Iron in PDB 6kps: Crystal Structure of Indoleamine 2,3-Dioxygenagse 1 (IDO1) in Complex with Compound 36

All present enzymatic activity of Crystal Structure of Indoleamine 2,3-Dioxygenagse 1 (IDO1) in Complex with Compound 36:
1.13.11.52;

The structure of Crystal Structure of Indoleamine 2,3-Dioxygenagse 1 (IDO1) in Complex with Compound 36, PDB code: 6kps 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)	29.74 / 2.25
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	85.693, 92.555, 130.661, 90.00, 90.00, 90.00
R / Rfree (%)	20.4 / 24.3

The binding sites of Iron atom in the Crystal Structure of Indoleamine 2,3-Dioxygenagse 1 (IDO1) in Complex with Compound 36 (pdb code 6kps). 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 36, PDB code: 6kps:
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 36


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 36 within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe501 b:49.8 occ:1.00 FE A:HEM501 0.0 49.8 1.0 NA A:HEM501 2.0 50.8 1.0 NB A:HEM501 2.1 43.7 1.0 ND A:HEM501 2.1 46.5 1.0 NC A:HEM501 2.1 43.9 1.0 N06 A:DU6502 2.3 47.5 1.0 NE2 A:HIS346 2.3 44.7 1.0 C1B A:HEM501 3.0 44.5 1.0 C4A A:HEM501 3.0 50.2 1.0 C1D A:HEM501 3.1 46.3 1.0 C1A A:HEM501 3.1 52.5 1.0 C4B A:HEM501 3.1 45.9 1.0 C4C A:HEM501 3.1 47.1 1.0 C4D A:HEM501 3.1 47.6 1.0 C05 A:DU6502 3.2 46.1 1.0 C1C A:HEM501 3.2 44.7 1.0 CD2 A:HIS346 3.2 43.4 1.0 C07 A:DU6502 3.2 49.2 1.0 CE1 A:HIS346 3.3 42.9 1.0 CHB A:HEM501 3.4 46.8 1.0 CHD A:HEM501 3.4 47.4 1.0 CHA A:HEM501 3.5 49.2 1.0 CHC A:HEM501 3.5 43.4 1.0 S04 A:DU6502 4.0 48.7 1.0 C3A A:HEM501 4.3 49.4 1.0 C2B A:HEM501 4.3 49.4 1.0 CB A:ALA264 4.3 45.3 1.0 C2A A:HEM501 4.3 49.0 1.0 N01 A:DU6502 4.3 47.4 1.0 C2D A:HEM501 4.3 48.4 1.0 C3B A:HEM501 4.3 48.5 1.0 CG A:HIS346 4.3 43.0 1.0 C3D A:HEM501 4.3 48.4 1.0 C3C A:HEM501 4.4 46.4 1.0 C2C A:HEM501 4.4 46.5 1.0 C08 A:DU6502 4.4 47.0 1.0 ND1 A:HIS346 4.4 44.2 1.0

Iron binding site 2 out of 2 in the Crystal Structure of Indoleamine 2,3-Dioxygenagse 1 (IDO1) in Complex with Compound 36


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 36 within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe501 b:45.4 occ:1.00 FE B:HEM501 0.0 45.4 1.0 NA B:HEM501 2.0 44.6 1.0 ND B:HEM501 2.0 44.1 1.0 NB B:HEM501 2.1 43.3 1.0 NC B:HEM501 2.1 43.4 1.0 NE2 B:HIS346 2.2 42.5 1.0 N06 B:DU6502 2.3 45.5 1.0 C4A B:HEM501 3.0 46.4 1.0 C1A B:HEM501 3.1 49.8 1.0 C1D B:HEM501 3.1 41.0 1.0 CD2 B:HIS346 3.1 41.8 1.0 C4D B:HEM501 3.1 42.8 1.0 C1B B:HEM501 3.1 42.9 1.0 C4B B:HEM501 3.1 42.5 1.0 C1C B:HEM501 3.1 41.8 1.0 C4C B:HEM501 3.1 39.8 1.0 C05 B:DU6502 3.2 42.7 1.0 C07 B:DU6502 3.3 46.5 1.0 CE1 B:HIS346 3.3 43.3 1.0 CHB B:HEM501 3.4 43.8 1.0 CHA B:HEM501 3.4 39.8 1.0 CHD B:HEM501 3.4 41.0 1.0 CHC B:HEM501 3.5 38.5 1.0 S04 B:DU6502 4.0 40.8 1.0 C3A B:HEM501 4.2 45.3 1.0 CG B:HIS346 4.3 43.9 1.0 C2A B:HEM501 4.3 49.4 1.0 CB B:ALA264 4.3 39.1 1.0 C2D B:HEM501 4.3 40.9 1.0 C3D B:HEM501 4.3 42.2 1.0 C2B B:HEM501 4.3 46.7 1.0 C3B B:HEM501 4.3 44.1 1.0 C2C B:HEM501 4.3 42.2 1.0 C3C B:HEM501 4.3 41.1 1.0 ND1 B:HIS346 4.3 45.6 1.0 N01 B:DU6502 4.4 46.4 1.0 C08 B:DU6502 4.4 41.6 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