Atomistry » Fluorine » PDB 16pk-1bw7 » 1ah3
Atomistry »
  Fluorine »
    PDB 16pk-1bw7 »
      1ah3 »

Fluorine in PDB 1ah3: Aldose Reductase Complexed with Tolrestat Inhibitor

Enzymatic activity of Aldose Reductase Complexed with Tolrestat Inhibitor

All present enzymatic activity of Aldose Reductase Complexed with Tolrestat Inhibitor:
1.1.1.21;

Protein crystallography data

The structure of Aldose Reductase Complexed with Tolrestat Inhibitor, PDB code: 1ah3 was solved by D.Moras, A.Podjarny, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 6.00 / 2.30
Space group P 43 21 2
Cell size a, b, c (Å), α, β, γ (°) 68.420, 68.420, 153.560, 90.00, 90.00, 90.00
R / Rfree (%) 20.7 / 29

Fluorine Binding Sites:

The binding sites of Fluorine atom in the Aldose Reductase Complexed with Tolrestat Inhibitor (pdb code 1ah3). This binding sites where shown within 5.0 Angstroms radius around Fluorine atom.
In total 3 binding sites of Fluorine where determined in the Aldose Reductase Complexed with Tolrestat Inhibitor, PDB code: 1ah3:
Jump to Fluorine binding site number: 1; 2; 3;

Fluorine binding site 1 out of 3 in 1ah3

Go back to Fluorine Binding Sites List in 1ah3
Fluorine binding site 1 out of 3 in the Aldose Reductase Complexed with Tolrestat Inhibitor


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 1 of Aldose Reductase Complexed with Tolrestat Inhibitor within 5.0Å range:
probe atom residue distance (Å) B Occ
A:F320

b:37.5
occ:1.00
F1 A:TOL320 0.0 37.5 1.0
C1 A:TOL320 1.4 34.7 1.0
F2 A:TOL320 2.2 34.4 1.0
F3 A:TOL320 2.2 47.2 1.0
HG A:SER302 2.3 20.0 1.0
C2 A:TOL320 2.4 39.5 1.0
OG A:SER302 2.7 58.1 1.0
C11 A:TOL320 2.8 35.6 1.0
C12 A:TOL320 2.9 37.5 1.0
CD1 A:LEU300 3.2 54.3 1.0
CG A:LEU300 3.5 58.0 1.0
C3 A:TOL320 3.6 37.2 1.0
CB A:LEU300 3.8 53.6 1.0
CB A:SER302 3.8 43.5 1.0
O1 A:TOL320 3.9 37.6 1.0
O A:HOH467 4.0 64.5 1.0
C10 A:TOL320 4.1 29.6 1.0
H A:SER302 4.1 20.0 1.0
C7 A:TOL320 4.3 39.5 1.0
CA A:LEU300 4.4 55.9 1.0
H A:CYS303 4.6 20.0 1.0
C5 A:TOL320 4.7 39.0 1.0
O A:LEU300 4.7 47.8 1.0
C A:LEU300 4.7 52.6 1.0
N A:SER302 4.8 50.1 1.0
CA A:SER302 4.8 45.8 1.0
N A:CYS303 5.0 44.2 1.0
CD2 A:LEU300 5.0 61.3 1.0
C6 A:TOL320 5.0 40.2 1.0

Fluorine binding site 2 out of 3 in 1ah3

Go back to Fluorine Binding Sites List in 1ah3
Fluorine binding site 2 out of 3 in the Aldose Reductase Complexed with Tolrestat Inhibitor


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 2 of Aldose Reductase Complexed with Tolrestat Inhibitor within 5.0Å range:
probe atom residue distance (Å) B Occ
A:F320

b:34.4
occ:1.00
F2 A:TOL320 0.0 34.4 1.0
C1 A:TOL320 1.4 34.7 1.0
F1 A:TOL320 2.2 37.5 1.0
F3 A:TOL320 2.2 47.2 1.0
C2 A:TOL320 2.4 39.5 1.0
O1 A:TOL320 2.5 37.6 1.0
C3 A:TOL320 2.8 37.2 1.0
HG A:SER302 3.5 20.0 1.0
CB A:CYS303 3.6 37.6 1.0
OG A:SER302 3.6 58.1 1.0
CG2 A:VAL130 3.7 44.3 1.0
C12 A:TOL320 3.7 37.5 1.0
C4 A:TOL320 3.9 32.5 1.0
CZ A:PHE115 3.9 17.9 1.0
N A:CYS303 4.1 44.2 1.0
H A:CYS303 4.1 20.0 1.0
CB A:SER302 4.2 43.5 1.0
C11 A:TOL320 4.2 35.6 1.0
C5 A:TOL320 4.3 39.0 1.0
CB A:LEU300 4.3 53.6 1.0
CA A:CYS303 4.4 42.4 1.0
C A:SER302 4.4 44.1 1.0
SG A:CYS303 4.4 60.1 1.0
CG A:LEU300 4.5 58.0 1.0
CE2 A:PHE115 4.6 19.3 1.0
O A:LEU300 4.7 47.8 1.0
CB A:VAL130 4.7 44.4 1.0
CA A:SER302 4.8 45.8 1.0
O A:SER302 4.8 40.4 1.0
CD1 A:PHE122 4.9 28.3 1.0
C7 A:TOL320 4.9 39.5 1.0
CE1 A:PHE115 4.9 13.3 1.0
CD1 A:LEU300 4.9 54.3 1.0
H A:SER302 4.9 20.0 1.0

Fluorine binding site 3 out of 3 in 1ah3

Go back to Fluorine Binding Sites List in 1ah3
Fluorine binding site 3 out of 3 in the Aldose Reductase Complexed with Tolrestat Inhibitor


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 3 of Aldose Reductase Complexed with Tolrestat Inhibitor within 5.0Å range:
probe atom residue distance (Å) B Occ
A:F320

b:47.2
occ:1.00
F3 A:TOL320 0.0 47.2 1.0
C1 A:TOL320 1.4 34.7 1.0
F2 A:TOL320 2.2 34.4 1.0
F1 A:TOL320 2.2 37.5 1.0
C2 A:TOL320 2.4 39.5 1.0
C11 A:TOL320 2.9 35.6 1.0
C12 A:TOL320 3.0 37.5 1.0
CD1 A:PHE122 3.2 28.3 1.0
O A:HOH467 3.4 64.5 1.0
CE1 A:PHE122 3.4 39.2 1.0
HG A:SER302 3.5 20.0 1.0
C3 A:TOL320 3.5 37.2 1.0
O1 A:TOL320 3.9 37.6 1.0
CG2 A:VAL130 4.0 44.3 1.0
OG A:SER302 4.1 58.1 1.0
CG A:PHE122 4.2 31.9 1.0
C10 A:TOL320 4.2 29.6 1.0
C7 A:TOL320 4.3 39.5 1.0
CZ A:PHE122 4.5 38.3 1.0
C5 A:TOL320 4.7 39.0 1.0
CB A:SER302 4.7 43.5 1.0
CB A:PHE122 4.7 34.9 1.0
O A:HOH605 4.7 41.5 1.0
CZ A:PHE115 4.7 17.9 1.0
CE2 A:PHE115 4.7 19.3 1.0
C6 A:TOL320 5.0 40.2 1.0

Reference:

A.Urzhumtsev, F.Tete-Favier, A.Mitschler, J.Barbanton, P.Barth, L.Urzhumtseva, J.F.Biellmann, A.Podjarny, D.Moras. A 'Specificity' Pocket Inferred From the Crystal Structures of the Complexes of Aldose Reductase with the Pharmaceutically Important Inhibitors Tolrestat and Sorbinil. Structure V. 5 601 1997.
ISSN: ISSN 0969-2126
PubMed: 9195881
DOI: 10.1016/S0969-2126(97)00216-5
Page generated: Sun Dec 13 11:28:10 2020

Last articles

Zn in 7VD8
Zn in 7V1R
Zn in 7V1Q
Zn in 7VPF
Zn in 7T85
Zn in 7T5F
Zn in 7NF9
Zn in 7M4M
Zn in 7M4O
Zn in 7M4N
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy