Iron in PDB 6kof: Crystal Structure of Indoleamine 2,3-Dioxygenagse 1 (IDO1) in Complex with Compound 47

All present enzymatic activity of Crystal Structure of Indoleamine 2,3-Dioxygenagse 1 (IDO1) in Complex with Compound 47:
1.13.11.52;

The structure of Crystal Structure of Indoleamine 2,3-Dioxygenagse 1 (IDO1) in Complex with Compound 47, PDB code: 6kof 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)	29.68 / 2.26
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	85.423, 92.571, 130.133, 90.00, 90.00, 90.00
R / Rfree (%)	19.5 / 22.7

The binding sites of Iron atom in the Crystal Structure of Indoleamine 2,3-Dioxygenagse 1 (IDO1) in Complex with Compound 47 (pdb code 6kof). 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 47, PDB code: 6kof:
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 47


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 47 within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe501 b:42.1 occ:1.00 FE A:HEM501 0.0 42.1 1.0 ND A:HEM501 2.0 42.5 1.0 NC A:HEM501 2.0 41.6 1.0 NB A:HEM501 2.1 41.3 1.0 NA A:HEM501 2.1 48.4 1.0 N06 A:DO9502 2.4 43.5 1.0 NE2 A:HIS346 2.4 42.3 1.0 C1D A:HEM501 3.0 38.2 1.0 C4C A:HEM501 3.1 41.0 1.0 C4A A:HEM501 3.1 43.1 1.0 C1B A:HEM501 3.1 41.0 1.0 C1C A:HEM501 3.1 43.7 1.0 C4B A:HEM501 3.1 44.5 1.0 C4D A:HEM501 3.1 43.3 1.0 C1A A:HEM501 3.1 46.8 1.0 CD2 A:HIS346 3.1 39.6 1.0 C05 A:DO9502 3.2 41.4 1.0 CHD A:HEM501 3.4 36.4 1.0 CHB A:HEM501 3.4 40.4 1.0 CHC A:HEM501 3.4 38.0 1.0 CHA A:HEM501 3.5 42.9 1.0 C07 A:DO9502 3.5 42.4 1.0 CE1 A:HIS346 3.5 36.9 1.0 S04 A:DO9502 3.9 40.8 1.0 C2D A:HEM501 4.3 45.6 1.0 C3C A:HEM501 4.3 44.6 1.0 C2C A:HEM501 4.3 45.2 1.0 C3A A:HEM501 4.3 41.0 1.0 C3D A:HEM501 4.3 49.6 1.0 C2B A:HEM501 4.3 44.9 1.0 C2A A:HEM501 4.3 47.1 1.0 C3B A:HEM501 4.3 45.5 1.0 CB A:ALA264 4.3 40.4 1.0 CG A:HIS346 4.4 40.0 1.0 N01 A:DO9502 4.4 48.0 1.0 ND1 A:HIS346 4.5 47.7 1.0 C08 A:DO9502 4.6 41.5 1.0

Iron binding site 2 out of 2 in the Crystal Structure of Indoleamine 2,3-Dioxygenagse 1 (IDO1) in Complex with Compound 47


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 47 within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe501 b:39.1 occ:1.00 FE B:HEM501 0.0 39.1 1.0 NB B:HEM501 2.0 42.1 1.0 ND B:HEM501 2.1 40.4 1.0 NA B:HEM501 2.1 42.7 1.0 NC B:HEM501 2.1 42.7 1.0 NE2 B:HIS346 2.4 41.1 1.0 N06 B:DO9502 2.4 38.7 1.0 C1B B:HEM501 3.0 44.4 1.0 C1D B:HEM501 3.0 37.2 1.0 C4A B:HEM501 3.1 40.0 1.0 C4B B:HEM501 3.1 35.9 1.0 C4C B:HEM501 3.1 36.6 1.0 C1C B:HEM501 3.1 35.7 1.0 C4D B:HEM501 3.1 43.8 1.0 CD2 B:HIS346 3.1 35.3 1.0 C1A B:HEM501 3.1 44.1 1.0 C05 B:DO9502 3.3 41.3 1.0 C07 B:DO9502 3.4 39.4 1.0 CHD B:HEM501 3.4 32.5 1.0 CHB B:HEM501 3.4 36.0 1.0 CHC B:HEM501 3.4 37.5 1.0 CHA B:HEM501 3.5 35.7 1.0 CE1 B:HIS346 3.5 42.6 1.0 S04 B:DO9502 4.1 38.0 1.0 C2B B:HEM501 4.3 44.6 1.0 C2D B:HEM501 4.3 44.1 1.0 C3B B:HEM501 4.3 43.1 1.0 C3A B:HEM501 4.3 38.6 1.0 C2C B:HEM501 4.3 42.2 1.0 C3C B:HEM501 4.3 38.5 1.0 C3D B:HEM501 4.3 46.1 1.0 C2A B:HEM501 4.3 35.9 1.0 CG B:HIS346 4.3 39.8 1.0 CB B:ALA264 4.4 37.9 1.0 N01 B:DO9502 4.4 41.9 1.0 ND1 B:HIS346 4.5 44.6 1.0 C08 B:DO9502 4.5 38.1 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