25.1 0.8 N A:CYS298 4.7 9.6 1.0 H A:LEU301 4.8 17.6 1.0 CG A:LEU300 4.9 13.8 1.0 N A:QXO402 4.9 10.3 0.6 C4 A:QXO402 4.9 11.9 0.4 O A:VAL297 4.9 10.9 1.0 HA A:ALA299 4.9 15.0 1.0 HB3 A:LEU300 5.0 16.3 1.0 C A:LEU300 5.0 14.2 1.0 CE2 A:TRP111 5.0 9.2 1.0

Fluorine binding site 2 out of 3 in the Human Aldose Reductase in Complex with A Ligand with A Fluoro-Indol- Acetic-Acid Structure (SCHL44172)


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 A Ligand with A Fluoro-Indol- Acetic-Acid Structure (SCHL44172) within 5.0Å range: probe atom residue distance (Å) B Occ A:F402 b:12.0 occ:0.36 F A:QXO402 0.0 12.0 0.4 C7 A:QXO402 1.4 11.8 0.4 C6 A:QXO402 2.3 11.4 0.4 C8 A:QXO402 2.4 12.0 0.4 HG13 A:VAL47 2.7 10.1 1.0 HD1 A:TYR48 2.8 8.8 1.0 O A:VAL47 3.0 8.1 1.0 C2 A:QXO402 3.1 11.3 0.6 HG22 A:VAL47 3.1 10.5 1.0 HA A:TYR48 3.2 8.8 1.0 HE1 A:TRP20 3.3 10.3 1.0 O A:HOH854 3.4 15.7 1.0 O A:HOH671 3.4 24.3 1.0 HD1 A:TRP20 3.5 9.6 1.0 C5 A:QXO402 3.6 11.3 0.4 C9 A:QXO402 3.6 12.1 0.4 CG1 A:VAL47 3.6 8.4 1.0 C A:VAL47 3.6 7.4 1.0 CD1 A:TYR48 3.7 7.3 1.0 NE1 A:TRP20 3.7 8.6 1.0 C3 A:QXO402 3.7 11.8 0.6 O A:HOH526 3.8 13.1 1.0 CD1 A:TRP20 3.9 8.0 1.0 CG2 A:VAL47 3.9 8.8 1.0 HE1 A:TYR48 4.0 8.6 1.0 CA A:TYR48 4.0 7.3 1.0 HG11 A:VAL47 4.0 10.1 1.0 N A:TYR48 4.1 7.0 1.0 C4 A:QXO402 4.1 11.9 0.4 HG12 A:VAL47 4.1 10.1 1.0 HG21 A:VAL47 4.2 10.5 1.0 CB A:VAL47 4.2 7.8 1.0 N A:QXO402 4.2 10.3 0.6 CE1 A:TYR48 4.3 7.2 1.0 CA A:VAL47 4.5 7.5 1.0 O A:HOH703 4.6 12.6 1.0 C1 A:QXO402 4.7 9.1 0.6 HG23 A:VAL47 4.7 10.5 1.0 H A:TYR48 4.7 8.4 1.0 CG A:TYR48 4.7 7.0 1.0 CE2 A:TRP20 4.8 8.7 1.0 O A:HOH853 4.8 27.8 1.0 N A:QXO402 4.9 10.8 0.4 CB A:TYR48 4.9 7.4 1.0 HA A:VAL47 5.0 9.0 1.0 C A:TYR48 5.0 7.5 1.0

Fluorine binding site 3 out of 3 in the Human Aldose Reductase in Complex with A Ligand with A Fluoro-Indol- Acetic-Acid Structure (SCHL44172)


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 A Ligand with A Fluoro-Indol- Acetic-Acid Structure (SCHL44172) within 5.0Å range: probe atom residue distance (Å) B Occ A:F403 b:34.1 occ:0.85 F A:QXO403 0.0 34.1 0.8 C7 A:QXO403 1.4 33.5 0.8 C6 A:QXO403 2.3 32.7 0.8 C8 A:QXO403 2.3 33.5 0.8 O A:HOH889 2.6 45.2 1.0 HZ3 A:TRP219 3.4 16.7 1.0 C5 A:QXO403 3.6 31.7 0.8 C9 A:QXO403 3.6 33.0 0.8 C9 A:QXO402 3.6 11.7 0.6 C4 A:QXO403 4.1 32.2 0.8 CZ3 A:TRP219 4.1 13.9 1.0 C4 A:QXO402 4.2 11.3 0.6 C3 A:QXO402 4.3 11.8 0.6 C9 A:QXO402 4.3 12.1 0.4 HE3 A:TRP219 4.4 16.3 1.0 C8 A:QXO402 4.6 11.5 0.6 CE3 A:TRP219 4.7 13.6 1.0 O1 A:QXO403 4.8 25.0 0.8 C4 A:QXO402 4.9 11.9 0.4 N A:QXO403 4.9 30.1 0.8 HE2 A:PHE122 5.0 15.2 1.0

L.-S.Hubert, A.Heine, G.Klebe, S.Reul, M.Schlitzer. Human Aldose Reductase in Complex with A Ligand with A Fluoro-Indol-Acetic-Acid Structure (SCHL44172) To Be Published.