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Fluorine in PDB 5r4t: Pandda Analysis Group Deposition -- Crystal Structure of Human Cleavage Factor Im in Complex with Sk-430

Protein crystallography data

The structure of Pandda Analysis Group Deposition -- Crystal Structure of Human Cleavage Factor Im in Complex with Sk-430, PDB code: 5r4t was solved by S.L.Kidd, N.Mateu, R.Talon, T.Krojer, A.Aimon, A.R.Bradley, M.Fairhead, L.Diaz-Saez, H.F.Sore, A.Madin, K.V.M.Huber, F.Von Delft, D.R.Spring, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 70.99 / 1.68
Space group P 32 2 1
Cell size a, b, c (Å), α, β, γ (°) 59.010, 59.010, 212.964, 90.00, 90.00, 120.00
R / Rfree (%) 21.3 / 25.9

Other elements in 5r4t:

The structure of Pandda Analysis Group Deposition -- Crystal Structure of Human Cleavage Factor Im in Complex with Sk-430 also contains other interesting chemical elements:

Zinc (Zn) 6 atoms

Fluorine Binding Sites:

The binding sites of Fluorine atom in the Pandda Analysis Group Deposition -- Crystal Structure of Human Cleavage Factor Im in Complex with Sk-430 (pdb code 5r4t). This binding sites where shown within 5.0 Angstroms radius around Fluorine atom.
In total 2 binding sites of Fluorine where determined in the Pandda Analysis Group Deposition -- Crystal Structure of Human Cleavage Factor Im in Complex with Sk-430, PDB code: 5r4t:
Jump to Fluorine binding site number: 1; 2;

Fluorine binding site 1 out of 2 in 5r4t

Go back to Fluorine Binding Sites List in 5r4t
Fluorine binding site 1 out of 2 in the Pandda Analysis Group Deposition -- Crystal Structure of Human Cleavage Factor Im in Complex with Sk-430


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 1 of Pandda Analysis Group Deposition -- Crystal Structure of Human Cleavage Factor Im in Complex with Sk-430 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:F305

b:46.2
occ:0.50
F A:RWG305 0.0 46.2 0.5
C11 A:RWG305 1.3 46.2 0.5
C10 A:RWG305 2.3 47.2 0.5
C12 A:RWG305 2.4 44.6 0.5
CD1 A:LEU97 2.6 46.8 1.0
CB A:LEU97 3.0 40.5 1.0
CG A:LEU97 3.3 44.1 1.0
C9 A:RWG305 3.5 43.9 0.5
C13 A:RWG305 3.6 42.7 0.5
CB A:LYS105 3.6 34.8 0.5
O A:LEU106 3.8 30.0 1.0
CD A:LYS105 3.9 35.4 0.5
CE2 A:TYR191 3.9 46.4 1.0
CG A:LYS105 4.0 34.9 0.5
C8 A:RWG305 4.0 45.1 0.5
C A:LEU106 4.2 25.9 1.0
O A:LYS105 4.3 31.2 0.5
CD2 A:LEU97 4.3 48.8 1.0
CA A:LEU97 4.3 35.6 1.0
CD2 A:TYR191 4.4 46.7 1.0
CA A:PRO107 4.4 28.6 1.0
N A:PRO107 4.4 29.5 1.0
C A:LYS105 4.4 32.1 0.5
CZ A:TYR191 4.4 47.0 1.0
O A:LEU97 4.6 40.8 1.0
CA A:LYS105 4.6 33.9 0.5
OH A:TYR191 4.6 49.1 1.0
C A:LEU97 4.8 36.4 1.0
CG2 A:ILE128 4.8 37.1 1.0
CE A:LYS105 4.9 36.1 0.5
N A:LEU97 4.9 33.5 1.0
N A:LEU106 4.9 29.7 1.0
CD1 A:ILE128 5.0 38.9 1.0

Fluorine binding site 2 out of 2 in 5r4t

Go back to Fluorine Binding Sites List in 5r4t
Fluorine binding site 2 out of 2 in the Pandda Analysis Group Deposition -- Crystal Structure of Human Cleavage Factor Im in Complex with Sk-430


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 2 of Pandda Analysis Group Deposition -- Crystal Structure of Human Cleavage Factor Im in Complex with Sk-430 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:F306

b:45.8
occ:0.78
F A:RWG306 0.0 45.8 0.8
C11 A:RWG306 1.3 50.1 0.8
C12 A:RWG306 2.3 49.0 0.8
C10 A:RWG306 2.4 48.6 0.8
O A:HOH467 3.1 48.8 1.0
C A:ALA183 3.2 33.9 1.0
N A:ALA183 3.2 31.4 1.0
CA A:ALA183 3.4 32.2 1.0
O A:ALA183 3.4 35.8 1.0
N A:LEU184 3.5 32.6 1.0
C13 A:RWG306 3.6 50.8 0.8
C9 A:RWG306 3.6 52.0 0.8
C A:LYS182 3.8 30.1 1.0
CB A:LYS182 3.9 39.0 1.0
C8 A:RWG306 4.1 52.2 0.8
O A:LYS182 4.4 33.6 1.0
CB A:LEU184 4.4 40.3 1.0
CA A:LEU184 4.4 36.0 1.0
CA A:LYS182 4.5 34.1 1.0
O A:HOH474 4.5 48.1 1.0
O A:HOH405 4.7 34.7 1.0
OG1 A:THR46 4.8 42.1 1.0
CB A:ALA183 4.9 33.6 1.0
O A:ASN44 5.0 39.8 1.0

Reference:

S.L.Kidd, N.Mateu, R.Talon, T.Krojer, A.Aimon, A.R.Bradley, M.Fairhead, L.Diaz-Saez, H.F.Sore, A.Madin, K.V.M.Huber, F.Von Delft, D.R.Spring. Pandda Analysis Group Deposition To Be Published.
Page generated: Tue Jul 15 06:46:43 2025

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