Fluorine in PDB 5wn8: Structural Insights Into Substrate and Inhibitor Binding Sites in Human Indoleamine 2,3-Dioxygenase 1

All present enzymatic activity of Structural Insights Into Substrate and Inhibitor Binding Sites in Human Indoleamine 2,3-Dioxygenase 1:
1.13.11.52;

The structure of Structural Insights Into Substrate and Inhibitor Binding Sites in Human Indoleamine 2,3-Dioxygenase 1, PDB code: 5wn8 was solved by A.Lewis-Ballester, K.N.Pham, D.Batabyal, S.Karkashon, J.B.Bonanno, T.L.Poulos, S.R.Yeh, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	29.69 / 2.50
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	86.735, 97.785, 128.739, 90.00, 90.00, 90.00
R / Rfree (%)	21.3 / 25.2

The structure of Structural Insights Into Substrate and Inhibitor Binding Sites in Human Indoleamine 2,3-Dioxygenase 1 also contains other interesting chemical elements:

Bromine	(Br)	2 atoms
Iron	(Fe)	2 atoms

The binding sites of Fluorine atom in the Structural Insights Into Substrate and Inhibitor Binding Sites in Human Indoleamine 2,3-Dioxygenase 1 (pdb code 5wn8). This binding sites where shown within 5.0 Angstroms radius around Fluorine atom.
In total 2 binding sites of Fluorine where determined in the Structural Insights Into Substrate and Inhibitor Binding Sites in Human Indoleamine 2,3-Dioxygenase 1, PDB code: 5wn8:
Jump to Fluorine binding site number: 1; 2;

Fluorine binding site 1 out of 2 in the Structural Insights Into Substrate and Inhibitor Binding Sites in Human Indoleamine 2,3-Dioxygenase 1


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 1 of Structural Insights Into Substrate and Inhibitor Binding Sites in Human Indoleamine 2,3-Dioxygenase 1 within 5.0Å range: probe atom residue distance (Å) B Occ A:F502 b:0.7 occ:1.00 F7 A:BBJ502 0.0 0.7 1.0 C3 A:BBJ502 1.3 0.6 1.0 C2 A:BBJ502 2.3 0.9 1.0 C4 A:BBJ502 2.4 0.4 1.0 CG2 A:VAL130 2.9 68.8 1.0 SG A:CYS129 3.0 70.8 1.0 CD1 A:PHE164 3.0 72.0 1.0 CE1 A:PHE164 3.0 71.4 1.0 BR8 A:BBJ502 3.0 0.7 1.0 C1 A:BBJ502 3.6 0.1 1.0 C5 A:BBJ502 3.7 0.3 1.0 O A:CYS129 4.1 67.5 1.0 C6 A:BBJ502 4.1 0.5 1.0 CG A:PHE164 4.1 70.8 1.0 CB A:CYS129 4.1 66.9 1.0 CZ A:PHE164 4.1 72.8 1.0 C A:CYS129 4.2 64.2 1.0 CB A:VAL130 4.3 67.6 1.0 CD1 A:TYR126 4.4 62.7 1.0 N A:VAL130 4.4 65.0 1.0 CE2 A:PHE163 4.5 80.6 1.0 CD2 A:PHE163 4.7 79.2 1.0 CA A:CYS129 4.8 64.8 1.0 CA A:VAL130 4.8 65.6 1.0 CE1 A:TYR126 4.8 63.8 1.0 CB A:PHE164 4.9 71.2 1.0 CA A:PHE164 4.9 71.1 1.0 CD1 A:LEU234 4.9 77.2 1.0 CD2 A:LEU234 5.0 80.7 1.0 CA A:TYR126 5.0 66.2 1.0

Fluorine binding site 2 out of 2 in the Structural Insights Into Substrate and Inhibitor Binding Sites in Human Indoleamine 2,3-Dioxygenase 1


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 2 of Structural Insights Into Substrate and Inhibitor Binding Sites in Human Indoleamine 2,3-Dioxygenase 1 within 5.0Å range: probe atom residue distance (Å) B Occ B:F502 b:0.5 occ:1.00 F7 B:BBJ502 0.0 0.5 1.0 C3 B:BBJ502 1.3 0.4 1.0 C2 B:BBJ502 2.3 0.4 1.0 C4 B:BBJ502 2.4 0.1 1.0 CG2 B:VAL130 2.9 58.1 1.0 SG B:CYS129 2.9 58.4 1.0 BR8 B:BBJ502 3.0 0.1 1.0 CE1 B:PHE164 3.2 53.5 1.0 CD1 B:PHE164 3.2 55.2 1.0 C1 B:BBJ502 3.6 0.5 1.0 C5 B:BBJ502 3.7 0.9 1.0 C6 B:BBJ502 4.1 0.9 1.0 CD1 B:TYR126 4.2 64.8 1.0 CB B:VAL130 4.2 58.6 1.0 O B:CYS129 4.3 56.6 1.0 C B:CYS129 4.3 58.4 1.0 CB B:CYS129 4.3 55.8 1.0 CZ B:PHE164 4.4 52.2 1.0 N B:VAL130 4.4 59.5 1.0 CG B:PHE164 4.4 54.5 1.0 CE2 B:PHE163 4.5 71.7 1.0 CA B:TYR126 4.7 59.9 1.0 CD2 B:PHE163 4.7 69.6 1.0 CE1 B:TYR126 4.7 65.7 1.0 CA B:VAL130 4.8 58.0 1.0 CA B:CYS129 4.9 56.7 1.0 CD1 B:LEU234 4.9 66.4 1.0 CD2 B:LEU234 4.9 64.5 1.0

A.Lewis-Ballester, K.N.Pham, D.Batabyal, S.Karkashon, J.B.Bonanno, T.L.Poulos, S.R.Yeh. Structural Insights Into Substrate and Inhibitor Binding Sites in Human Indoleamine 2,3-Dioxygenase 1. Nat Commun V. 8 1693 2017.
ISSN: ESSN 2041-1723
PubMed: 29167421
DOI: 10.1038/S41467-017-01725-8