Fluorine in PDB 6xum: Human Aldose Reductase Mutant L300/301A in Complex with A Ligand with An Idd Structure ({5-Fluoro-2-[(3-Nitrobenzyl) Carbamoyl]Phenoxy}Acetic Acid)

Enzymatic activity of Human Aldose Reductase Mutant L300/301A in Complex with A Ligand with An Idd Structure ({5-Fluoro-2-[(3-Nitrobenzyl) Carbamoyl]Phenoxy}Acetic Acid)

All present enzymatic activity of Human Aldose Reductase Mutant L300/301A in Complex with A Ligand with An Idd Structure ({5-Fluoro-2-[(3-Nitrobenzyl) Carbamoyl]Phenoxy}Acetic Acid):
1.1.1.21; 1.1.1.300; 1.1.1.372; 1.1.1.54;

Protein crystallography data

The structure of Human Aldose Reductase Mutant L300/301A in Complex with A Ligand with An Idd Structure ({5-Fluoro-2-[(3-Nitrobenzyl) Carbamoyl]Phenoxy}Acetic Acid), PDB code: 6xum was solved by L.-S.Hubert, M.Ley, A.Heine, G.Klebe, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 38.56 / 0.97
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 47.288, 66.739, 49.378, 90, 92.22, 90
R / Rfree (%) 11.9 / 12.8

Fluorine Binding Sites:

The binding sites of Fluorine atom in the Human Aldose Reductase Mutant L300/301A in Complex with A Ligand with An Idd Structure ({5-Fluoro-2-[(3-Nitrobenzyl) Carbamoyl]Phenoxy}Acetic Acid) (pdb code 6xum). 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 L300/301A in Complex with A Ligand with An Idd Structure ({5-Fluoro-2-[(3-Nitrobenzyl) Carbamoyl]Phenoxy}Acetic Acid), PDB code: 6xum:

Fluorine binding site 1 out of 1 in 6xum

Go back to Fluorine Binding Sites List in 6xum
Fluorine binding site 1 out of 1 in the Human Aldose Reductase Mutant L300/301A in Complex with A Ligand with An Idd Structure ({5-Fluoro-2-[(3-Nitrobenzyl) Carbamoyl]Phenoxy}Acetic Acid)


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 L300/301A in Complex with A Ligand with An Idd Structure ({5-Fluoro-2-[(3-Nitrobenzyl) Carbamoyl]Phenoxy}Acetic Acid) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:F401

b:10.5
occ:0.95
 F27 A:30L401 0.0 10.5 0.9
C26 A:30L401 1.4 9.7 0.9
C24 A:30L401 2.3 11.7 0.9
C28 A:30L401 2.3 8.1 0.9
HG13 A:VAL47 2.7 7.1 1.0
HD1 A:TYR48 2.7 6.5 1.0
HA A:TYR48 3.1 6.7 1.0
O A:VAL47 3.2 6.4 1.0
HG22 A:VAL47 3.3 8.1 1.0
HE1 A:TRP20 3.3 8.0 1.0
O A:HOH828 3.5 13.5 1.0
O A:HOH683 3.5 18.2 1.0
HD1 A:TRP20 3.5 7.5 1.0
C30 A:30L401 3.6 8.1 0.9
C22 A:30L401 3.6 12.0 0.9
CD1 A:TYR48 3.6 5.4 1.0
NE1 A:TRP20 3.7 6.7 1.0
O A:HOH554 3.7 9.6 1.0
CG1 A:VAL47 3.7 5.9 1.0
C A:VAL47 3.7 5.7 1.0
CD1 A:TRP20 3.8 6.3 1.0
HE1 A:TYR48 3.9 6.6 1.0
CA A:TYR48 4.0 5.6 1.0
CG2 A:VAL47 4.1 6.8 1.0
N A:TYR48 4.1 5.4 1.0
HG11 A:VAL47 4.1 7.1 1.0
C21 A:30L401 4.1 10.4 0.9
O A:HOH781 4.2 18.4 0.5
CE1 A:TYR48 4.2 5.5 1.0
HG12 A:VAL47 4.2 7.1 1.0
CB A:VAL47 4.3 6.0 1.0
HG21 A:VAL47 4.3 8.1 1.0
CA A:VAL47 4.6 5.9 1.0
CG A:TYR48 4.6 5.4 1.0
H A:TYR48 4.7 6.4 1.0
CE2 A:TRP20 4.7 6.8 1.0
O31 A:30L401 4.7 7.2 0.9
O A:HOH631 4.7 9.7 1.0
O A:HOH859 4.8 11.9 1.0
HG23 A:VAL47 4.8 8.1 1.0
CB A:TYR48 4.8 5.6 1.0
CG A:TRP20 4.9 6.1 1.0
C A:TYR48 5.0 5.8 1.0
C32 A:30L401 5.0 7.1 0.9

Reference:

L.-S.Hubert, M.Ley, F.Scheer, W.Diederich, A.Heine, G.Klebe. Human Aldose Reductase Mutant L300/301A in Complex with A Ligand with An Idd Structure ({5-Fluoro-2-[(3-Nitrobenzyl)Carbamoyl]Phenoxy}Acetic Acid) To Be Published.
Page generated: Wed Mar 3 13:28:44 2021

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