Iron in PDB 6kw7: Crystal Structure of Indoleamine 2,3-Dioxygenagse 1 (IDO1) in Complex with Compound 12

All present enzymatic activity of Crystal Structure of Indoleamine 2,3-Dioxygenagse 1 (IDO1) in Complex with Compound 12:
1.13.11.52;

The structure of Crystal Structure of Indoleamine 2,3-Dioxygenagse 1 (IDO1) in Complex with Compound 12, PDB code: 6kw7 was solved by Y.H.Peng, S.Y.Wu, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	29.50 / 3.02
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	85.466, 91.982, 129.158, 90.00, 90.00, 90.00
R / Rfree (%)	20.4 / 25.1

The structure of Crystal Structure of Indoleamine 2,3-Dioxygenagse 1 (IDO1) in Complex with Compound 12 also contains other interesting chemical elements:

Bromine

(Br)

2 atoms

The binding sites of Iron atom in the Crystal Structure of Indoleamine 2,3-Dioxygenagse 1 (IDO1) in Complex with Compound 12 (pdb code 6kw7). 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 Indoleamine 2,3-Dioxygenagse 1 (IDO1) in Complex with Compound 12, PDB code: 6kw7:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in the Crystal Structure of Indoleamine 2,3-Dioxygenagse 1 (IDO1) in Complex with Compound 12


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 Indoleamine 2,3-Dioxygenagse 1 (IDO1) in Complex with Compound 12 within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe501 b:70.7 occ:1.00 FE A:HEM501 0.0 70.7 1.0 NC A:HEM501 2.0 76.2 1.0 ND A:HEM501 2.0 79.5 1.0 NB A:HEM501 2.1 78.3 1.0 NA A:HEM501 2.1 79.0 1.0 NAC A:DYC502 2.4 77.8 1.0 NE2 A:HIS346 2.4 73.5 1.0 C1D A:HEM501 3.0 75.1 1.0 C4C A:HEM501 3.0 75.7 1.0 C1C A:HEM501 3.0 72.8 1.0 C4D A:HEM501 3.1 76.3 1.0 C4B A:HEM501 3.1 75.6 1.0 CD2 A:HIS346 3.1 71.3 1.0 C1B A:HEM501 3.1 76.2 1.0 C4A A:HEM501 3.1 77.4 1.0 C1A A:HEM501 3.1 82.0 1.0 CAB A:DYC502 3.2 75.1 1.0 CAD A:DYC502 3.3 80.9 1.0 CHD A:HEM501 3.4 74.1 1.0 CE1 A:HIS346 3.4 74.0 1.0 CHC A:HEM501 3.4 73.7 1.0 CHA A:HEM501 3.5 77.4 1.0 CHB A:HEM501 3.5 75.4 1.0 SAH A:DYC502 4.0 78.3 1.0 C2D A:HEM501 4.2 71.0 1.0 C2C A:HEM501 4.3 72.3 1.0 C3D A:HEM501 4.3 71.4 1.0 C3C A:HEM501 4.3 70.5 1.0 CG A:HIS346 4.3 75.4 1.0 C2B A:HEM501 4.3 80.3 1.0 C3B A:HEM501 4.3 78.0 1.0 C3A A:HEM501 4.4 80.0 1.0 C2A A:HEM501 4.4 82.7 1.0 NAA A:DYC502 4.4 80.7 1.0 CAE A:DYC502 4.4 81.5 1.0 ND1 A:HIS346 4.4 80.9 1.0 CB A:ALA264 4.4 71.5 1.0

Iron binding site 2 out of 2 in the Crystal Structure of Indoleamine 2,3-Dioxygenagse 1 (IDO1) in Complex with Compound 12


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 Indoleamine 2,3-Dioxygenagse 1 (IDO1) in Complex with Compound 12 within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe501 b:67.2 occ:1.00 FE B:HEM501 0.0 67.2 1.0 ND B:HEM501 2.0 68.3 1.0 NB B:HEM501 2.1 66.5 1.0 NA B:HEM501 2.1 63.6 1.0 NC B:HEM501 2.1 71.5 1.0 NE2 B:HIS346 2.4 64.3 1.0 NAC B:DYC502 2.4 68.6 1.0 CE1 B:HIS346 2.9 65.1 1.0 C4D B:HEM501 3.0 66.9 1.0 C1D B:HEM501 3.1 69.4 1.0 C1A B:HEM501 3.1 68.9 1.0 C1C B:HEM501 3.1 67.0 1.0 C4B B:HEM501 3.1 66.7 1.0 C4C B:HEM501 3.1 68.6 1.0 C1B B:HEM501 3.1 69.5 1.0 C4A B:HEM501 3.1 65.8 1.0 CAD B:DYC502 3.3 66.6 1.0 CAB B:DYC502 3.4 65.3 1.0 CHA B:HEM501 3.4 68.1 1.0 CHC B:HEM501 3.4 66.7 1.0 CHD B:HEM501 3.4 69.1 1.0 CHB B:HEM501 3.5 66.7 1.0 CD2 B:HIS346 3.5 63.2 1.0 ND1 B:HIS346 4.1 67.0 1.0 SAH B:DYC502 4.2 62.6 1.0 C3D B:HEM501 4.2 63.7 1.0 C2D B:HEM501 4.3 66.4 1.0 C2C B:HEM501 4.3 62.7 1.0 C2A B:HEM501 4.3 69.0 1.0 C3C B:HEM501 4.3 61.6 1.0 C3B B:HEM501 4.3 69.0 1.0 C3A B:HEM501 4.3 64.7 1.0 C2B B:HEM501 4.3 72.1 1.0 CG B:HIS346 4.4 69.3 1.0 CB B:ALA264 4.4 60.6 1.0 CAE B:DYC502 4.4 67.4 1.0 NAA B:DYC502 4.5 69.7 1.0

Y.H.Peng, F.Y.Liao, C.T.Tseng, R.Kuppusamy, A.S.Li, C.H.Chen, Y.S.Fan, S.Y.Wang, M.H.Wu, C.C.Hsueh, J.Y.Chang, L.C.Lee, C.Shih, K.S.Shia, T.K.Yeh, M.S.Hung, C.C.Kuo, J.S.Song, S.Y.Wu, S.H.Ueng. Unique Sulfur-Aromatic Interactions Contribute to the Binding of Potent Imidazothiazole Indoleamine 2,3-Dioxygenase Inhibitors. J.Med.Chem. V. 63 1642 2020.
ISSN: ISSN 0022-2623
PubMed: 31961685
DOI: 10.1021/ACS.JMEDCHEM.9B01549