Iron in PDB 7m7d: Crystal Structure of the Indoleamine 2,3-Dioxygenagse 1 (IDO1) Complexed with Iacs-8968

All present enzymatic activity of Crystal Structure of the Indoleamine 2,3-Dioxygenagse 1 (IDO1) Complexed with Iacs-8968:
1.13.11.52;

The structure of Crystal Structure of the Indoleamine 2,3-Dioxygenagse 1 (IDO1) Complexed with Iacs-8968, PDB code: 7m7d was solved by P.G.Leonard, J.B.Cross, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	33.29 / 2.60
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	85.86, 91.79, 128.78, 90, 90, 90
R / Rfree (%)	20.9 / 23.5

The structure of Crystal Structure of the Indoleamine 2,3-Dioxygenagse 1 (IDO1) Complexed with Iacs-8968 also contains other interesting chemical elements:

Fluorine

(F)

6 atoms

The binding sites of Iron atom in the Crystal Structure of the Indoleamine 2,3-Dioxygenagse 1 (IDO1) Complexed with Iacs-8968 (pdb code 7m7d). 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 Iacs-8968, PDB code: 7m7d:
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 Iacs-8968


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 Iacs-8968 within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe502 b:49.4 occ:1.00 FE A:HEM502 0.0 49.4 1.0 NC A:HEM502 2.1 42.0 1.0 NA A:HEM502 2.1 46.2 1.0 NB A:HEM502 2.1 46.4 1.0 ND A:HEM502 2.1 41.5 1.0 N16 A:YRM501 2.2 47.0 1.0 NE2 A:HIS346 2.5 51.3 1.0 C4C A:HEM502 3.1 41.0 1.0 C1C A:HEM502 3.1 46.0 1.0 C15 A:YRM501 3.1 49.7 1.0 CD2 A:HIS346 3.1 51.8 1.0 C1D A:HEM502 3.1 47.3 1.0 C4B A:HEM502 3.1 45.9 1.0 C1A A:HEM502 3.1 48.5 1.0 C4A A:HEM502 3.2 46.3 1.0 C4D A:HEM502 3.2 45.6 1.0 C1B A:HEM502 3.2 44.6 1.0 C17 A:YRM501 3.3 49.9 1.0 CHD A:HEM502 3.5 50.1 1.0 CHC A:HEM502 3.5 43.8 1.0 CHA A:HEM502 3.5 49.7 1.0 CHB A:HEM502 3.6 45.8 1.0 CE1 A:HIS346 3.7 54.3 1.0 N10 A:YRM501 4.3 56.4 1.0 C3C A:HEM502 4.3 46.9 1.0 C11 A:YRM501 4.4 55.6 1.0 C2C A:HEM502 4.4 49.5 1.0 CG A:HIS346 4.4 60.6 1.0 C3B A:HEM502 4.4 41.8 1.0 C2A A:HEM502 4.4 47.3 1.0 C3A A:HEM502 4.4 47.1 1.0 C2B A:HEM502 4.4 51.6 1.0 C2D A:HEM502 4.4 52.1 1.0 C3D A:HEM502 4.4 49.5 1.0 ND1 A:HIS346 4.6 64.4 1.0 CB A:ALA264 4.8 46.4 1.0

Iron binding site 2 out of 2 in the Crystal Structure of the Indoleamine 2,3-Dioxygenagse 1 (IDO1) Complexed with Iacs-8968


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 Iacs-8968 within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe502 b:49.8 occ:1.00 FE B:HEM502 0.0 49.8 1.0 NC B:HEM502 2.1 61.1 1.0 NA B:HEM502 2.1 54.9 1.0 NB B:HEM502 2.1 62.0 1.0 ND B:HEM502 2.1 57.3 1.0 N16 B:YRM501 2.3 59.8 1.0 NE2 B:HIS346 2.4 60.8 1.0 C4C B:HEM502 3.1 62.8 1.0 C1A B:HEM502 3.1 54.5 1.0 C1C B:HEM502 3.1 62.2 1.0 C4B B:HEM502 3.2 60.0 1.0 C1D B:HEM502 3.2 56.2 1.0 C15 B:YRM501 3.2 55.9 1.0 C4A B:HEM502 3.2 56.1 1.0 C4D B:HEM502 3.2 53.7 1.0 C1B B:HEM502 3.2 60.4 1.0 CE1 B:HIS346 3.3 54.4 1.0 CD2 B:HIS346 3.4 58.5 1.0 C17 B:YRM501 3.4 58.9 1.0 CHD B:HEM502 3.5 59.9 1.0 CHA B:HEM502 3.5 52.7 1.0 CHC B:HEM502 3.5 60.7 1.0 CHB B:HEM502 3.6 60.7 1.0 N10 B:YRM501 4.4 65.5 1.0 ND1 B:HIS346 4.4 61.3 1.0 C3C B:HEM502 4.4 63.5 1.0 C2C B:HEM502 4.4 61.7 1.0 C2A B:HEM502 4.4 57.7 1.0 C3A B:HEM502 4.4 57.3 1.0 C3B B:HEM502 4.4 63.7 1.0 C2B B:HEM502 4.4 62.2 1.0 C2D B:HEM502 4.4 50.1 1.0 C3D B:HEM502 4.4 53.8 1.0 CG B:HIS346 4.5 57.6 1.0 C11 B:YRM501 4.5 63.0 1.0 CB B:ALA264 4.8 49.9 1.0

M.M.Hamilton, F.Mseeh, T.J.Mcafoos, P.G.Leonard, N.J.Reyna, A.L.Harris, A.Xu, M.Han, M.J.Soth, B.Czako, J.P.Theroff, P.K.Mandal, J.P.Burke, B.Virgin-Downey, A.Petrocchi, D.Pfaffinger, N.E.Rogers, C.A.Parker, S.S.Yu, Y.Jiang, S.Krapp, A.Lammens, G.Trevitt, M.R.Tremblay, K.Mikule, K.Wilcoxen, J.B.Cross, P.Jones, J.R.Marszalek, R.T.Lewis. Discovery of Iacs-9779 and Iacs-70465 As Potent Inhibitors Targeting Indoleamine 2,3-Dioxygenase 1 (IDO1) Apoenzyme. J.Med.Chem. V. 64 11302 2021.
ISSN: ISSN 0022-2623
PubMed: 34292726
DOI: 10.1021/ACS.JMEDCHEM.1C00679