Bromine 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:

Fluorine	(F)	2 atoms
Iron	(Fe)	2 atoms

The binding sites of Bromine 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 Bromine atom.
In total 2 binding sites of Bromine where determined in the Structural Insights Into Substrate and Inhibitor Binding Sites in Human Indoleamine 2,3-Dioxygenase 1, PDB code: 5wn8:
Jump to Bromine binding site number: 1; 2;

Bromine 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 Bromine with other atoms in the Br 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:Br502 b:0.7 occ:1.00 BR8 A:BBJ502 0.0 0.7 1.0 C2 A:BBJ502 1.9 0.9 1.0 C1 A:BBJ502 2.8 0.1 1.0 C3 A:BBJ502 2.9 0.6 1.0 F7 A:BBJ502 3.0 0.7 1.0 SG A:CYS129 3.3 70.8 1.0 C A:GLY262 3.4 90.3 1.0 CD2 A:LEU234 3.5 80.7 1.0 CA A:GLY262 3.5 87.7 1.0 O A:GLY262 3.7 95.1 1.0 CD1 A:LEU234 3.7 77.2 1.0 N A:SER263 3.8 89.2 1.0 CG A:LEU234 3.9 79.2 1.0 CB A:LEU234 4.0 79.2 1.0 C6 A:BBJ502 4.1 0.5 1.0 C4 A:BBJ502 4.2 0.4 1.0 CE1 A:PHE164 4.5 71.4 1.0 CA A:SER263 4.6 85.7 1.0 C5 A:BBJ502 4.7 0.3 1.0 N A:GLY262 4.7 85.6 1.0 O A:SER263 4.9 85.5 1.0 C A:SER263 4.9 85.3 1.0 CA A:LEU234 4.9 80.9 1.0 CB A:CYS129 5.0 66.9 1.0

Bromine 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 Bromine with other atoms in the Br 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:Br502 b:0.1 occ:1.00 BR8 B:BBJ502 0.0 0.1 1.0 C2 B:BBJ502 1.9 0.4 1.0 C1 B:BBJ502 2.8 0.5 1.0 C3 B:BBJ502 2.8 0.4 1.0 F7 B:BBJ502 3.0 0.5 1.0 SG B:CYS129 3.4 58.4 1.0 CA B:GLY262 3.4 82.5 1.0 C B:GLY262 3.6 84.9 1.0 CD2 B:LEU234 3.7 64.5 1.0 N B:SER263 3.9 83.9 1.0 O B:GLY262 4.0 86.8 1.0 CD1 B:LEU234 4.0 66.4 1.0 C6 B:BBJ502 4.1 0.9 1.0 C4 B:BBJ502 4.1 0.1 1.0 CG B:LEU234 4.2 66.5 1.0 N B:TYR126 4.4 57.3 1.0 CB B:LEU234 4.5 66.1 1.0 O B:SER263 4.5 82.6 1.0 N B:GLY262 4.5 79.6 1.0 CA B:TYR126 4.6 59.9 1.0 C5 B:BBJ502 4.6 0.9 1.0 CA B:SER263 4.7 80.7 1.0 C B:VAL125 4.7 55.7 1.0 C B:SER263 4.8 80.8 1.0 O B:VAL125 4.9 51.2 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