Fluorine in PDB 2r24: Human Aldose Reductase Structure

All present enzymatic activity of Human Aldose Reductase Structure:
1.1.1.21;

The structure of Human Aldose Reductase Structure, PDB code: 2r24 was solved by M.P.Blakeley, F.Ruiz, R.Cachau, I.Hazemann, F.Meilleur, A.Mitschler, S.Ginell, P.Afonine, O.N.Ventura, A.Cousido-Siah, M.Haertlein, A.Joachimiak, D.Myles, A.Podjarny, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	N/A / 1.75
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	50.066, 67.126, 47.862, 90.00, 92.41, 90.00
R / Rfree (%)	25.7 / 29.1

The structure of Human Aldose Reductase Structure also contains other interesting chemical elements:

Bromine

(Br)

1 atom

The binding sites of Fluorine atom in the Human Aldose Reductase Structure (pdb code 2r24). 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 Structure, PDB code: 2r24:
Jump to Fluorine binding site number: 1; 2;

Fluorine binding site 1 out of 2 in the Human Aldose Reductase Structure


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 Structure within 5.0Å range: probe atom residue distance (Å) B Occ A:F317 b:18.5 occ:1.00 F9 A:LDT317 0.0 18.5 1.0 C5 A:LDT317 1.3 12.8 1.0 C2 A:LDT317 2.3 10.6 1.0 C6 A:LDT317 2.5 12.4 1.0 DD1 A:TYR48 2.6 5.6 1.0 DG13 A:VAL47 2.7 4.7 1.0 DA A:TYR48 3.1 6.1 1.0 O A:VAL47 3.1 9.2 1.0 DG22 A:VAL47 3.2 3.8 1.0 DE1 A:TRP20 3.3 4.3 1.0 DD1 A:TRP20 3.4 10.6 1.0 O A:HOH576 3.5 37.2 1.0 CD1 A:TYR48 3.5 4.0 1.0 C A:VAL47 3.6 5.5 1.0 CG1 A:VAL47 3.7 7.1 1.0 NE1 A:TRP20 3.7 6.5 1.0 C4 A:LDT317 3.7 9.6 1.0 O A:HOH344 3.7 20.0 1.0 CD1 A:TRP20 3.7 6.8 1.0 C3 A:LDT317 3.8 12.3 1.0 O A:HOH346 3.8 27.7 1.0 DE1 A:TYR48 3.9 2.0 1.0 CA A:TYR48 3.9 7.2 1.0 N A:TYR48 4.0 5.6 1.0 CG2 A:VAL47 4.0 10.0 1.0 O A:HOH345 4.0 25.2 1.0 CE1 A:TYR48 4.1 3.5 1.0 DG12 A:VAL47 4.1 9.2 1.0 DG11 A:VAL47 4.1 8.7 1.0 DG21 A:VAL47 4.2 11.2 1.0 C7 A:LDT317 4.2 10.9 1.0 CB A:VAL47 4.3 9.4 1.0 CG A:TYR48 4.5 4.0 1.0 D A:TYR48 4.6 6.8 1.0 CA A:VAL47 4.6 6.7 1.0 O A:HOH334 4.6 10.6 1.0 CE2 A:TRP20 4.7 7.2 1.0 CB A:TYR48 4.7 3.5 1.0 DG23 A:VAL47 4.8 10.5 1.0 CG A:TRP20 4.9 4.5 1.0 O15 A:LDT317 4.9 12.8 1.0 O A:HOH515 4.9 30.1 1.0 C A:TYR48 4.9 5.7 1.0

Fluorine binding site 2 out of 2 in the Human Aldose Reductase Structure


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 Structure within 5.0Å range: probe atom residue distance (Å) B Occ A:F317 b:16.9 occ:1.00 F14 A:LDT317 0.0 16.9 1.0 C27 A:LDT317 1.3 12.3 1.0 C24 A:LDT317 2.4 12.4 1.0 C28 A:LDT317 2.4 10.2 1.0 DA A:ALA299 2.5 13.1 1.0 C13 A:LDT317 2.8 14.2 1.0 DB2 A:LEU300 2.9 17.3 1.0 CA A:ALA299 3.0 18.4 1.0 C A:ALA299 3.1 23.6 1.0 DH2 A:TRP111 3.1 12.4 1.0 N A:ALA299 3.2 13.2 1.0 N A:LEU300 3.3 21.3 1.0 CH2 A:TRP111 3.3 10.9 1.0 DB3 A:LEU300 3.4 20.3 1.0 D A:LEU300 3.4 21.7 1.0 CB A:LEU300 3.5 23.2 1.0 C A:CYS298 3.6 11.4 1.0 D A:ALA299 3.6 14.5 1.0 O A:ALA299 3.6 26.2 1.0 C25 A:LDT317 3.7 10.4 1.0 CZ2 A:TRP111 3.7 8.8 1.0 C26 A:LDT317 3.8 13.3 1.0 O A:CYS298 3.8 16.8 1.0 DZ2 A:TRP111 3.8 5.7 1.0 CZ3 A:TRP111 3.9 6.2 1.0 CA A:LEU300 4.0 22.9 1.0 DE2 A:PHE311 4.0 10.8 1.0 DE1 A:TYR309 4.1 29.6 1.0 N17 A:LDT317 4.1 13.6 1.0 DZ3 A:TRP111 4.1 3.6 1.0 DG A:CYS298 4.2 19.1 1.0 DD22 A:LEU300 4.3 25.8 1.0 C29 A:LDT317 4.3 10.1 1.0 DB3 A:CYS298 4.4 21.7 1.0 CB A:ALA299 4.5 27.8 1.0 DA A:CYS298 4.5 5.6 1.0 CE2 A:TRP111 4.5 7.7 1.0 CA A:CYS298 4.6 8.7 1.0 OH A:TYR309 4.6 28.4 1.0 DA A:LEU300 4.6 27.3 1.0 DD23 A:LEU300 4.7 21.4 1.0 DB1 A:ALA299 4.7 33.4 1.0 CE3 A:TRP111 4.7 5.7 1.0 CG A:LEU300 4.8 27.7 1.0 CD2 A:LEU300 4.8 25.1 1.0 DB2 A:ALA299 4.8 27.3 1.0 CB A:CYS298 4.9 19.1 1.0 CE1 A:TYR309 4.9 23.6 1.0 CE2 A:PHE311 4.9 15.5 1.0 CD2 A:TRP111 5.0 5.4 1.0 SG A:CYS298 5.0 21.1 1.0

M.P.Blakeley, F.Ruiz, R.Cachau, I.Hazemann, F.Meilleur, A.Mitschler, S.Ginell, P.Afonine, O.N.Ventura, A.Cousido-Siah, M.Haertlein, A.Joachimiak, D.Myles, A.Podjarny. Quantum Model of Catalysis Based on Mobile Proton Revealed By Subatomic X-Ray and Neutron Diffraction Studies of H-Aldose Reductase Proc.Natl.Acad.Sci.Usa V. 105 1844 2008.
ISSN: ISSN 0027-8424
PubMed: 18250329
DOI: 10.1073/PNAS.0711659105