Fluorine in PDB 2pdi: Human Aldose Reductase Mutant L300A Complexed with Zopolrestat at 1.55 A.

All present enzymatic activity of Human Aldose Reductase Mutant L300A Complexed with Zopolrestat at 1.55 A.:
1.1.1.21;

The structure of Human Aldose Reductase Mutant L300A Complexed with Zopolrestat at 1.55 A., PDB code: 2pdi was solved by H.Steuber, A.Heine, G.Klebe, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	30.00 / 1.55
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	49.440, 66.860, 47.300, 90.00, 92.95, 90.00
R / Rfree (%)	15.5 / 20

The binding sites of Fluorine atom in the Human Aldose Reductase Mutant L300A Complexed with Zopolrestat at 1.55 A. (pdb code 2pdi). 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 Mutant L300A Complexed with Zopolrestat at 1.55 A., PDB code: 2pdi:
Jump to Fluorine binding site number: 1; 2; 3;

Fluorine binding site 1 out of 3 in the Human Aldose Reductase Mutant L300A Complexed with Zopolrestat at 1.55 A.


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 Mutant L300A Complexed with Zopolrestat at 1.55 A. within 5.0Å range: probe atom residue distance (Å) B Occ A:F600 b:7.9 occ:1.00 F1 A:ZST600 0.0 7.9 1.0 C19 A:ZST600 1.4 8.7 1.0 F3 A:ZST600 2.0 14.3 1.0 F2 A:ZST600 2.1 13.8 1.0 C15 A:ZST600 2.3 5.9 1.0 C14 A:ZST600 2.8 8.6 1.0 OG1 A:THR113 3.1 7.7 1.0 CG2 A:THR113 3.3 8.6 1.0 CE3 A:TRP111 3.3 6.9 1.0 CD A:PRO310 3.4 9.0 1.0 C16 A:ZST600 3.4 6.1 1.0 CB A:THR113 3.8 8.2 1.0 CB A:TRP111 3.9 5.1 1.0 CG A:PRO310 4.0 9.4 1.0 CD2 A:TRP111 4.0 7.6 1.0 CZ3 A:TRP111 4.0 7.9 1.0 CD A:PRO112 4.1 5.4 1.0 C13 A:ZST600 4.1 9.8 1.0 CG A:TRP111 4.3 7.5 1.0 CG A:PRO112 4.3 7.6 1.0 N A:THR113 4.5 6.6 1.0 C12 A:ZST600 4.6 8.3 1.0 N A:PRO112 4.7 7.5 1.0 CD1 A:TYR309 4.7 15.4 1.0 N A:PRO310 4.7 11.0 1.0 CA A:TYR309 4.7 11.9 1.0 C11 A:ZST600 4.8 9.2 1.0 CA A:THR113 4.9 9.8 1.0 CA A:TRP111 4.9 5.0 1.0 O A:ASP308 4.9 7.9 1.0

Fluorine binding site 2 out of 3 in the Human Aldose Reductase Mutant L300A Complexed with Zopolrestat at 1.55 A.


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 Mutant L300A Complexed with Zopolrestat at 1.55 A. within 5.0Å range: probe atom residue distance (Å) B Occ A:F600 b:13.8 occ:1.00 F2 A:ZST600 0.0 13.8 1.0 C19 A:ZST600 1.3 8.7 1.0 F1 A:ZST600 2.1 7.9 1.0 F3 A:ZST600 2.2 14.3 1.0 C15 A:ZST600 2.4 5.9 1.0 C14 A:ZST600 3.1 8.6 1.0 CG2 A:THR113 3.2 8.6 1.0 CB A:CYS303 3.2 16.9 1.0 OG1 A:THR113 3.3 7.7 1.0 C16 A:ZST600 3.4 6.1 1.0 CD1 A:TYR309 3.7 15.4 1.0 CB A:THR113 3.7 8.2 1.0 O A:CYS303 3.9 11.2 1.0 SG A:CYS303 3.9 10.3 1.0 CD A:PRO310 4.3 9.0 1.0 CA A:CYS303 4.4 8.3 1.0 C13 A:ZST600 4.4 9.8 1.0 CA A:TYR309 4.4 11.9 1.0 C A:CYS303 4.4 8.2 1.0 CE1 A:TYR309 4.4 13.4 1.0 CG A:TYR309 4.7 11.2 1.0 CB A:HIS306 4.7 8.7 1.0 CB A:TYR309 4.7 18.2 1.0 C12 A:ZST600 4.7 8.3 1.0 CE1 A:PHE115 4.7 8.2 1.0 CZ A:PHE115 4.9 8.3 1.0 CE3 A:TRP111 5.0 6.9 1.0 C11 A:ZST600 5.0 9.2 1.0

Fluorine binding site 3 out of 3 in the Human Aldose Reductase Mutant L300A Complexed with Zopolrestat at 1.55 A.


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 Mutant L300A Complexed with Zopolrestat at 1.55 A. within 5.0Å range: probe atom residue distance (Å) B Occ A:F600 b:14.3 occ:1.00 F3 A:ZST600 0.0 14.3 1.0 C19 A:ZST600 1.3 8.7 1.0 F1 A:ZST600 2.0 7.9 1.0 F2 A:ZST600 2.2 13.8 1.0 C15 A:ZST600 2.3 5.9 1.0 C16 A:ZST600 2.6 6.1 1.0 CD1 A:TYR309 3.1 15.4 1.0 CD A:PRO310 3.1 9.0 1.0 CE1 A:TYR309 3.3 13.4 1.0 C14 A:ZST600 3.6 8.6 1.0 CG A:PRO310 3.9 9.4 1.0 CE3 A:TRP111 3.9 6.9 1.0 CZ3 A:TRP111 3.9 7.9 1.0 C12 A:ZST600 4.0 8.3 1.0 CG A:TYR309 4.2 11.2 1.0 CB A:CYS303 4.2 16.9 1.0 N A:PRO310 4.4 11.0 1.0 CA A:TYR309 4.4 11.9 1.0 CZ A:TYR309 4.4 14.8 1.0 CG2 A:THR113 4.6 8.6 1.0 C13 A:ZST600 4.7 9.8 1.0 CB A:TYR309 4.7 18.2 1.0 CE2 A:PHE311 4.8 7.5 1.0 C11 A:ZST600 4.8 9.2 1.0 OG1 A:THR113 4.8 7.7 1.0 CD2 A:TRP111 4.9 7.6 1.0 O A:CYS303 4.9 11.2 1.0 CD2 A:PHE311 4.9 5.5 1.0 C A:TYR309 4.9 9.9 1.0 CH2 A:TRP111 5.0 6.1 1.0

H.Steuber, A.Heine, A.Podjarny, G.Klebe. Merging the Binding Sites of Aldose and Aldehyde Reductase For Detection of Inhibitor Selectivity-Determining Features. J.Mol.Biol. V. 379 991 2008.
ISSN: ISSN 0022-2836
PubMed: 18495158
DOI: 10.1016/J.JMB.2008.03.063