Iron in PDB 5xe1: Crystal Structure of the Indoleamine 2,3-Dioxygenagse 1 (IDO1) Complexed with INCB14943

All present enzymatic activity of Crystal Structure of the Indoleamine 2,3-Dioxygenagse 1 (IDO1) Complexed with INCB14943:
1.13.11.52;

The structure of Crystal Structure of the Indoleamine 2,3-Dioxygenagse 1 (IDO1) Complexed with INCB14943, PDB code: 5xe1 was solved by J.Xu, U.Wu, J.Liu, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	25.00 / 3.20
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	87.050, 97.380, 128.470, 90.00, 90.00, 90.00
R / Rfree (%)	22.8 / 27.4

The structure of Crystal Structure of the Indoleamine 2,3-Dioxygenagse 1 (IDO1) Complexed with INCB14943 also contains other interesting chemical elements:

Fluorine	(F)	2 atoms
Chlorine	(Cl)	2 atoms

The binding sites of Iron atom in the Crystal Structure of the Indoleamine 2,3-Dioxygenagse 1 (IDO1) Complexed with INCB14943 (pdb code 5xe1). 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 the Indoleamine 2,3-Dioxygenagse 1 (IDO1) Complexed with INCB14943, PDB code: 5xe1:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in the Crystal Structure of the Indoleamine 2,3-Dioxygenagse 1 (IDO1) Complexed with INCB14943


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 the Indoleamine 2,3-Dioxygenagse 1 (IDO1) Complexed with INCB14943 within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe501 b:84.9 occ:1.00 FE A:HEM501 0.0 84.9 1.0 ND A:HEM501 1.9 83.1 1.0 NAO A:IUU502 2.0 0.0 1.0 NE2 A:HIS346 2.0 89.8 1.0 NA A:HEM501 2.0 85.3 1.0 NB A:HEM501 2.1 80.8 1.0 NC A:HEM501 2.1 80.7 1.0 OAP A:IUU502 2.4 0.8 1.0 CE1 A:HIS346 2.8 88.6 1.0 C1D A:HEM501 2.9 81.4 1.0 C4D A:HEM501 2.9 83.1 1.0 C1A A:HEM501 3.0 85.9 1.0 C4B A:HEM501 3.0 79.2 1.0 C1B A:HEM501 3.0 81.8 1.0 CAG A:IUU502 3.0 0.5 1.0 C4A A:HEM501 3.1 84.1 1.0 C4C A:HEM501 3.1 81.0 1.0 C1C A:HEM501 3.1 80.5 1.0 CD2 A:HIS346 3.2 86.0 1.0 CHA A:HEM501 3.4 85.2 1.0 CHD A:HEM501 3.4 81.2 1.0 CHC A:HEM501 3.4 79.1 1.0 CHB A:HEM501 3.4 82.8 1.0 NAH A:IUU502 3.8 0.3 1.0 ND1 A:HIS346 4.0 88.2 1.0 CAA A:IUU502 4.0 0.1 1.0 C3D A:HEM501 4.2 80.6 1.0 C2D A:HEM501 4.2 80.5 1.0 C2A A:HEM501 4.2 86.8 1.0 CG A:HIS346 4.2 86.0 1.0 C3A A:HEM501 4.2 85.1 1.0 C2B A:HEM501 4.2 81.0 1.0 C3B A:HEM501 4.3 78.7 1.0 C3C A:HEM501 4.3 80.3 1.0 C2C A:HEM501 4.3 81.2 1.0 CB A:ALA264 4.4 86.9 1.0 NAF A:IUU502 4.7 0.5 1.0 CAB A:IUU502 4.7 0.2 1.0 NAE A:IUU502 5.0 0.8 1.0

Iron binding site 2 out of 2 in the Crystal Structure of the Indoleamine 2,3-Dioxygenagse 1 (IDO1) Complexed with INCB14943


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 the Indoleamine 2,3-Dioxygenagse 1 (IDO1) Complexed with INCB14943 within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe501 b:76.5 occ:1.00 FE B:HEM501 0.0 76.5 1.0 ND B:HEM501 1.9 77.5 1.0 NAO B:IUU502 2.0 99.2 1.0 NE2 B:HIS346 2.0 76.1 1.0 NA B:HEM501 2.0 77.4 1.0 NC B:HEM501 2.1 73.5 1.0 NB B:HEM501 2.1 75.9 1.0 OAP B:IUU502 2.2 0.4 1.0 CE1 B:HIS346 2.8 74.0 1.0 C4D B:HEM501 2.9 78.8 1.0 C1D B:HEM501 2.9 77.8 1.0 C1A B:HEM501 3.0 78.7 1.0 C4A B:HEM501 3.0 75.7 1.0 C4B B:HEM501 3.0 74.8 1.0 C4C B:HEM501 3.0 75.5 1.0 C1B B:HEM501 3.0 75.3 1.0 C1C B:HEM501 3.1 73.8 1.0 CAG B:IUU502 3.1 0.6 1.0 CD2 B:HIS346 3.2 73.2 1.0 CHA B:HEM501 3.4 78.7 1.0 CHD B:HEM501 3.4 77.1 1.0 CHC B:HEM501 3.4 74.1 1.0 CHB B:HEM501 3.4 74.7 1.0 NAH B:IUU502 3.9 0.5 1.0 CAA B:IUU502 4.0 100.0 1.0 ND1 B:HIS346 4.0 73.2 1.0 C3D B:HEM501 4.1 78.9 1.0 C2D B:HEM501 4.2 77.6 1.0 CG B:HIS346 4.2 72.2 1.0 C2A B:HEM501 4.2 79.5 1.0 C3A B:HEM501 4.2 77.7 1.0 C3C B:HEM501 4.2 75.2 1.0 C2C B:HEM501 4.2 74.4 1.0 C2B B:HEM501 4.3 74.7 1.0 C3B B:HEM501 4.3 74.8 1.0 NAF B:IUU502 4.4 99.4 1.0 CB B:ALA264 4.5 79.2 1.0 CAB B:IUU502 4.6 99.7 1.0

Y.Wu, T.Xu, J.Liu, K.Ding, J.Xu. Structural Insights Into the Binding Mechanism of IDO1 with Hydroxylamidine Based Inhibitor INCB14943 Biochem. Biophys. Res. V. 487 339 2017COMMUN..
ISSN: ESSN 1090-2104
PubMed: 28412361
DOI: 10.1016/J.BBRC.2017.04.061