Iron 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:

Chlorine

(Cl)

2 atoms

The binding sites of Iron 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 Iron atom.
In total 2 binding sites of Iron 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 Iron binding site number: 1; 2;

Iron 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 Iron with other atoms in the Fe 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:Fe503 b:39.3 occ:1.00 FE A:HEM503 0.0 39.3 1.0 NA A:HEM503 1.9 39.5 1.0 NC A:HEM503 1.9 39.1 1.0 ND A:HEM503 2.0 39.4 1.0 NB A:HEM503 2.0 39.0 1.0 NE2 A:HIS346 2.2 46.9 1.0 N1 A:C82501 2.2 48.9 1.0 C1D A:HEM503 2.9 39.7 1.0 C1B A:HEM503 2.9 39.4 1.0 C4C A:HEM503 2.9 39.4 1.0 C4A A:HEM503 3.0 39.5 1.0 C1C A:HEM503 3.0 39.0 1.0 C4B A:HEM503 3.0 39.2 1.0 C4D A:HEM503 3.0 39.7 1.0 N2 A:C82501 3.0 48.5 1.0 C1A A:HEM503 3.0 39.7 1.0 CE1 A:HIS346 3.1 47.0 1.0 CD2 A:HIS346 3.2 46.6 1.0 C7 A:C82501 3.3 48.9 1.0 CHB A:HEM503 3.3 39.8 1.0 CHD A:HEM503 3.3 40.1 1.0 CHC A:HEM503 3.4 39.8 1.0 CHA A:HEM503 3.5 40.1 1.0 H6 A:C82501 3.5 48.6 1.0 C3C A:HEM503 4.2 39.8 1.0 C2C A:HEM503 4.2 39.6 1.0 C3A A:HEM503 4.2 40.0 1.0 C2D A:HEM503 4.2 40.1 1.0 C2B A:HEM503 4.2 39.5 1.0 C2A A:HEM503 4.2 40.1 1.0 N3 A:C82501 4.2 50.0 1.0 C3D A:HEM503 4.2 40.2 1.0 ND1 A:HIS346 4.3 47.9 1.0 CG A:HIS346 4.3 45.5 1.0 C3B A:HEM503 4.3 39.7 1.0 C6 A:C82501 4.4 48.7 1.0 CB A:ALA264 4.6 38.2 1.0 N A:ALA502 5.0 38.7 1.0

Iron 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 Iron with other atoms in the Fe 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:Fe503 b:39.8 occ:1.00 FE C:HEM503 0.0 39.8 1.0 NB C:HEM503 1.9 39.5 1.0 NC C:HEM503 1.9 39.7 1.0 NA C:HEM503 1.9 39.9 1.0 ND C:HEM503 2.0 39.8 1.0 NE2 C:HIS346 2.1 43.2 1.0 N1 C:C82501 2.3 48.6 1.0 C1B C:HEM503 2.9 39.9 1.0 C4A C:HEM503 2.9 39.9 1.0 C4B C:HEM503 3.0 39.8 1.0 C1C C:HEM503 3.0 39.6 1.0 C1D C:HEM503 3.0 40.1 1.0 C4C C:HEM503 3.0 39.9 1.0 CE1 C:HIS346 3.0 42.8 1.0 C1A C:HEM503 3.1 40.1 1.0 C4D C:HEM503 3.1 40.1 1.0 CD2 C:HIS346 3.1 44.0 1.0 N2 C:C82501 3.1 47.1 1.0 C7 C:C82501 3.3 48.1 1.0 CHB C:HEM503 3.3 40.3 1.0 CHC C:HEM503 3.4 40.3 1.0 CHD C:HEM503 3.4 40.6 1.0 H6 C:C82501 3.5 48.6 1.0 CHA C:HEM503 3.5 40.5 1.0 C2C C:HEM503 4.2 40.2 1.0 C2B C:HEM503 4.2 40.0 1.0 ND1 C:HIS346 4.2 44.3 1.0 C3C C:HEM503 4.2 40.2 1.0 C3A C:HEM503 4.2 40.5 1.0 CG C:HIS346 4.2 43.2 1.0 C3B C:HEM503 4.2 40.2 1.0 C2A C:HEM503 4.3 40.6 1.0 C2D C:HEM503 4.3 40.6 1.0 N3 C:C82501 4.3 48.6 1.0 C3D C:HEM503 4.3 40.6 1.0 C6 C:C82501 4.4 49.1 1.0 CB C:ALA264 4.7 46.2 1.0 N C:ALA502 5.0 44.2 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