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Fluorine in PDB 5ryw: EPB41L3 Pandda Analysis Group Deposition -- Crystal Structure of the Ferm Domain of Human EPB41L3 in Complex with Z2856434829

Protein crystallography data

The structure of EPB41L3 Pandda Analysis Group Deposition -- Crystal Structure of the Ferm Domain of Human EPB41L3 in Complex with Z2856434829, PDB code: 5ryw was solved by W.J.Bradshaw, V.L.Katis, J.A.Newman, F.Von Delft, C.H.Arrowsmith, A.M.Edwards, C.Bountra, O.Gileadi, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 41.76 / 1.66
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 38.720, 77.310, 99.130, 90.00, 90.00, 90.00
R / Rfree (%) 20.7 / 25.2

Fluorine Binding Sites:

The binding sites of Fluorine atom in the EPB41L3 Pandda Analysis Group Deposition -- Crystal Structure of the Ferm Domain of Human EPB41L3 in Complex with Z2856434829 (pdb code 5ryw). This binding sites where shown within 5.0 Angstroms radius around Fluorine atom.
In total 2 binding sites of Fluorine where determined in the EPB41L3 Pandda Analysis Group Deposition -- Crystal Structure of the Ferm Domain of Human EPB41L3 in Complex with Z2856434829, PDB code: 5ryw:
Jump to Fluorine binding site number: 1; 2;

Fluorine binding site 1 out of 2 in 5ryw

Go back to Fluorine Binding Sites List in 5ryw
Fluorine binding site 1 out of 2 in the EPB41L3 Pandda Analysis Group Deposition -- Crystal Structure of the Ferm Domain of Human EPB41L3 in Complex with Z2856434829


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 1 of EPB41L3 Pandda Analysis Group Deposition -- Crystal Structure of the Ferm Domain of Human EPB41L3 in Complex with Z2856434829 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:F401

b:30.8
occ:0.80
F16 A:ELQ401 0.0 30.8 0.8
C14 A:ELQ401 1.3 27.1 0.8
C13 A:ELQ401 2.3 26.2 0.8
C15 A:ELQ401 2.3 25.6 0.8
F17 A:ELQ401 2.6 28.9 0.8
O A:PHE386 2.9 25.6 0.8
CD1 A:LEU390 3.1 61.9 0.8
CD1 A:PHE387 3.2 21.4 0.8
CA A:PHE387 3.5 26.7 0.8
C10 A:ELQ401 3.6 24.7 0.8
C12 A:ELQ401 3.6 24.1 0.8
C A:PHE386 3.7 23.5 0.8
CE1 A:PHE387 3.8 22.3 0.8
CD1 A:PHE386 3.8 21.4 0.8
CE1 A:PHE386 3.9 22.0 0.8
N A:PHE387 4.0 24.9 0.8
CG A:PHE387 4.1 23.6 0.8
C11 A:ELQ401 4.1 24.5 0.8
CG A:LEU390 4.2 61.8 0.8
CD2 A:LEU390 4.3 61.6 0.8
C A:PHE387 4.3 31.3 0.8
CB A:PHE387 4.3 24.5 0.8
O A:PHE387 4.4 31.5 0.8
CG A:PHE386 4.6 21.6 0.8
CB A:LEU389 4.8 69.0 0.8
CZ A:PHE386 4.8 22.8 0.8
N A:LEU390 4.8 65.8 0.8
C08 A:ELQ401 4.8 26.6 0.8
CB A:LEU390 4.9 63.0 0.8
CA A:PHE386 4.9 22.3 0.8
N A:LEU389 4.9 62.5 0.8
CZ A:PHE387 4.9 21.6 0.8
C A:LEU389 4.9 66.2 0.8

Fluorine binding site 2 out of 2 in 5ryw

Go back to Fluorine Binding Sites List in 5ryw
Fluorine binding site 2 out of 2 in the EPB41L3 Pandda Analysis Group Deposition -- Crystal Structure of the Ferm Domain of Human EPB41L3 in Complex with Z2856434829


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 2 of EPB41L3 Pandda Analysis Group Deposition -- Crystal Structure of the Ferm Domain of Human EPB41L3 in Complex with Z2856434829 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:F401

b:28.9
occ:0.80
F17 A:ELQ401 0.0 28.9 0.8
C13 A:ELQ401 1.3 26.2 0.8
C14 A:ELQ401 2.3 27.1 0.8
C12 A:ELQ401 2.4 24.1 0.8
F16 A:ELQ401 2.6 30.8 0.8
C1 A:DMS404 3.1 31.3 0.8
C11 A:ELQ401 3.6 24.5 0.8
C15 A:ELQ401 3.6 25.6 0.8
CE1 A:PHE387 3.6 22.3 0.8
CE1 A:PHE386 3.7 22.0 0.8
CD1 A:LEU390 3.8 61.9 0.8
CE1 A:TYR150 3.9 18.4 1.0
CD1 A:PHE387 4.0 21.4 0.8
OH A:TYR150 4.0 23.1 1.0
C10 A:ELQ401 4.0 24.7 0.8
CD1 A:PHE386 4.4 21.4 0.8
CZ A:TYR150 4.4 19.9 1.0
CZ A:PHE386 4.5 22.8 0.8
S A:DMS404 4.5 30.2 0.8
O A:DMS404 4.5 31.5 0.8
CD A:PRO191 4.6 23.4 1.0
CD2 A:LEU390 4.7 61.6 0.8
CZ A:PHE387 4.7 21.6 0.8
CG A:LEU390 4.8 61.8 0.8
CD1 A:TYR150 4.9 17.4 1.0
C2 A:DMS404 5.0 28.9 0.8

Reference:

W.J.Bradshaw, V.L.Katis, J.A.Newman, F.Von Delft, C.H.Arrowsmith, A.M.Edwards, C.Bountra, O.Gileadi. EPB41L3 Pandda Analysis Group Deposition To Be Published.
Page generated: Tue Jul 15 07:02:04 2025

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