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Fluorine in PDB 2fzd: Human Aldose Reductase Complexed with Tolrestat at 1.08 A Resolution.

Enzymatic activity of Human Aldose Reductase Complexed with Tolrestat at 1.08 A Resolution.

All present enzymatic activity of Human Aldose Reductase Complexed with Tolrestat at 1.08 A Resolution.:
1.1.1.21;

Protein crystallography data

The structure of Human Aldose Reductase Complexed with Tolrestat at 1.08 A Resolution., PDB code: 2fzd was solved by H.Steuber, M.Zentgraf, C.Gerlach, C.A.Sotriffer, 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 / 1.08
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 49.450, 66.679, 46.060, 90.00, 92.45, 90.00
R / Rfree (%) 11 / 13.7

Fluorine Binding Sites:

The binding sites of Fluorine atom in the Human Aldose Reductase Complexed with Tolrestat at 1.08 A Resolution. (pdb code 2fzd). This binding sites where shown within 5.0 Angstroms radius around Fluorine atom.
In total 3 binding sites of Fluorine where determined in the Human Aldose Reductase Complexed with Tolrestat at 1.08 A Resolution., PDB code: 2fzd:
Jump to Fluorine binding site number: 1; 2; 3;

Fluorine binding site 1 out of 3 in 2fzd

Go back to Fluorine Binding Sites List in 2fzd
Fluorine binding site 1 out of 3 in the Human Aldose Reductase Complexed with Tolrestat at 1.08 A Resolution.


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 Complexed with Tolrestat at 1.08 A Resolution. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:F317

b:15.9
occ:1.00
F1 A:TOL317 0.0 15.9 1.0
C1 A:TOL317 1.3 9.1 1.0
F2 A:TOL317 2.1 16.7 1.0
F3 A:TOL317 2.1 17.4 1.0
C2 A:TOL317 2.3 7.6 1.0
C12 A:TOL317 2.9 7.6 1.0
C11 A:TOL317 2.9 9.2 1.0
OG A:SER302 2.9 34.3 1.0
O A:HOH635 3.0 31.4 1.0
C3 A:TOL317 3.4 7.2 1.0
O A:HOH657 3.6 33.8 1.0
O A:HOH618 3.7 33.7 1.0
CB A:LEU300 3.7 17.0 1.0
O1 A:TOL317 3.7 8.4 1.0
CD2 A:LEU300 4.0 25.5 1.0
CG A:LEU300 4.2 19.0 1.0
C10 A:TOL317 4.2 9.1 1.0
CB A:SER302 4.2 41.0 1.0
C7 A:TOL317 4.2 6.4 1.0
CD1 A:LEU300 4.3 22.2 1.0
CA A:LEU300 4.3 16.7 1.0
O A:HOH487 4.4 15.5 1.0
O A:HOH592 4.4 23.5 1.0
CB A:CYS303 4.6 23.5 1.0
C5 A:TOL317 4.6 6.6 1.0
O A:LEU300 4.7 23.8 1.0
N A:CYS303 4.7 26.3 1.0
C A:LEU300 4.7 20.8 1.0
C A:SER302 4.9 31.5 1.0
C6 A:TOL317 4.9 6.0 1.0
CA A:SER302 4.9 36.7 1.0
N A:SER302 4.9 31.9 1.0

Fluorine binding site 2 out of 3 in 2fzd

Go back to Fluorine Binding Sites List in 2fzd
Fluorine binding site 2 out of 3 in the Human Aldose Reductase Complexed with Tolrestat at 1.08 A Resolution.


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 Complexed with Tolrestat at 1.08 A Resolution. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:F317

b:16.7
occ:1.00
F2 A:TOL317 0.0 16.7 1.0
C1 A:TOL317 1.3 9.1 1.0
F3 A:TOL317 2.1 17.4 1.0
F1 A:TOL317 2.1 15.9 1.0
C2 A:TOL317 2.3 7.6 1.0
O1 A:TOL317 2.4 8.4 1.0
C3 A:TOL317 2.8 7.2 1.0
CB A:CYS303 3.6 23.5 1.0
CG1 A:VAL130 3.6 20.4 1.0
OG A:SER302 3.6 34.3 1.0
C12 A:TOL317 3.6 7.6 1.0
C4 A:TOL317 3.7 10.3 1.0
CZ A:PHE115 3.8 9.5 1.0
SG A:CYS303 3.9 26.1 1.0
C5 A:TOL317 4.2 6.6 1.0
C11 A:TOL317 4.2 9.2 1.0
CE2 A:PHE115 4.4 8.7 1.0
CA A:CYS303 4.4 23.0 1.0
N A:CYS303 4.5 26.3 1.0
O A:HOH618 4.5 33.7 1.0
CB A:LEU300 4.6 17.0 1.0
CE1 A:PHE115 4.7 10.0 1.0
C7 A:TOL317 4.8 6.4 1.0
C A:SER302 4.8 31.5 1.0
O A:HOH635 4.8 31.4 1.0
CD1 A:LEU300 4.9 22.2 1.0
CB A:VAL130 4.9 16.5 1.0
C6 A:TOL317 4.9 6.0 1.0

Fluorine binding site 3 out of 3 in 2fzd

Go back to Fluorine Binding Sites List in 2fzd
Fluorine binding site 3 out of 3 in the Human Aldose Reductase Complexed with Tolrestat at 1.08 A Resolution.


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 3 of Human Aldose Reductase Complexed with Tolrestat at 1.08 A Resolution. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:F317

b:17.4
occ:1.00
F3 A:TOL317 0.0 17.4 1.0
C1 A:TOL317 1.3 9.1 1.0
F2 A:TOL317 2.1 16.7 1.0
F1 A:TOL317 2.1 15.9 1.0
C2 A:TOL317 2.4 7.6 1.0
C12 A:TOL317 2.9 7.6 1.0
C11 A:TOL317 2.9 9.2 1.0
O A:HOH487 3.2 15.5 1.0
O A:HOH618 3.2 33.7 1.0
CD1 A:PHE122 3.4 9.4 1.0
C3 A:TOL317 3.5 7.2 1.0
OG A:SER302 3.7 34.3 1.0
O1 A:TOL317 3.8 8.4 1.0
CE1 A:PHE122 4.0 9.3 1.0
C10 A:TOL317 4.2 9.1 1.0
C7 A:TOL317 4.2 6.4 1.0
CG1 A:VAL130 4.3 20.4 1.0
CG A:PHE122 4.4 7.2 1.0
O A:HOH592 4.6 23.5 1.0
C5 A:TOL317 4.6 6.6 1.0
CB A:PHE122 4.6 8.9 1.0
CE2 A:PHE115 4.7 8.7 1.0
CZ A:PHE115 4.7 9.5 1.0
O A:HOH635 4.8 31.4 1.0
O A:HOH657 4.9 33.8 1.0
C6 A:TOL317 4.9 6.0 1.0

Reference:

H.Steuber, M.Zentgraf, C.Gerlach, C.A.Sotriffer, A.Heine, G.Klebe. Expect the Unexpected or Caveat For Drug Designers: Multiple Structure Determinations Using Aldose Reductase Crystals Treated Under Varying Soaking and Co-Crystallisation Conditions. J.Mol.Biol. V. 363 174 2006.
ISSN: ISSN 0022-2836
PubMed: 16952371
DOI: 10.1016/J.JMB.2006.08.011
Page generated: Sun Dec 13 11:36:17 2020

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