Fluorine in PDB 6o3i: Crystal Structure of Human IDO1 Bound to Navoximod (Nlg-919)

All present enzymatic activity of Crystal Structure of Human IDO1 Bound to Navoximod (Nlg-919):
1.13.11.52;

The structure of Crystal Structure of Human IDO1 Bound to Navoximod (Nlg-919), PDB code: 6o3i was solved by S.F.Harris, A.Oh, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	74.17 / 2.69
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	85.062, 90.224, 130.237, 90.00, 90.00, 90.00
R / Rfree (%)	21.6 / 26.4

The structure of Crystal Structure of Human IDO1 Bound to Navoximod (Nlg-919) also contains other interesting chemical elements:

Iron

(Fe)

2 atoms

The binding sites of Fluorine atom in the Crystal Structure of Human IDO1 Bound to Navoximod (Nlg-919) (pdb code 6o3i). This binding sites where shown within 5.0 Angstroms radius around Fluorine atom.
In total 2 binding sites of Fluorine where determined in the Crystal Structure of Human IDO1 Bound to Navoximod (Nlg-919), PDB code: 6o3i:
Jump to Fluorine binding site number: 1; 2;

Fluorine binding site 1 out of 2 in the Crystal Structure of Human IDO1 Bound to Navoximod (Nlg-919)


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 Human IDO1 Bound to Navoximod (Nlg-919) within 5.0Å range: probe atom residue distance (Å) B Occ A:F502 b:54.0 occ:1.00 F27 A:LKP502 0.0 54.0 1.0 C3 A:LKP502 1.3 48.2 1.0 C2 A:LKP502 2.3 46.6 1.0 C4 A:LKP502 2.3 49.1 1.0 C12 A:LKP502 3.0 46.9 1.0 H13 A:LKP502 3.2 47.4 1.0 CA A:GLY262 3.2 54.6 1.0 C14 A:LKP502 3.2 46.6 1.0 C A:GLY262 3.3 56.7 1.0 CD2 A:LEU234 3.6 54.9 1.0 C1 A:LKP502 3.6 47.2 1.0 C5 A:LKP502 3.6 49.2 1.0 CD1 A:LEU234 3.6 52.4 1.0 N A:SER263 3.8 51.0 1.0 CB A:LEU234 3.8 48.7 1.0 O A:GLY262 3.8 57.2 1.0 CG A:LEU234 3.8 52.7 1.0 C6 A:LKP502 4.1 46.4 1.0 H16 A:LKP502 4.2 47.7 1.0 C15 A:LKP502 4.3 47.6 1.0 C20 A:LKP502 4.4 58.4 1.0 N A:GLY262 4.4 55.3 1.0 N8 A:LKP502 4.4 46.1 1.0 C7 A:LKP502 4.7 47.5 1.0 CA A:SER263 4.7 50.0 1.0 CE2 A:PHE163 4.9 47.0 1.0 O A:LEU234 4.9 55.8 1.0 SG A:CYS129 4.9 50.3 1.0 CA A:LEU234 4.9 49.2 1.0 C18 A:LKP502 4.9 52.8 1.0

Fluorine binding site 2 out of 2 in the Crystal Structure of Human IDO1 Bound to Navoximod (Nlg-919)


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 Human IDO1 Bound to Navoximod (Nlg-919) within 5.0Å range: probe atom residue distance (Å) B Occ B:F502 b:54.4 occ:1.00 F27 B:LKP502 0.0 54.4 1.0 C3 B:LKP502 1.3 52.1 1.0 C2 B:LKP502 2.3 52.4 1.0 C4 B:LKP502 2.3 53.1 1.0 C12 B:LKP502 3.1 53.5 1.0 H13 B:LKP502 3.1 53.4 1.0 CA B:GLY262 3.1 56.7 1.0 C B:GLY262 3.3 58.9 1.0 C14 B:LKP502 3.3 61.2 1.0 N B:SER263 3.6 54.6 1.0 C1 B:LKP502 3.6 50.8 1.0 C5 B:LKP502 3.6 51.9 1.0 O B:GLY262 3.8 58.4 1.0 CB B:LEU234 4.0 58.0 1.0 CD2 B:LEU234 4.0 62.7 1.0 CD1 B:LEU234 4.0 61.3 1.0 C6 B:LKP502 4.1 50.4 1.0 CG B:LEU234 4.2 61.8 1.0 H16 B:LKP502 4.3 66.2 1.0 N B:GLY262 4.3 57.9 1.0 C15 B:LKP502 4.3 66.2 1.0 N8 B:LKP502 4.4 46.2 1.0 C20 B:LKP502 4.4 75.0 1.0 CA B:SER263 4.5 54.4 1.0 C7 B:LKP502 4.7 46.1 1.0 C B:SER263 4.8 56.7 1.0 SG B:CYS129 4.8 60.6 1.0 O B:LEU234 5.0 63.1 1.0

S.Kumar, J.P.Waldo, F.A.Jaipuri, A.Marcinowicz, C.Van Allen, J.Adams, T.Kesharwani, X.Zhang, R.Metz, A.J.Oh, S.F.Harris, M.R.Mautino. Discovery of Clinical Candidate (1R,4R)-4-((R)-2-((S)-6-Fluoro-5H-Imidazo[5, 1-A]Isoindol-5-Yl)-1-Hydroxyethyl)Cyclohexan-1-Ol (Navoximod), A Potent and Selective Inhibitor of Indoleamine 2,3-Dioxygenase 1. J.Med.Chem. V. 62 6705 2019.
ISSN: ISSN 0022-2623
PubMed: 31264862
DOI: 10.1021/ACS.JMEDCHEM.9B00662