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Fluorine in PDB 2pdx: Human Aldose Reductase Double Mutant S302R-C303D Complexed with Zopolrestat.

Enzymatic activity of Human Aldose Reductase Double Mutant S302R-C303D Complexed with Zopolrestat.

All present enzymatic activity of Human Aldose Reductase Double Mutant S302R-C303D Complexed with Zopolrestat.:
1.1.1.21;

Protein crystallography data

The structure of Human Aldose Reductase Double Mutant S302R-C303D Complexed with Zopolrestat., PDB code: 2pdx was solved by H.Steuber, A.Heine, G.Klebe, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 30.00 / 1.65
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 49.290, 67.260, 47.800, 90.00, 91.40, 90.00
R / Rfree (%) 17.4 / 23.2

Fluorine Binding Sites:

The binding sites of Fluorine atom in the Human Aldose Reductase Double Mutant S302R-C303D Complexed with Zopolrestat. (pdb code 2pdx). 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 Double Mutant S302R-C303D Complexed with Zopolrestat., PDB code: 2pdx:
Jump to Fluorine binding site number: 1; 2; 3;

Fluorine binding site 1 out of 3 in 2pdx

Go back to Fluorine Binding Sites List in 2pdx
Fluorine binding site 1 out of 3 in the Human Aldose Reductase Double Mutant S302R-C303D Complexed with Zopolrestat.


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 Double Mutant S302R-C303D Complexed with Zopolrestat. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:F600

b:23.6
occ:1.00
F1 A:ZST600 0.0 23.6 1.0
C19 A:ZST600 1.3 27.7 1.0
F3 A:ZST600 2.1 35.6 1.0
F2 A:ZST600 2.2 22.8 1.0
C15 A:ZST600 2.3 10.9 1.0
C14 A:ZST600 3.0 10.8 1.0
C16 A:ZST600 3.2 18.8 1.0
CG2 A:THR113 3.5 12.8 1.0
CD A:PRO310 3.6 13.9 1.0
OG1 A:THR113 3.7 11.3 1.0
CD1 A:TYR309 3.7 16.6 1.0
CE3 A:TRP111 4.1 7.0 1.0
CB A:THR113 4.2 7.0 1.0
C13 A:ZST600 4.2 9.4 1.0
CA A:TYR309 4.3 13.0 1.0
CE1 A:TYR309 4.3 17.4 1.0
CZ3 A:TRP111 4.4 9.9 1.0
C12 A:ZST600 4.4 9.8 1.0
CG A:PRO310 4.6 23.6 1.0
CG A:TYR309 4.6 17.5 1.0
N A:PRO310 4.7 12.6 1.0
CB A:TYR309 4.8 19.4 1.0
C11 A:ZST600 4.8 14.4 1.0
CD2 A:TRP111 4.9 7.5 1.0
CG2 A:THR304 4.9 20.0 1.0

Fluorine binding site 2 out of 3 in 2pdx

Go back to Fluorine Binding Sites List in 2pdx
Fluorine binding site 2 out of 3 in the Human Aldose Reductase Double Mutant S302R-C303D Complexed with Zopolrestat.


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 Double Mutant S302R-C303D Complexed with Zopolrestat. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:F600

b:22.8
occ:1.00
F2 A:ZST600 0.0 22.8 1.0
C19 A:ZST600 1.3 27.7 1.0
F3 A:ZST600 2.0 35.6 1.0
F1 A:ZST600 2.2 23.6 1.0
C15 A:ZST600 2.4 10.9 1.0
C14 A:ZST600 2.8 10.8 1.0
OG1 A:THR113 3.4 11.3 1.0
C16 A:ZST600 3.5 18.8 1.0
CD1 A:LEU301 3.5 51.2 1.0
CG2 A:THR113 3.6 12.8 1.0
CB A:THR113 3.8 7.0 1.0
CZ A:PHE115 3.8 11.1 1.0
CE1 A:PHE115 3.9 6.2 1.0
C13 A:ZST600 4.1 9.4 1.0
CG2 A:THR304 4.2 20.0 1.0
CB A:LEU301 4.3 35.6 1.0
CG A:LEU301 4.4 47.1 1.0
CB A:HIS306 4.6 12.0 1.0
C12 A:ZST600 4.7 9.8 1.0
CD1 A:TYR309 4.7 16.6 1.0
C11 A:ZST600 4.9 14.4 1.0
CG A:HIS306 4.9 15.3 1.0
OG1 A:THR304 4.9 17.2 1.0
CB A:THR304 4.9 21.2 1.0

Fluorine binding site 3 out of 3 in 2pdx

Go back to Fluorine Binding Sites List in 2pdx
Fluorine binding site 3 out of 3 in the Human Aldose Reductase Double Mutant S302R-C303D Complexed with Zopolrestat.


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 Double Mutant S302R-C303D Complexed with Zopolrestat. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:F600

b:35.6
occ:1.00
F3 A:ZST600 0.0 35.6 1.0
C19 A:ZST600 1.3 27.7 1.0
F2 A:ZST600 2.0 22.8 1.0
F1 A:ZST600 2.1 23.6 1.0
C15 A:ZST600 2.4 10.9 1.0
C16 A:ZST600 2.8 18.8 1.0
CB A:LEU301 3.2 35.6 1.0
CD1 A:TYR309 3.3 16.6 1.0
CG2 A:THR304 3.5 20.0 1.0
C14 A:ZST600 3.6 10.8 1.0
CE1 A:TYR309 3.6 17.4 1.0
CD1 A:LEU301 3.7 51.2 1.0
O A:LEU301 3.8 27.1 1.0
CG A:LEU301 3.9 47.1 1.0
O A:LEU300 3.9 29.4 1.0
C12 A:ZST600 4.2 9.8 1.0
C A:LEU301 4.3 22.4 1.0
CB A:THR304 4.3 21.2 1.0
CA A:LEU301 4.4 35.2 1.0
CG A:TYR309 4.5 17.5 1.0
C13 A:ZST600 4.7 9.4 1.0
C A:LEU300 4.8 20.8 1.0
CG2 A:THR113 4.9 12.8 1.0
CB A:TYR309 4.9 19.4 1.0
OG1 A:THR304 4.9 17.2 1.0
C11 A:ZST600 5.0 14.4 1.0
CZ A:TYR309 5.0 13.8 1.0

Reference:

H.Steuber, A.Heine, A.Podjarny, G.Klebe. Merging the Binding Sites of Aldose and Aldehyde Reductase For Detection of Inhibitor Selectivity-Determining Features. J.Mol.Biol. V. 379 991 2008.
ISSN: ISSN 0022-2836
PubMed: 18495158
DOI: 10.1016/J.JMB.2008.03.063
Page generated: Sun Dec 13 11:38:58 2020

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