Atomistry » Fluorine » PDB 3l8v-3lxp » 3lqg
Atomistry »
  Fluorine »
    PDB 3l8v-3lxp »
      3lqg »

Fluorine in PDB 3lqg: Human Aldose Reductase Mutant T113A Complexed with IDD388

Enzymatic activity of Human Aldose Reductase Mutant T113A Complexed with IDD388

All present enzymatic activity of Human Aldose Reductase Mutant T113A Complexed with IDD388:
1.1.1.21;

Protein crystallography data

The structure of Human Aldose Reductase Mutant T113A Complexed with IDD388, PDB code: 3lqg 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 / 1.35
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 49.060, 66.690, 47.130, 90.00, 92.38, 90.00
R / Rfree (%) 11.6 / 16.1

Other elements in 3lqg:

The structure of Human Aldose Reductase Mutant T113A Complexed with IDD388 also contains other interesting chemical elements:

Bromine (Br) 2 atoms
Chlorine (Cl) 1 atom

Fluorine Binding Sites:

The binding sites of Fluorine atom in the Human Aldose Reductase Mutant T113A Complexed with IDD388 (pdb code 3lqg). 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 T113A Complexed with IDD388, PDB code: 3lqg:

Fluorine binding site 1 out of 1 in 3lqg

Go back to Fluorine Binding Sites List in 3lqg
Fluorine binding site 1 out of 1 in the Human Aldose Reductase Mutant T113A Complexed with IDD388


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 T113A Complexed with IDD388 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:F600

b:9.7
occ:1.00
F9 A:388600 0.0 9.7 1.0
C7 A:388600 1.3 8.5 1.0
C6 A:388600 2.4 9.8 1.0
C2 A:388600 2.4 7.4 1.0
C1 A:388600 2.8 8.3 1.0
C A:ALA299 3.2 11.2 1.0
CA A:ALA299 3.2 10.5 1.0
N A:LEU300 3.3 9.3 1.0
CH2 A:TRP111 3.3 6.6 1.0
CB A:LEU300 3.5 9.9 1.0
CZ3 A:TRP111 3.6 6.8 1.0
C3 A:388600 3.6 6.9 1.0
C5 A:388600 3.6 8.8 1.0
N A:ALA299 3.7 10.3 1.0
CZ2 A:TRP111 3.9 6.8 1.0
O A:ALA299 3.9 12.6 1.0
CA A:LEU300 4.0 9.9 1.0
CE1 A:TYR309 4.1 9.8 1.0
C4 A:388600 4.1 7.1 1.0
OH A:TYR309 4.2 10.7 1.0
C A:CYS298 4.2 10.5 1.0
N10 A:388600 4.2 7.6 1.0
O A:CYS298 4.2 12.3 1.0
CE2 A:PHE311 4.4 10.8 1.0
CE3 A:TRP111 4.4 6.1 1.0
CE2 A:TRP111 4.6 6.8 1.0
CB A:ALA299 4.6 12.6 1.0
CZ A:TYR309 4.6 10.5 1.0
CD2 A:TRP111 4.8 6.0 1.0
CG A:LEU300 4.8 10.8 1.0
CD2 A:PHE311 4.9 11.2 1.0
O A:LEU300 4.9 11.5 1.0
C A:LEU300 5.0 9.6 1.0
CD2 A:LEU300 5.0 12.4 1.0
SG A:CYS298 5.0 8.6 0.7

Reference:

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
Page generated: Wed Jul 31 20:34:37 2024

Last articles

Zn in 9JYW
Zn in 9IR4
Zn in 9IR3
Zn in 9GMX
Zn in 9GMW
Zn in 9JEJ
Zn in 9ERF
Zn in 9ERE
Zn in 9EGV
Zn in 9EGW
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy