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Fluorine in PDB 3ilu: Crystal Structure of the Ampa Subunit GLUR2 Bound to the Allosteric Modulator, Hydroflumethiazide

Protein crystallography data

The structure of Crystal Structure of the Ampa Subunit GLUR2 Bound to the Allosteric Modulator, Hydroflumethiazide, PDB code: 3ilu was solved by A.H.Ahmed, C.P.Ptak, R.E.Oswald, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 23.64 / 2.00
Space group P 2 21 21
Cell size a, b, c (Å), α, β, γ (°) 47.289, 114.194, 163.732, 90.00, 90.00, 90.00
R / Rfree (%) 18.8 / 22.6

Other elements in 3ilu:

The structure of Crystal Structure of the Ampa Subunit GLUR2 Bound to the Allosteric Modulator, Hydroflumethiazide also contains other interesting chemical elements:

Zinc (Zn) 5 atoms

Fluorine Binding Sites:

The binding sites of Fluorine atom in the Crystal Structure of the Ampa Subunit GLUR2 Bound to the Allosteric Modulator, Hydroflumethiazide (pdb code 3ilu). This binding sites where shown within 5.0 Angstroms radius around Fluorine atom.
In total 9 binding sites of Fluorine where determined in the Crystal Structure of the Ampa Subunit GLUR2 Bound to the Allosteric Modulator, Hydroflumethiazide, PDB code: 3ilu:
Jump to Fluorine binding site number: 1; 2; 3; 4; 5; 6; 7; 8; 9;

Fluorine binding site 1 out of 9 in 3ilu

Go back to Fluorine Binding Sites List in 3ilu
Fluorine binding site 1 out of 9 in the Crystal Structure of the Ampa Subunit GLUR2 Bound to the Allosteric Modulator, Hydroflumethiazide


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 1 of Crystal Structure of the Ampa Subunit GLUR2 Bound to the Allosteric Modulator, Hydroflumethiazide within 5.0Å range:
probe atom residue distance (Å) B Occ
B:F800

b:20.0
occ:0.50
 F12 B:HFZ800 0.0 20.0 0.5
C11 B:HFZ800 1.4 20.0 0.5
F13 B:HFZ800 2.2 20.0 0.5
F14 B:HFZ800 2.2 20.0 0.5
C10 B:HFZ800 2.4 20.0 0.5
C09 B:HFZ800 2.7 20.0 0.5
O B:HOH379 3.1 30.7 1.0
O B:HOH398 3.3 35.8 1.0
O B:HOH533 3.3 35.3 1.0
O B:HOH269 3.4 27.4 1.0
C05 B:HFZ800 3.7 20.0 0.5
O B:PHE106 3.8 22.6 1.0
CB E:SER217 3.8 34.5 1.0
O E:SER217 4.0 28.2 1.0
C B:PHE106 4.1 23.4 1.0
C08 B:HFZ800 4.2 20.0 0.5
O04 B:HFZ800 4.2 20.0 0.5
CA B:MET107 4.3 20.9 1.0
N B:MET107 4.3 20.7 1.0
O E:HOH434 4.4 38.5 1.0
C E:SER217 4.5 30.4 1.0
S02 B:HFZ800 4.5 20.0 0.5
N B:SER108 4.6 17.6 1.0
CD1 B:LEU247 4.6 25.5 1.0
C B:MET107 4.8 23.9 1.0
OG E:SER217 4.8 39.5 1.0
CA E:SER217 4.8 28.9 1.0
N01 B:HFZ800 4.9 20.0 0.5
O B:PRO105 4.9 19.7 1.0
C06 B:HFZ800 4.9 20.0 0.5
OG B:SER242 5.0 29.4 1.0
CA B:PHE106 5.0 19.5 1.0

Fluorine binding site 2 out of 9 in 3ilu

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Fluorine binding site 2 out of 9 in the Crystal Structure of the Ampa Subunit GLUR2 Bound to the Allosteric Modulator, Hydroflumethiazide


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 2 of Crystal Structure of the Ampa Subunit GLUR2 Bound to the Allosteric Modulator, Hydroflumethiazide within 5.0Å range:
probe atom residue distance (Å) B Occ
B:F800

b:20.0
occ:0.50
 F13 B:HFZ800 0.0 20.0 0.5
C11 B:HFZ800 1.4 20.0 0.5
F14 B:HFZ800 2.2 20.0 0.5
F12 B:HFZ800 2.2 20.0 0.5
C10 B:HFZ800 2.4 20.0 0.5
N01 B:HFZ800 2.8 20.0 0.5
O04 B:HFZ800 2.8 20.0 0.5
S02 B:HFZ800 2.9 20.0 0.5
C05 B:HFZ800 2.9 20.0 0.5
CB E:SER217 3.2 34.5 1.0
O E:HOH434 3.4 38.5 1.0
O B:HOH269 3.5 27.4 1.0
C09 B:HFZ800 3.6 20.0 0.5
CB B:SER108 3.9 29.4 1.0
C E:SER217 4.0 30.4 1.0
OG E:SER217 4.0 39.5 1.0
O E:SER217 4.1 28.2 1.0
N B:SER108 4.2 17.6 1.0
CA E:SER217 4.2 28.9 1.0
N E:LYS218 4.3 25.1 1.0
C06 B:HFZ800 4.3 20.0 0.5
O03 B:HFZ800 4.6 20.0 0.5
OG B:SER108 4.6 43.3 1.0
CA B:SER108 4.6 28.4 1.0
O B:HOH379 4.6 30.7 1.0
O03 E:HFZ800 4.7 20.0 0.5
C08 B:HFZ800 4.8 20.0 0.5
CA E:LYS218 4.8 27.5 1.0
C B:MET107 4.8 23.9 1.0
O B:HOH398 4.9 35.8 1.0
O B:HOH533 4.9 35.3 1.0

Fluorine binding site 3 out of 9 in 3ilu

Go back to Fluorine Binding Sites List in 3ilu
Fluorine binding site 3 out of 9 in the Crystal Structure of the Ampa Subunit GLUR2 Bound to the Allosteric Modulator, Hydroflumethiazide


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 3 of Crystal Structure of the Ampa Subunit GLUR2 Bound to the Allosteric Modulator, Hydroflumethiazide within 5.0Å range:
probe atom residue distance (Å) B Occ
B:F800

b:20.0
occ:0.50
 F14 B:HFZ800 0.0 20.0 0.5
C11 B:HFZ800 1.4 20.0 0.5
F13 B:HFZ800 2.2 20.0 0.5
F12 B:HFZ800 2.2 20.0 0.5
C10 B:HFZ800 2.4 20.0 0.5
O04 B:HFZ800 2.4 20.0 0.5
N B:SER108 2.8 17.6 1.0
C B:MET107 2.9 23.9 1.0
CA B:MET107 3.0 20.9 1.0
C05 B:HFZ800 3.1 20.0 0.5
N B:MET107 3.2 20.7 1.0
O B:HOH269 3.2 27.4 1.0
S02 B:HFZ800 3.3 20.0 0.5
C09 B:HFZ800 3.4 20.0 0.5
CA B:SER108 3.7 28.4 1.0
C B:PHE106 3.7 23.4 1.0
O B:MET107 3.7 20.6 1.0
CB B:SER108 3.7 29.4 1.0
O B:PHE106 3.9 22.6 1.0
O B:HOH379 4.0 30.7 1.0
N01 B:HFZ800 4.2 20.0 0.5
O B:PRO105 4.4 19.7 1.0
C06 B:HFZ800 4.4 20.0 0.5
CB B:MET107 4.5 24.7 1.0
C B:PRO105 4.6 22.1 1.0
O03 E:HFZ800 4.6 20.0 0.5
CB B:PRO105 4.6 20.3 1.0
CA B:PHE106 4.6 19.5 1.0
C08 B:HFZ800 4.6 20.0 0.5
O E:HOH434 4.6 38.5 1.0
O03 B:HFZ800 4.7 20.0 0.5
OG B:SER108 4.7 43.3 1.0
N B:PHE106 4.7 19.8 1.0

Fluorine binding site 4 out of 9 in 3ilu

Go back to Fluorine Binding Sites List in 3ilu
Fluorine binding site 4 out of 9 in the Crystal Structure of the Ampa Subunit GLUR2 Bound to the Allosteric Modulator, Hydroflumethiazide


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 4 of Crystal Structure of the Ampa Subunit GLUR2 Bound to the Allosteric Modulator, Hydroflumethiazide within 5.0Å range:
probe atom residue distance (Å) B Occ
E:F800

b:20.0
occ:0.50
 F12 E:HFZ800 0.0 20.0 0.5
C11 E:HFZ800 1.4 20.0 0.5
F13 E:HFZ800 2.2 20.0 0.5
F14 E:HFZ800 2.2 20.0 0.5
C10 E:HFZ800 2.4 20.0 0.5
C09 E:HFZ800 2.7 20.0 0.5
O E:HOH444 2.8 37.3 1.0
O B:HOH351 3.3 35.6 1.0
O E:HOH268 3.6 25.0 1.0
CB B:SER217 3.6 31.9 1.0
C05 E:HFZ800 3.7 20.0 0.5
O B:SER217 3.8 31.0 1.0
O E:PHE106 4.0 23.3 1.0
O B:HOH305 4.0 36.8 1.0
C08 E:HFZ800 4.2 20.0 0.5
O04 E:HFZ800 4.2 20.0 0.5
C B:SER217 4.3 29.2 1.0
C E:PHE106 4.4 24.6 1.0
CA E:MET107 4.5 23.0 1.0
OG B:SER217 4.5 37.7 1.0
S02 E:HFZ800 4.5 20.0 0.5
CA B:SER217 4.6 27.7 1.0
N E:MET107 4.6 20.5 1.0
N E:SER108 4.8 22.0 1.0
N01 E:HFZ800 4.9 20.0 0.5
C06 E:HFZ800 4.9 20.0 0.5
C E:MET107 5.0 25.5 1.0

Fluorine binding site 5 out of 9 in 3ilu

Go back to Fluorine Binding Sites List in 3ilu
Fluorine binding site 5 out of 9 in the Crystal Structure of the Ampa Subunit GLUR2 Bound to the Allosteric Modulator, Hydroflumethiazide


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 5 of Crystal Structure of the Ampa Subunit GLUR2 Bound to the Allosteric Modulator, Hydroflumethiazide within 5.0Å range:
probe atom residue distance (Å) B Occ
E:F800

b:20.0
occ:0.50
 F13 E:HFZ800 0.0 20.0 0.5
C11 E:HFZ800 1.4 20.0 0.5
F14 E:HFZ800 2.2 20.0 0.5
F12 E:HFZ800 2.2 20.0 0.5
C10 E:HFZ800 2.4 20.0 0.5
N01 E:HFZ800 2.8 20.0 0.5
O04 E:HFZ800 2.8 20.0 0.5
O B:HOH305 2.9 36.8 1.0
S02 E:HFZ800 2.9 20.0 0.5
C05 E:HFZ800 2.9 20.0 0.5
CB B:SER217 3.0 31.9 1.0
O E:HOH554 3.4 43.9 1.0
O E:HOH268 3.5 25.0 1.0
C09 E:HFZ800 3.6 20.0 0.5
C B:SER217 3.9 29.2 1.0
OG B:SER217 3.9 37.7 1.0
CB E:SER108 3.9 32.8 1.0
CA B:SER217 4.0 27.7 1.0
O B:SER217 4.1 31.0 1.0
N B:LYS218 4.3 26.0 1.0
N E:SER108 4.3 22.0 1.0
C06 E:HFZ800 4.3 20.0 0.5
O E:HOH444 4.4 37.3 1.0
O03 E:HFZ800 4.6 20.0 0.5
CA E:SER108 4.7 27.2 1.0
C08 E:HFZ800 4.8 20.0 0.5
O03 B:HFZ800 4.8 20.0 0.5
CA B:LYS218 4.8 26.0 1.0
O B:HOH351 4.9 35.6 1.0
OG E:SER108 4.9 42.4 1.0
C E:MET107 4.9 25.5 1.0

Fluorine binding site 6 out of 9 in 3ilu

Go back to Fluorine Binding Sites List in 3ilu
Fluorine binding site 6 out of 9 in the Crystal Structure of the Ampa Subunit GLUR2 Bound to the Allosteric Modulator, Hydroflumethiazide


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 6 of Crystal Structure of the Ampa Subunit GLUR2 Bound to the Allosteric Modulator, Hydroflumethiazide within 5.0Å range:
probe atom residue distance (Å) B Occ
E:F800

b:20.0
occ:0.50
 F14 E:HFZ800 0.0 20.0 0.5
C11 E:HFZ800 1.4 20.0 0.5
F13 E:HFZ800 2.2 20.0 0.5
F12 E:HFZ800 2.2 20.0 0.5
C10 E:HFZ800 2.4 20.0 0.5
O04 E:HFZ800 2.4 20.0 0.5
N E:SER108 2.9 22.0 1.0
CA E:MET107 3.0 23.0 1.0
C E:MET107 3.0 25.5 1.0
C05 E:HFZ800 3.1 20.0 0.5
O E:HOH268 3.2 25.0 1.0
S02 E:HFZ800 3.3 20.0 0.5
N E:MET107 3.3 20.5 1.0
C09 E:HFZ800 3.4 20.0 0.5
O E:HOH444 3.5 37.3 1.0
C E:PHE106 3.7 24.6 1.0
CB E:SER108 3.8 32.8 1.0
CA E:SER108 3.8 27.2 1.0
O E:PHE106 3.9 23.3 1.0
O E:MET107 3.9 21.8 1.0
N01 E:HFZ800 4.2 20.0 0.5
O B:HOH305 4.3 36.8 1.0
C06 E:HFZ800 4.4 20.0 0.5
CB E:MET107 4.4 22.5 1.0
C08 E:HFZ800 4.6 20.0 0.5
O03 B:HFZ800 4.6 20.0 0.5
O03 E:HFZ800 4.7 20.0 0.5
CA E:PHE106 4.7 23.1 1.0
O E:PRO105 4.7 23.2 1.0
CB E:PRO105 4.8 23.2 1.0
C E:PRO105 4.9 24.1 1.0
CG E:MET107 4.9 25.9 1.0
N E:PHE106 4.9 21.1 1.0
CB B:SER217 5.0 31.9 1.0
OG E:SER108 5.0 42.4 1.0

Fluorine binding site 7 out of 9 in 3ilu

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Fluorine binding site 7 out of 9 in the Crystal Structure of the Ampa Subunit GLUR2 Bound to the Allosteric Modulator, Hydroflumethiazide


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 7 of Crystal Structure of the Ampa Subunit GLUR2 Bound to the Allosteric Modulator, Hydroflumethiazide within 5.0Å range:
probe atom residue distance (Å) B Occ
H:F800

b:20.0
occ:0.50
 F12 H:HFZ800 0.0 20.0 0.5
C11 H:HFZ800 1.4 20.0 0.5
F13 H:HFZ800 2.2 20.0 0.5
F14 H:HFZ800 2.2 20.0 0.5
C10 H:HFZ800 2.4 20.0 0.5
C09 H:HFZ800 2.7 20.0 0.5
O H:HOH384 2.8 31.5 1.0
O H:HOH286 3.4 24.9 1.0
O H:HOH306 3.6 29.8 1.0
C05 H:HFZ800 3.7 20.0 0.5
O H:PHE106 3.8 21.4 1.0
C H:PHE106 4.2 20.6 1.0
C08 H:HFZ800 4.2 20.0 0.5
O04 H:HFZ800 4.2 20.0 0.5
CA H:MET107 4.4 22.4 1.0
N H:MET107 4.4 19.9 1.0
S02 H:HFZ800 4.5 20.0 0.5
N H:SER108 4.7 19.6 1.0
N01 H:HFZ800 4.9 20.0 0.5
C06 H:HFZ800 4.9 20.0 0.5
C H:MET107 4.9 24.1 1.0
CD1 H:LEU247 5.0 28.2 1.0
O H:PRO105 5.0 18.1 1.0

Fluorine binding site 8 out of 9 in 3ilu

Go back to Fluorine Binding Sites List in 3ilu
Fluorine binding site 8 out of 9 in the Crystal Structure of the Ampa Subunit GLUR2 Bound to the Allosteric Modulator, Hydroflumethiazide


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 8 of Crystal Structure of the Ampa Subunit GLUR2 Bound to the Allosteric Modulator, Hydroflumethiazide within 5.0Å range:
probe atom residue distance (Å) B Occ
H:F800

b:20.0
occ:0.50
 F13 H:HFZ800 0.0 20.0 0.5
C11 H:HFZ800 1.4 20.0 0.5
F14 H:HFZ800 2.2 20.0 0.5
F12 H:HFZ800 2.2 20.0 0.5
C10 H:HFZ800 2.4 20.0 0.5
N01 H:HFZ800 2.8 20.0 0.5
O04 H:HFZ800 2.8 20.0 0.5
S02 H:HFZ800 2.9 20.0 0.5
C05 H:HFZ800 2.9 20.0 0.5
O H:HOH286 3.4 24.9 1.0
C09 H:HFZ800 3.6 20.0 0.5
CB H:SER108 3.8 28.9 1.0
N H:SER108 4.2 19.6 1.0
O H:HOH384 4.3 31.5 1.0
C06 H:HFZ800 4.3 20.0 0.5
O03 H:HFZ800 4.6 20.0 0.5
CA H:SER108 4.6 23.4 1.0
C08 H:HFZ800 4.8 20.0 0.5
C H:MET107 4.8 24.1 1.0
OG H:SER108 4.9 37.3 1.0
CA H:MET107 5.0 22.4 1.0

Fluorine binding site 9 out of 9 in 3ilu

Go back to Fluorine Binding Sites List in 3ilu
Fluorine binding site 9 out of 9 in the Crystal Structure of the Ampa Subunit GLUR2 Bound to the Allosteric Modulator, Hydroflumethiazide


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 9 of Crystal Structure of the Ampa Subunit GLUR2 Bound to the Allosteric Modulator, Hydroflumethiazide within 5.0Å range:
probe atom residue distance (Å) B Occ
H:F800

b:20.0
occ:0.50
 F14 H:HFZ800 0.0 20.0 0.5
C11 H:HFZ800 1.4 20.0 0.5
F13 H:HFZ800 2.2 20.0 0.5
F12 H:HFZ800 2.2 20.0 0.5
C10 H:HFZ800 2.4 20.0 0.5
O04 H:HFZ800 2.4 20.0 0.5
N H:SER108 2.9 19.6 1.0
CA H:MET107 3.0 22.4 1.0
C H:MET107 3.0 24.1 1.0
C05 H:HFZ800 3.1 20.0 0.5
N H:MET107 3.2 19.9 1.0
S02 H:HFZ800 3.3 20.0 0.5
O H:HOH286 3.4 24.9 1.0
C09 H:HFZ800 3.4 20.0 0.5
C H:PHE106 3.5 20.6 1.0
O H:HOH384 3.7 31.5 1.0
O H:PHE106 3.8 21.4 1.0
O H:MET107 3.8 20.5 1.0
CA H:SER108 3.8 23.4 1.0
CB H:SER108 3.9 28.9 1.0
N01 H:HFZ800 4.2 20.0 0.5
O H:PRO105 4.4 18.1 1.0
C06 H:HFZ800 4.4 20.0 0.5
CA H:PHE106 4.5 18.9 1.0
CB H:MET107 4.5 22.6 1.0
CB H:PRO105 4.5 18.5 1.0
C H:PRO105 4.5 19.7 1.0
C08 H:HFZ800 4.6 20.0 0.5
N H:PHE106 4.6 20.1 1.0
O03 H:HFZ800 4.7 20.0 0.5

Reference:

C.P.Ptak, A.H.Ahmed, R.E.Oswald. Probing the Allosteric Modulator Binding Site of GLUR2 with Thiazide Derivatives Biochemistry V. 48 8594 2009.
ISSN: ISSN 0006-2960
PubMed: 19673491
DOI: 10.1021/BI901127S
Page generated: Wed Jul 31 19:31:53 2024

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