Iron in PDB 8u5i: Crystal Structure of Human IDO1 Bound to Compound 23

All present enzymatic activity of Crystal Structure of Human IDO1 Bound to Compound 23:
1.13.11.52;

The structure of Crystal Structure of Human IDO1 Bound to Compound 23, PDB code: 8u5i was solved by S.Steinbacher, A.Lammens, S.F.Harris, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	45.31 / 2.17
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	84.862, 89.888, 133.52, 90, 90, 90
R / Rfree (%)	17.7 / 21.9

The binding sites of Iron atom in the Crystal Structure of Human IDO1 Bound to Compound 23 (pdb code 8u5i). 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 Human IDO1 Bound to Compound 23, PDB code: 8u5i:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in the Crystal Structure of Human IDO1 Bound to Compound 23


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 Human IDO1 Bound to Compound 23 within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe501 b:24.6 occ:1.00 FE A:HEM501 0.0 24.6 1.0 NC A:HEM501 2.0 28.7 1.0 NB A:HEM501 2.0 27.0 1.0 NA A:HEM501 2.0 21.7 1.0 N28 A:W2Z502 2.1 19.9 1.0 NE2 A:HIS346 2.1 20.6 1.0 ND A:HEM501 2.1 26.4 1.0 C27 A:W2Z502 3.0 20.1 1.0 C1C A:HEM501 3.0 28.1 1.0 C4C A:HEM501 3.0 30.3 1.0 C1B A:HEM501 3.0 26.6 1.0 C4B A:HEM501 3.0 26.7 1.0 C4A A:HEM501 3.1 25.0 1.0 CD2 A:HIS346 3.1 27.8 1.0 CE1 A:HIS346 3.1 24.8 1.0 C1A A:HEM501 3.1 26.2 1.0 C29 A:W2Z502 3.1 21.8 1.0 C1D A:HEM501 3.1 24.0 1.0 C4D A:HEM501 3.1 23.6 1.0 CHC A:HEM501 3.4 30.6 1.0 CHB A:HEM501 3.4 23.8 1.0 CHD A:HEM501 3.4 28.4 1.0 CHA A:HEM501 3.5 23.8 1.0 N26 A:W2Z502 4.1 19.6 1.0 ND1 A:HIS346 4.2 25.2 1.0 C25 A:W2Z502 4.2 20.1 1.0 CG A:HIS346 4.2 23.5 1.0 C2C A:HEM501 4.2 28.6 1.0 C3C A:HEM501 4.2 29.4 1.0 C2B A:HEM501 4.3 24.6 1.0 C3A A:HEM501 4.3 23.3 1.0 C3B A:HEM501 4.3 23.9 1.0 C2A A:HEM501 4.3 26.8 1.0 C2D A:HEM501 4.4 27.2 1.0 C3D A:HEM501 4.4 27.8 1.0 CB A:ALA264 4.7 28.3 1.0

Iron binding site 2 out of 2 in the Crystal Structure of Human IDO1 Bound to Compound 23


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 Human IDO1 Bound to Compound 23 within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe501 b:24.6 occ:1.00 FE B:HEM501 0.0 24.6 1.0 NC B:HEM501 2.0 21.3 1.0 NB B:HEM501 2.0 22.7 1.0 NA B:HEM501 2.0 19.9 1.0 ND B:HEM501 2.1 24.8 1.0 NE2 B:HIS346 2.1 22.3 1.0 N28 B:W2Z502 2.1 25.1 1.0 C27 B:W2Z502 3.0 20.7 1.0 C1C B:HEM501 3.0 20.7 1.0 C4B B:HEM501 3.0 21.2 1.0 C1A B:HEM501 3.0 22.1 1.0 C4C B:HEM501 3.0 22.4 1.0 CD2 B:HIS346 3.1 25.2 1.0 C4D B:HEM501 3.1 25.0 1.0 C1D B:HEM501 3.1 25.0 1.0 C1B B:HEM501 3.1 22.5 1.0 C4A B:HEM501 3.1 19.7 1.0 CE1 B:HIS346 3.1 23.5 1.0 C29 B:W2Z502 3.1 23.5 1.0 CHC B:HEM501 3.4 26.5 1.0 CHA B:HEM501 3.4 21.9 1.0 CHD B:HEM501 3.4 23.0 1.0 CHB B:HEM501 3.4 22.7 1.0 N26 B:W2Z502 4.2 24.4 1.0 ND1 B:HIS346 4.2 25.1 1.0 CG B:HIS346 4.2 24.9 1.0 C25 B:W2Z502 4.3 24.9 1.0 C2C B:HEM501 4.3 23.2 1.0 C3C B:HEM501 4.3 25.4 1.0 C2A B:HEM501 4.3 23.6 1.0 C3B B:HEM501 4.3 23.3 1.0 C3A B:HEM501 4.3 22.8 1.0 C2B B:HEM501 4.3 24.2 1.0 C3D B:HEM501 4.3 23.0 1.0 C2D B:HEM501 4.3 25.6 1.0 CB B:ALA264 4.6 23.8 1.0

R.Pastor, S.F.Harris. Exploiting Stereo-Complexity to Identify Spirocyclic Imidazoisoindoles As Potent and Orally Bioavailable Dual Inhibitors of Indoleamine-2,3-Dioxygenase and Tryptophan-2,3-Dioxygenase To Be Published.