Fluorine in PDB 8dip: The Crystal Structure of I38T Mutant Pa Endonuclease (2009/H1N1/California) in Complex with Compound SJ001023030

The structure of The Crystal Structure of I38T Mutant Pa Endonuclease (2009/H1N1/California) in Complex with Compound SJ001023030, PDB code: 8dip was solved by M.G.Cuypers, J.P.Slavish, Z.Rankovic, S.W.White, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	39.98 / 2.50
Space group	I 4 2 2
Cell size a, b, c (Å), α, β, γ (°)	89.316, 89.316, 134.121, 90, 90, 90
R / Rfree (%)	22.8 / 27

The structure of The Crystal Structure of I38T Mutant Pa Endonuclease (2009/H1N1/California) in Complex with Compound SJ001023030 also contains other interesting chemical elements:

Manganese

(Mn)

2 atoms

The binding sites of Fluorine atom in the The Crystal Structure of I38T Mutant Pa Endonuclease (2009/H1N1/California) in Complex with Compound SJ001023030 (pdb code 8dip). This binding sites where shown within 5.0 Angstroms radius around Fluorine atom.
In total 3 binding sites of Fluorine where determined in the The Crystal Structure of I38T Mutant Pa Endonuclease (2009/H1N1/California) in Complex with Compound SJ001023030, PDB code: 8dip:
Jump to Fluorine binding site number: 1; 2; 3;

Fluorine binding site 1 out of 3 in the The Crystal Structure of I38T Mutant Pa Endonuclease (2009/H1N1/California) in Complex with Compound SJ001023030


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 1 of The Crystal Structure of I38T Mutant Pa Endonuclease (2009/H1N1/California) in Complex with Compound SJ001023030 within 5.0Å range: probe atom residue distance (Å) B Occ A:F204 b:149.0 occ:1.00 F26 A:SE9204 0.0 149.0 1.0 C25 A:SE9204 1.4 157.2 1.0 F27 A:SE9204 2.2 163.8 1.0 F28 A:SE9204 2.2 151.2 1.0 C23 A:SE9204 2.4 153.7 1.0 C22 A:SE9204 2.7 146.2 1.0 C24 A:SE9204 3.6 143.8 1.0 C21 A:SE9204 4.1 133.6 1.0 O A:HOH316 4.7 70.4 1.0 CE A:LYS34 4.7 112.3 1.0 C19 A:SE9204 4.7 133.7 1.0 C20 A:SE9204 4.9 131.4 1.0

Fluorine binding site 2 out of 3 in the The Crystal Structure of I38T Mutant Pa Endonuclease (2009/H1N1/California) in Complex with Compound SJ001023030


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 2 of The Crystal Structure of I38T Mutant Pa Endonuclease (2009/H1N1/California) in Complex with Compound SJ001023030 within 5.0Å range: probe atom residue distance (Å) B Occ A:F204 b:163.8 occ:1.00 F27 A:SE9204 0.0 163.8 1.0 C25 A:SE9204 1.4 157.2 1.0 F28 A:SE9204 2.2 151.2 1.0 F26 A:SE9204 2.2 149.0 1.0 C23 A:SE9204 2.4 153.7 1.0 C24 A:SE9204 2.8 143.8 1.0 C22 A:SE9204 3.5 146.2 1.0 C19 A:SE9204 4.1 133.7 1.0 C21 A:SE9204 4.7 133.6 1.0 C20 A:SE9204 4.9 131.4 1.0

Fluorine binding site 3 out of 3 in the The Crystal Structure of I38T Mutant Pa Endonuclease (2009/H1N1/California) in Complex with Compound SJ001023030


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 3 of The Crystal Structure of I38T Mutant Pa Endonuclease (2009/H1N1/California) in Complex with Compound SJ001023030 within 5.0Å range: probe atom residue distance (Å) B Occ A:F204 b:151.2 occ:1.00 F28 A:SE9204 0.0 151.2 1.0 C25 A:SE9204 1.4 157.2 1.0 F27 A:SE9204 2.2 163.8 1.0 F26 A:SE9204 2.2 149.0 1.0 C23 A:SE9204 2.4 153.7 1.0 C24 A:SE9204 3.1 143.8 1.0 C22 A:SE9204 3.3 146.2 1.0 CE A:LYS34 3.7 112.3 1.0 C30 A:SE9204 3.9 132.0 1.0 C19 A:SE9204 4.3 133.7 1.0 C29 A:SE9204 4.5 123.1 1.0 C21 A:SE9204 4.5 133.6 1.0 N31 A:SE9204 4.7 127.4 1.0 CD A:LYS34 4.7 108.3 1.0 C20 A:SE9204 4.9 131.4 1.0

P.J.Slavish, M.G.Cuypers, M.A.Rimmer, A.Abdolvahabi, T.Jeevan, G.Kumar, J.A.Jarusiewicz, S.Vaithiyalingam, J.C.Jones, J.J.Bowling, J.E.Price, R.M.Dubois, J.Min, R.J.Webby, Z.Rankovic, S.W.White. Chemical Scaffold Recycling: Structure-Guided Conversion of An Hiv Integrase Inhibitor Into A Potent Influenza Virus Rna-Dependent Rna Polymerase Inhibitor Designed to Minimize Resistance Potential. Eur.J.Med.Chem. V. 247 15035 2023.
ISSN: ISSN 0223-5234
PubMed: 36603507
DOI: 10.1016/J.EJMECH.2022.115035