Fluorine in PDB 2pdk: Human Aldose Reductase Mutant L301M Complexed with Sorbinil.

All present enzymatic activity of Human Aldose Reductase Mutant L301M Complexed with Sorbinil.:
1.1.1.21;

The structure of Human Aldose Reductase Mutant L301M Complexed with Sorbinil., PDB code: 2pdk 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)	50.00 / 1.55
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	49.420, 66.620, 47.370, 90.00, 91.86, 90.00
R / Rfree (%)	15.9 / 20.1

The binding sites of Fluorine atom in the Human Aldose Reductase Mutant L301M Complexed with Sorbinil. (pdb code 2pdk). 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 Human Aldose Reductase Mutant L301M Complexed with Sorbinil., PDB code: 2pdk:

Fluorine binding site 1 out of 1 in the Human Aldose Reductase Mutant L301M 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 Human Aldose Reductase Mutant L301M Complexed with Sorbinil. within 5.0Å range: probe atom residue distance (Å) B Occ A:F600 b:65.6 occ:1.00 F1 A:SBI600 0.0 65.6 1.0 C1 A:SBI600 1.3 32.8 1.0 C11 A:SBI600 2.4 30.6 1.0 C2 A:SBI600 2.4 26.3 1.0 O A:VAL47 3.0 14.3 1.0 O A:HOH614 3.6 15.5 1.0 O A:HOH905 3.6 33.1 1.0 C3 A:SBI600 3.7 46.0 1.0 C10 A:SBI600 3.7 36.3 1.0 C A:VAL47 3.7 11.7 1.0 NE1 A:TRP20 3.8 21.6 1.0 CG1 A:VAL47 3.9 12.8 1.0 CG2 A:VAL47 3.9 14.4 1.0 CD1 A:TRP20 4.0 14.8 1.0 CD1 A:TYR48 4.0 11.2 1.0 C4 A:SBI600 4.1 44.6 1.0 CA A:TYR48 4.2 10.6 1.0 N A:TYR48 4.2 12.1 1.0 CB A:VAL47 4.3 12.4 1.0 O A:HOH688 4.4 20.7 1.0 CA A:VAL47 4.7 11.2 1.0 CE1 A:TYR48 4.7 14.4 1.0 O A:HOH618 4.7 16.3 1.0 CE2 A:TRP20 4.9 15.3 1.0 C7 A:SBI600 5.0 37.2 1.0 CG A:TYR48 5.0 7.7 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