Iron in PDB 4pk5: Crystal Structure of the Indoleamine 2,3-Dioxygenagse 1 (IDO1) Complexed with Amg-1

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

The structure of Crystal Structure of the Indoleamine 2,3-Dioxygenagse 1 (IDO1) Complexed with Amg-1, PDB code: 4pk5 was solved by T.Kohno, S.Tojo, T.Ishii, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	74.55 / 2.79
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	84.799, 90.414, 131.757, 90.00, 90.00, 90.00
R / Rfree (%)	18.5 / 25.6

The binding sites of Iron atom in the Crystal Structure of the Indoleamine 2,3-Dioxygenagse 1 (IDO1) Complexed with Amg-1 (pdb code 4pk5). 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 Amg-1, PDB code: 4pk5:
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 Amg-1


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 Amg-1 within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe501 b:32.5 occ:1.00 FE A:HEM501 0.0 32.5 1.0 ND A:HEM501 1.9 29.0 1.0 NA A:HEM501 2.0 33.0 1.0 N17 A:PKJ502 2.0 34.8 1.0 NE2 A:HIS346 2.0 34.9 1.0 NC A:HEM501 2.1 31.3 1.0 NB A:HEM501 2.1 32.2 1.0 CE1 A:HIS346 2.8 30.7 1.0 N16 A:PKJ502 2.9 34.0 1.0 C4D A:HEM501 2.9 29.9 1.0 C1D A:HEM501 2.9 29.4 1.0 C1A A:HEM501 3.0 34.8 1.0 C4B A:HEM501 3.0 30.9 1.0 C4A A:HEM501 3.0 36.6 1.0 C4C A:HEM501 3.0 34.3 1.0 C1B A:HEM501 3.0 34.1 1.0 C1C A:HEM501 3.0 31.3 1.0 C18 A:PKJ502 3.1 33.5 1.0 CD2 A:HIS346 3.2 34.7 1.0 CHA A:HEM501 3.3 31.2 1.0 CHD A:HEM501 3.4 30.2 1.0 CHC A:HEM501 3.4 32.4 1.0 CHB A:HEM501 3.5 34.0 1.0 ND1 A:HIS346 4.0 30.1 1.0 C15 A:PKJ502 4.0 36.4 1.0 S19 A:PKJ502 4.1 37.9 1.0 C3D A:HEM501 4.2 32.6 1.0 C2D A:HEM501 4.2 30.5 1.0 CG A:HIS346 4.2 31.2 1.0 N22 A:PKJ502 4.2 34.5 1.0 C2A A:HEM501 4.2 35.5 1.0 C3A A:HEM501 4.2 37.5 1.0 C2C A:HEM501 4.2 32.0 1.0 C3C A:HEM501 4.2 35.3 1.0 C2B A:HEM501 4.3 31.4 1.0 C3B A:HEM501 4.3 31.0 1.0 CB A:ALA264 4.4 31.7 1.0

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


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 Amg-1 within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe501 b:38.4 occ:1.00 FE B:HEM501 0.0 38.4 1.0 ND B:HEM501 1.9 40.8 1.0 NE2 B:HIS346 1.9 37.2 1.0 NA B:HEM501 2.0 38.3 1.0 N17 B:PKJ502 2.0 38.4 1.0 NB B:HEM501 2.1 38.2 1.0 NC B:HEM501 2.1 37.9 1.0 CE1 B:HIS346 2.8 34.2 1.0 C1D B:HEM501 2.9 37.5 1.0 C4D B:HEM501 2.9 40.4 1.0 C1A B:HEM501 3.0 42.0 1.0 CD2 B:HIS346 3.0 34.4 1.0 N16 B:PKJ502 3.0 41.7 1.0 C18 B:PKJ502 3.0 37.4 1.0 C4A B:HEM501 3.0 40.7 1.0 C1B B:HEM501 3.0 40.2 1.0 C4C B:HEM501 3.0 40.0 1.0 C4B B:HEM501 3.0 38.9 1.0 C1C B:HEM501 3.1 38.8 1.0 CHD B:HEM501 3.4 37.6 1.0 CHA B:HEM501 3.4 38.7 1.0 CHB B:HEM501 3.4 41.4 1.0 CHC B:HEM501 3.5 38.0 1.0 S19 B:PKJ502 3.8 37.6 1.0 ND1 B:HIS346 4.0 36.5 1.0 CG B:HIS346 4.1 34.6 1.0 C15 B:PKJ502 4.1 43.5 1.0 N22 B:PKJ502 4.2 37.4 1.0 C3A B:HEM501 4.2 40.6 1.0 C2A B:HEM501 4.2 44.4 1.0 C2D B:HEM501 4.2 38.3 1.0 C3D B:HEM501 4.2 39.2 1.0 C2B B:HEM501 4.2 40.1 1.0 C3C B:HEM501 4.3 40.1 1.0 C3B B:HEM501 4.3 39.2 1.0 C2C B:HEM501 4.3 38.5 1.0 CB B:ALA264 4.3 37.9 1.0

S.Tojo, T.Kohno, T.Tanaka, S.Kamioka, Y.Ota, T.Ishii, K.Kamimoto, S.Asano, Y.Isobe. Crystal Structures and Structure-Activity Relationships of Imidazothiazole Derivatives As IDO1 Inhibitors. Acs Med.Chem.Lett. V. 5 1119 2014.
ISSN: ISSN 1948-5875
PubMed: 25313323
DOI: 10.1021/ML500247W