Chlorine in PDB 6f0a: Crystal Structure of Human Indoleamine 2,3-Dioxygenase Bound to A Triazole Inhibitor and Alanine Molecule.

All present enzymatic activity of Crystal Structure of Human Indoleamine 2,3-Dioxygenase Bound to A Triazole Inhibitor and Alanine Molecule.:
1.13.11.52;

The structure of Crystal Structure of Human Indoleamine 2,3-Dioxygenase Bound to A Triazole Inhibitor and Alanine Molecule., PDB code: 6f0a was solved by M.K.Swan, M.Latchem, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	71.78 / 2.26
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	85.480, 96.890, 132.190, 90.00, 90.00, 90.00
R / Rfree (%)	19.1 / 22.5

The structure of Crystal Structure of Human Indoleamine 2,3-Dioxygenase Bound to A Triazole Inhibitor and Alanine Molecule. also contains other interesting chemical elements:

Iron

(Fe)

2 atoms

The binding sites of Chlorine atom in the Crystal Structure of Human Indoleamine 2,3-Dioxygenase Bound to A Triazole Inhibitor and Alanine Molecule. (pdb code 6f0a). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 2 binding sites of Chlorine where determined in the Crystal Structure of Human Indoleamine 2,3-Dioxygenase Bound to A Triazole Inhibitor and Alanine Molecule., PDB code: 6f0a:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in the Crystal Structure of Human Indoleamine 2,3-Dioxygenase Bound to A Triazole Inhibitor and Alanine Molecule.


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Crystal Structure of Human Indoleamine 2,3-Dioxygenase Bound to A Triazole Inhibitor and Alanine Molecule. within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl501 b:50.5 occ:1.00 CL A:C82501 0.0 50.5 1.0 C2 A:C82501 1.7 54.1 1.0 C1 A:C82501 2.7 57.0 1.0 C3 A:C82501 2.7 54.4 1.0 H2 A:C82501 2.8 57.5 1.0 H3 A:C82501 2.8 54.9 1.0 CB A:CYS129 3.3 48.5 1.0 O A:VAL125 3.8 37.1 1.0 C A:VAL125 3.8 37.7 1.0 CD2 A:LEU234 3.9 38.7 1.0 SG A:CYS129 3.9 54.2 1.0 CD2 A:LEU124 3.9 35.3 1.0 C A:C82501 4.0 56.5 1.0 C4 A:C82501 4.0 54.6 1.0 N A:TYR126 4.0 34.1 1.0 CG A:LEU124 4.0 36.8 1.0 CA A:GLY262 4.1 41.8 1.0 O A:LEU124 4.3 37.4 1.0 CA A:TYR126 4.4 33.4 1.0 CA A:VAL125 4.4 32.1 1.0 C A:LEU124 4.5 38.2 1.0 C5 A:C82501 4.5 53.7 1.0 N A:VAL125 4.5 33.5 1.0 CA A:CYS129 4.7 46.4 1.0 C A:GLY262 4.7 45.0 1.0 CB A:LEU234 4.8 36.7 1.0 H1 A:C82501 4.8 57.0 1.0 CB A:LEU124 4.8 33.3 1.0 H4 A:C82501 4.8 54.9 1.0 CG A:LEU234 4.8 39.7 1.0 N A:GLY262 4.9 42.7 1.0 N A:CYS129 5.0 44.7 1.0

Chlorine binding site 2 out of 2 in the Crystal Structure of Human Indoleamine 2,3-Dioxygenase Bound to A Triazole Inhibitor and Alanine Molecule.


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Crystal Structure of Human Indoleamine 2,3-Dioxygenase Bound to A Triazole Inhibitor and Alanine Molecule. within 5.0Å range: probe atom residue distance (Å) B Occ C:Cl501 b:56.3 occ:1.00 CL C:C82501 0.0 56.3 1.0 C2 C:C82501 1.7 57.0 1.0 C1 C:C82501 2.7 60.1 1.0 C3 C:C82501 2.7 58.5 1.0 H2 C:C82501 2.8 60.8 1.0 H3 C:C82501 2.8 59.1 1.0 CB C:CYS129 3.4 52.3 1.0 O C:VAL125 3.7 42.7 1.0 CA C:GLY262 3.7 47.8 1.0 C C:VAL125 3.7 42.8 1.0 CD2 C:LEU124 3.9 47.2 1.0 CD2 C:LEU234 3.9 46.4 1.0 N C:TYR126 4.0 39.2 1.0 C C:C82501 4.0 60.2 1.0 C4 C:C82501 4.0 58.1 1.0 CG C:LEU124 4.0 46.0 1.0 SG C:CYS129 4.1 57.5 1.0 CA C:TYR126 4.3 39.4 1.0 O C:LEU124 4.3 44.3 1.0 CA C:VAL125 4.3 38.3 1.0 C C:GLY262 4.4 52.9 1.0 C C:LEU124 4.5 45.2 1.0 C5 C:C82501 4.5 56.0 1.0 N C:VAL125 4.5 40.5 1.0 N C:GLY262 4.5 46.7 1.0 CA C:CYS129 4.8 51.1 1.0 H1 C:C82501 4.8 60.6 1.0 H4 C:C82501 4.8 58.4 1.0 CB C:LEU124 4.8 41.1 1.0 CB C:LEU234 4.9 40.5 1.0 CG C:LEU234 4.9 44.2 1.0 N C:SER263 5.0 48.0 1.0 O C:GLY262 5.0 53.5 1.0

J.A.C.Alexandre, M.K.Swan, M.J.Latchem, D.Boyall, J.R.Pollard, S.W.Hughes, J.Westcott. New 4-Amino-1,2,3-Triazole Inhibitors of Indoleamine 2,3-Dioxygenase Form A Long-Lived Complex with the Enzyme and Display Exquisite Cellular Potency. Chembiochem V. 19 552 2018.
ISSN: ESSN 1439-7633
PubMed: 29240291
DOI: 10.1002/CBIC.201700560