Fluorine in PDB 3lbo: Human Aldose Reductase Mutant T113C Complexed with IDD594

All present enzymatic activity of Human Aldose Reductase Mutant T113C Complexed with IDD594:
1.1.1.21;

The structure of Human Aldose Reductase Mutant T113C Complexed with IDD594, PDB code: 3lbo was solved by C.Koch, A.Heine, G.Klebe, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	10.00 / 1.10
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	49.180, 66.700, 47.240, 90.00, 92.40, 90.00
R / Rfree (%)	11.3 / 14.4

The structure of Human Aldose Reductase Mutant T113C Complexed with IDD594 also contains other interesting chemical elements:

Bromine

(Br)

2 atoms

The binding sites of Fluorine atom in the Human Aldose Reductase Mutant T113C Complexed with IDD594 (pdb code 3lbo). 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 Mutant T113C Complexed with IDD594, PDB code: 3lbo:
Jump to Fluorine binding site number: 1; 2;

Fluorine binding site 1 out of 2 in the Human Aldose Reductase Mutant T113C Complexed with IDD594


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 T113C Complexed with IDD594 within 5.0Å range: probe atom residue distance (Å) B Occ A:F600 b:9.1 occ:1.00 F9 A:LDT600 0.0 9.1 1.0 C5 A:LDT600 1.4 7.2 1.0 C2 A:LDT600 2.3 6.6 1.0 C6 A:LDT600 2.4 7.8 1.0 O A:VAL47 3.1 5.0 1.0 C4 A:LDT600 3.6 6.7 1.0 O A:HOH1009 3.6 7.9 1.0 C3 A:LDT600 3.6 7.5 1.0 CD1 A:TYR48 3.6 4.9 1.0 O A:HOH1058 3.6 12.9 1.0 C A:VAL47 3.7 4.7 1.0 CG1 A:VAL47 3.7 5.6 1.0 NE1 A:TRP20 3.7 5.9 1.0 CD1 A:TRP20 3.9 5.6 1.0 CA A:TYR48 4.0 4.9 1.0 CG2 A:VAL47 4.0 5.6 1.0 N A:TYR48 4.0 4.6 1.0 C7 A:LDT600 4.1 7.3 1.0 CE1 A:TYR48 4.2 5.0 1.0 CB A:VAL47 4.3 5.2 1.0 CA A:VAL47 4.6 4.8 1.0 CG A:TYR48 4.7 4.3 1.0 O A:HOH1104 4.7 10.3 1.0 O15 A:LDT600 4.8 6.3 1.0 CE2 A:TRP20 4.8 6.0 1.0 CB A:TYR48 4.8 4.8 1.0 O A:HOH1032 4.8 7.9 1.0 C A:TYR48 4.9 4.7 1.0 CG A:TRP20 5.0 5.1 1.0

Fluorine binding site 2 out of 2 in the Human Aldose Reductase Mutant T113C Complexed with IDD594


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 T113C Complexed with IDD594 within 5.0Å range: probe atom residue distance (Å) B Occ A:F600 b:9.2 occ:1.00 F14 A:LDT600 0.0 9.2 1.0 C27 A:LDT600 1.3 7.3 1.0 C28 A:LDT600 2.3 7.7 1.0 C24 A:LDT600 2.4 7.0 1.0 C13 A:LDT600 2.8 7.7 1.0 C A:ALA299 3.1 10.1 1.0 CA A:ALA299 3.1 9.2 1.0 CH2 A:TRP111 3.3 7.4 1.0 N A:LEU300 3.3 8.7 1.0 N A:ALA299 3.4 8.4 1.0 CB A:LEU300 3.5 9.4 1.0 C26 A:LDT600 3.6 7.2 1.0 C25 A:LDT600 3.6 7.9 1.0 O A:ALA299 3.7 11.5 1.0 CZ3 A:TRP111 3.7 7.2 1.0 CZ2 A:TRP111 3.7 7.2 1.0 C A:CYS298 3.9 8.2 0.5 C A:CYS298 3.9 7.3 0.5 O A:CYS298 4.0 9.3 0.5 CA A:LEU300 4.0 8.4 1.0 C29 A:LDT600 4.1 7.1 1.0 O A:CYS298 4.1 8.3 0.5 N17 A:LDT600 4.2 8.4 1.0 OH A:TYR309 4.3 9.8 1.0 CE2 A:TRP111 4.5 6.7 1.0 CE3 A:TRP111 4.5 6.2 1.0 CE1 A:TYR309 4.5 8.6 1.0 CB A:ALA299 4.5 11.8 1.0 CE2 A:PHE311 4.6 9.7 1.0 SG A:CYS298 4.7 7.4 0.5 CA A:CYS298 4.8 7.2 0.5 CB A:CYS298 4.8 9.6 0.5 CD2 A:TRP111 4.8 5.3 1.0 CG A:LEU300 4.8 11.3 1.0 CZ A:TYR309 4.9 9.6 1.0 CD2 A:LEU300 4.9 12.2 1.0 CA A:CYS298 5.0 7.9 0.5

C.Koch, A.Heine, G.Klebe. Tracing the Detail: How Mutations Affect Binding Modes and Thermodynamic Signatures of Closely Related Aldose Reductase Inhibitors J.Mol.Biol. V. 406 700 2011.
ISSN: ISSN 0022-2836
PubMed: 21185307
DOI: 10.1016/J.JMB.2010.11.058