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Fluorine in PDB 7od9: Crystal Structure of Activated Chey Fused to the C-Terminal Domain of Chef

Protein crystallography data

The structure of Crystal Structure of Activated Chey Fused to the C-Terminal Domain of Chef, PDB code: 7od9 was solved by F.Altegoer, P.Weiland, G.Bange, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 44.07 / 2.30
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 56.29, 70.87, 59.82, 90, 91.6, 90
R / Rfree (%) 25 / 30.7

Other elements in 7od9:

The structure of Crystal Structure of Activated Chey Fused to the C-Terminal Domain of Chef also contains other interesting chemical elements:

Magnesium (Mg) 2 atoms

Fluorine Binding Sites:

The binding sites of Fluorine atom in the Crystal Structure of Activated Chey Fused to the C-Terminal Domain of Chef (pdb code 7od9). This binding sites where shown within 5.0 Angstroms radius around Fluorine atom.
In total 6 binding sites of Fluorine where determined in the Crystal Structure of Activated Chey Fused to the C-Terminal Domain of Chef, PDB code: 7od9:
Jump to Fluorine binding site number: 1; 2; 3; 4; 5; 6;

Fluorine binding site 1 out of 6 in 7od9

Go back to Fluorine Binding Sites List in 7od9
Fluorine binding site 1 out of 6 in the Crystal Structure of Activated Chey Fused to the C-Terminal Domain of Chef


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 Activated Chey Fused to the C-Terminal Domain of Chef within 5.0Å range:
probe atom residue distance (Å) B Occ
B:F202

b:43.9
occ:1.00
F1 B:BEF202 0.0 43.9 1.0
BE B:BEF202 1.5 54.4 1.0
MG B:MG201 2.0 50.5 0.9
OD2 B:ASP57 2.3 51.1 1.0
O F:HOH404 2.5 36.8 1.0
F3 B:BEF202 2.5 38.0 1.0
F2 B:BEF202 2.6 49.5 1.0
OD1 B:ASP57 2.6 50.5 1.0
CG B:ASP57 2.8 41.3 1.0
O B:VAL59 2.8 42.8 1.0
O B:HOH325 3.1 51.5 1.0
CB B:VAL59 3.5 56.8 1.0
N B:VAL59 3.6 42.9 1.0
C B:VAL59 3.7 54.0 1.0
CA B:VAL59 3.8 55.0 1.0
OD1 B:ASP12 3.8 61.5 1.0
O F:PHE348 3.9 56.5 1.0
NZ B:LYS107 4.2 43.8 1.0
CB B:ASP57 4.3 42.2 1.0
CG1 B:VAL59 4.4 49.4 1.0
N B:ILE58 4.5 50.3 1.0
CG2 B:VAL59 4.5 52.4 1.0
C B:ILE58 4.7 48.8 1.0
CG B:ASP12 4.7 52.6 1.0
OD2 B:ASP12 4.8 49.7 1.0
OD2 B:ASP11 4.8 51.5 1.0
OD1 B:ASP11 4.9 52.2 1.0
OG1 B:THR85 4.9 52.4 1.0
CG B:MET60 4.9 63.7 1.0
N B:MET60 4.9 46.8 1.0
C F:PHE348 5.0 56.5 1.0
OG B:SER86 5.0 59.6 1.0

Fluorine binding site 2 out of 6 in 7od9

Go back to Fluorine Binding Sites List in 7od9
Fluorine binding site 2 out of 6 in the Crystal Structure of Activated Chey Fused to the C-Terminal Domain of Chef


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 Activated Chey Fused to the C-Terminal Domain of Chef within 5.0Å range:
probe atom residue distance (Å) B Occ
B:F202

b:49.5
occ:1.00
F2 B:BEF202 0.0 49.5 1.0
BE B:BEF202 1.6 54.4 1.0
OD1 B:ASP57 2.4 50.5 1.0
F3 B:BEF202 2.5 38.0 1.0
F1 B:BEF202 2.6 43.9 1.0
NZ B:LYS107 2.8 43.8 1.0
N B:SER86 2.9 56.5 1.0
CA B:THR85 3.4 55.1 1.0
CE B:LYS107 3.4 46.2 1.0
CG B:ASP57 3.4 41.3 1.0
OG B:SER86 3.5 59.6 1.0
OG1 B:THR85 3.5 52.4 1.0
C B:THR85 3.6 54.7 1.0
O F:HOH404 3.6 36.8 1.0
CB B:SER86 3.7 58.1 1.0
CD B:LYS107 3.8 47.0 1.0
OD2 B:ASP57 3.9 51.1 1.0
CA B:SER86 3.9 57.5 1.0
O F:PHE348 3.9 56.5 1.0
CB B:THR85 4.0 46.1 1.0
MG B:MG201 4.3 50.5 0.9
O B:CYS84 4.3 41.1 1.0
N B:THR85 4.6 55.8 1.0
C F:PHE348 4.6 56.5 1.0
CG B:LYS107 4.7 55.9 1.0
CB B:ASP57 4.7 42.2 1.0
O B:THR85 4.7 51.8 1.0
OD1 B:ASP11 4.7 52.2 1.0
C B:SER86 4.9 61.1 1.0
N B:VAL87 4.9 59.5 1.0
N B:ILE58 4.9 50.3 1.0
C B:CYS84 4.9 46.8 1.0

Fluorine binding site 3 out of 6 in 7od9

Go back to Fluorine Binding Sites List in 7od9
Fluorine binding site 3 out of 6 in the Crystal Structure of Activated Chey Fused to the C-Terminal Domain of Chef


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 Activated Chey Fused to the C-Terminal Domain of Chef within 5.0Å range:
probe atom residue distance (Å) B Occ
B:F202

b:38.0
occ:1.00
F3 B:BEF202 0.0 38.0 1.0
BE B:BEF202 1.5 54.4 1.0
OD1 B:ASP57 2.2 50.5 1.0
F2 B:BEF202 2.5 49.5 1.0
F1 B:BEF202 2.5 43.9 1.0
OG1 B:THR85 2.6 52.4 1.0
N B:VAL59 2.7 42.9 1.0
N B:ILE58 2.9 50.3 1.0
CG B:ASP57 3.0 41.3 1.0
OD2 B:ASP57 3.3 51.1 1.0
CB B:THR85 3.3 46.1 1.0
CA B:ILE58 3.5 52.8 1.0
C B:ILE58 3.6 48.8 1.0
CB B:ILE58 3.6 42.4 1.0
CB B:VAL59 3.7 56.8 1.0
CA B:VAL59 3.7 55.0 1.0
CA B:THR85 3.8 55.1 1.0
CG2 B:VAL59 4.0 52.4 1.0
C B:ASP57 4.0 49.2 1.0
N B:SER86 4.0 56.5 1.0
CB B:ASP57 4.2 42.2 1.0
O B:VAL59 4.2 42.8 1.0
MG B:MG201 4.2 50.5 0.9
CA B:ASP57 4.2 47.9 1.0
CG2 B:ILE58 4.4 50.2 1.0
C B:VAL59 4.4 54.0 1.0
C B:THR85 4.5 54.7 1.0
CG1 B:VAL87 4.5 62.3 1.0
O F:HOH404 4.7 36.8 1.0
CG2 B:THR85 4.7 50.5 1.0
O B:ILE58 4.7 47.7 1.0
O B:CYS84 4.8 41.1 1.0
CG1 B:ILE58 4.8 46.1 1.0
NZ B:LYS107 4.8 43.8 1.0
OG B:SER86 4.8 59.6 1.0
N B:VAL87 4.9 59.5 1.0

Fluorine binding site 4 out of 6 in 7od9

Go back to Fluorine Binding Sites List in 7od9
Fluorine binding site 4 out of 6 in the Crystal Structure of Activated Chey Fused to the C-Terminal Domain of Chef


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 Activated Chey Fused to the C-Terminal Domain of Chef within 5.0Å range:
probe atom residue distance (Å) B Occ
A:F202

b:73.0
occ:1.00
F1 A:BEF202 0.0 73.0 1.0
BE A:BEF202 1.5 75.2 1.0
OD1 A:ASP57 2.2 80.9 1.0
F3 A:BEF202 2.5 69.1 1.0
F2 A:BEF202 2.6 88.2 1.0
CG A:ASP57 3.0 81.5 1.0
N A:VAL59 3.1 79.8 1.0
OD2 A:ASP57 3.1 72.5 1.0
OG1 A:THR85 3.2 67.3 1.0
CB A:VAL59 3.2 83.7 1.0
MG A:MG201 3.4 80.2 1.0
CA A:VAL59 3.6 84.6 1.0
O A:VAL59 3.6 94.1 1.0
N A:ILE58 3.8 75.3 1.0
CG2 A:VAL59 3.9 56.3 1.0
C A:ILE58 4.0 71.1 1.0
C A:VAL59 4.1 90.0 1.0
OG A:SER86 4.1 77.2 1.0
CB A:THR85 4.1 64.8 1.0
CA A:ILE58 4.3 68.2 1.0
N A:SER86 4.3 63.6 1.0
CB A:ASP57 4.4 70.6 1.0
CG1 A:VAL59 4.4 74.6 1.0
CA A:THR85 4.5 70.6 1.0
CG2 A:VAL87 4.5 65.5 1.0
O A:HOH309 4.6 81.1 1.0
CB A:ILE58 4.7 81.7 1.0
C A:ASP57 4.7 68.9 1.0
CA A:ASP57 4.7 68.8 1.0
CD1 A:ILE58 4.8 76.3 1.0
O A:HOH304 4.9 103.6 1.0

Fluorine binding site 5 out of 6 in 7od9

Go back to Fluorine Binding Sites List in 7od9
Fluorine binding site 5 out of 6 in the Crystal Structure of Activated Chey Fused to the C-Terminal Domain of Chef


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 Activated Chey Fused to the C-Terminal Domain of Chef within 5.0Å range:
probe atom residue distance (Å) B Occ
A:F202

b:88.2
occ:1.00
F2 A:BEF202 0.0 88.2 1.0
BE A:BEF202 1.6 75.2 1.0
MG A:MG201 2.0 80.2 1.0
O A:HOH309 2.2 81.1 1.0
OD2 A:ASP57 2.4 72.5 1.0
F3 A:BEF202 2.5 69.1 1.0
F1 A:BEF202 2.6 73.0 1.0
OD1 A:ASP57 3.1 80.9 1.0
CG A:ASP57 3.1 81.5 1.0
C C:PHE348 3.5 83.8 1.0
O C:PHE348 3.5 82.3 1.0
O A:VAL59 3.7 94.1 1.0
OD1 A:ASP12 3.8 92.0 1.0
O A:HOH304 3.9 103.6 1.0
NZ A:LYS107 4.1 70.2 1.0
OG A:SER86 4.3 77.2 1.0
OD1 A:ASP11 4.5 76.2 1.0
CB A:VAL59 4.5 83.7 1.0
CB A:ASP57 4.5 70.6 1.0
OD2 A:ASP11 4.6 77.8 1.0
CG A:ASP12 4.6 94.7 1.0
OD2 A:ASP12 4.6 94.7 1.0
C A:VAL59 4.7 90.0 1.0
CG A:ASP11 4.9 77.9 1.0
CG1 A:VAL59 4.9 74.6 1.0
N A:VAL59 5.0 79.8 1.0
CA C:PHE348 5.0 85.4 1.0
CA A:VAL59 5.0 84.6 1.0

Fluorine binding site 6 out of 6 in 7od9

Go back to Fluorine Binding Sites List in 7od9
Fluorine binding site 6 out of 6 in the Crystal Structure of Activated Chey Fused to the C-Terminal Domain of Chef


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 Activated Chey Fused to the C-Terminal Domain of Chef within 5.0Å range:
probe atom residue distance (Å) B Occ
A:F202

b:69.1
occ:1.00
F3 A:BEF202 0.0 69.1 1.0
BE A:BEF202 1.5 75.2 1.0
F2 A:BEF202 2.5 88.2 1.0
F1 A:BEF202 2.5 73.0 1.0
N A:SER86 2.7 63.6 1.0
OD1 A:ASP57 2.9 80.9 1.0
OG A:SER86 2.9 77.2 1.0
CA A:THR85 3.2 70.6 1.0
OG1 A:THR85 3.3 67.3 1.0
NZ A:LYS107 3.4 70.2 1.0
C A:THR85 3.4 70.6 1.0
CB A:SER86 3.6 71.9 1.0
CE A:LYS107 3.6 75.9 1.0
CD A:LYS107 3.7 65.2 1.0
CA A:SER86 3.7 72.6 1.0
CG A:ASP57 3.7 81.5 1.0
CB A:THR85 3.7 64.8 1.0
OD2 A:ASP57 3.9 72.5 1.0
O C:PHE348 4.0 82.3 1.0
CG A:LYS107 4.1 70.1 1.0
O A:HOH309 4.4 81.1 1.0
MG A:MG201 4.4 80.2 1.0
C C:PHE348 4.4 83.8 1.0
N A:THR85 4.4 62.7 1.0
O A:CYS84 4.5 60.3 1.0
O A:THR85 4.6 68.0 1.0
N A:VAL87 4.6 70.5 1.0
C A:SER86 4.7 72.0 1.0
C A:CYS84 4.9 61.3 1.0

Reference:

F.Altegoer, T.E.F.Quax, P.Weiland, P.Nussbaum, P.I.Giammarinaro, M.Patro, Z.Li, D.Oesterhelt, M.Grininger, S.V.Albers, G.Bange. Structural Insights Into the Mechanism of Archaellar Rotational Switching. Nat Commun V. 13 2857 2022.
ISSN: ESSN 2041-1723
PubMed: 35606361
DOI: 10.1038/S41467-022-30358-9
Page generated: Tue Jul 15 22:31:56 2025

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