Iron in PDB 7ah5: Crystal Structure of Indoleamine 2,3-Dioxygenase 1 (IDO1) in Complex with Ferric Heme and Mmg-0706

All present enzymatic activity of Crystal Structure of Indoleamine 2,3-Dioxygenase 1 (IDO1) in Complex with Ferric Heme and Mmg-0706:
1.13.11.52;

The structure of Crystal Structure of Indoleamine 2,3-Dioxygenase 1 (IDO1) in Complex with Ferric Heme and Mmg-0706, PDB code: 7ah5 was solved by U.F.Roehrig, A.Reynaud, F.Pojer, O.Michielin, V.Zoete, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	46.55 / 2.90
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	84.988, 93.106, 130.36, 90, 90, 90
R / Rfree (%)	23.1 / 29.2

The structure of Crystal Structure of Indoleamine 2,3-Dioxygenase 1 (IDO1) in Complex with Ferric Heme and Mmg-0706 also contains other interesting chemical elements:

Chlorine

(Cl)

4 atoms

The binding sites of Iron atom in the Crystal Structure of Indoleamine 2,3-Dioxygenase 1 (IDO1) in Complex with Ferric Heme and Mmg-0706 (pdb code 7ah5). 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-Dioxygenase 1 (IDO1) in Complex with Ferric Heme and Mmg-0706, PDB code: 7ah5:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in the Crystal Structure of Indoleamine 2,3-Dioxygenase 1 (IDO1) in Complex with Ferric Heme and Mmg-0706


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-Dioxygenase 1 (IDO1) in Complex with Ferric Heme and Mmg-0706 within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe501 b:62.2 occ:1.00 FE A:HEM501 0.0 62.2 1.0 N03 A:RCQ502 2.0 57.4 0.8 ND A:HEM501 2.0 54.7 1.0 NA A:HEM501 2.0 55.8 1.0 NB A:HEM501 2.1 60.6 1.0 NC A:HEM501 2.1 51.0 1.0 NE2 A:HIS346 2.5 58.7 1.0 N02 A:RCQ502 2.8 53.3 0.8 C4A A:HEM501 3.0 62.5 1.0 C1A A:HEM501 3.0 62.6 1.0 C08 A:RCQ502 3.0 57.8 0.8 C4D A:HEM501 3.0 58.9 1.0 C1D A:HEM501 3.0 57.0 1.0 C1B A:HEM501 3.1 60.4 1.0 C4C A:HEM501 3.1 54.2 1.0 C4B A:HEM501 3.1 54.0 1.0 C1C A:HEM501 3.2 51.5 1.0 CD2 A:HIS346 3.2 57.0 1.0 CHA A:HEM501 3.4 61.5 1.0 CHB A:HEM501 3.4 59.3 1.0 CHD A:HEM501 3.4 55.5 1.0 CHC A:HEM501 3.5 50.6 1.0 CE1 A:HIS346 3.6 61.5 1.0 C07 A:RCQ502 4.0 54.8 0.8 N04 A:RCQ502 4.1 57.8 0.8 C3A A:HEM501 4.1 64.6 1.0 C2A A:HEM501 4.2 63.8 1.0 C2D A:HEM501 4.2 59.9 1.0 C3D A:HEM501 4.2 58.7 1.0 C2B A:HEM501 4.3 64.2 1.0 C3C A:HEM501 4.3 58.8 1.0 C3B A:HEM501 4.3 58.6 1.0 C2C A:HEM501 4.4 56.1 1.0 CG A:HIS346 4.4 67.3 1.0 ND1 A:HIS346 4.5 71.2 1.0 CB A:ALA264 4.6 50.0 1.0

Iron binding site 2 out of 2 in the Crystal Structure of Indoleamine 2,3-Dioxygenase 1 (IDO1) in Complex with Ferric Heme and Mmg-0706


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-Dioxygenase 1 (IDO1) in Complex with Ferric Heme and Mmg-0706 within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe501 b:56.7 occ:0.93 FE B:HEM501 0.0 56.7 0.9 N03 B:RCQ502 1.9 55.7 0.9 NC B:HEM501 2.0 54.6 0.9 ND B:HEM501 2.0 53.3 0.9 NB B:HEM501 2.0 58.9 0.9 NA B:HEM501 2.1 52.6 0.9 NE2 B:HIS346 2.5 51.9 1.0 C08 B:RCQ502 2.8 51.8 0.9 N02 B:RCQ502 2.9 57.2 0.9 C4C B:HEM501 3.0 55.4 0.9 C1D B:HEM501 3.0 51.6 0.9 C4A B:HEM501 3.0 51.1 0.9 C1C B:HEM501 3.0 56.9 0.9 C1B B:HEM501 3.1 55.6 0.9 C4B B:HEM501 3.1 60.7 0.9 C1A B:HEM501 3.1 53.8 0.9 C4D B:HEM501 3.1 52.0 0.9 CD2 B:HIS346 3.3 55.6 1.0 CHD B:HEM501 3.4 54.6 0.9 CHB B:HEM501 3.4 54.5 0.9 CHC B:HEM501 3.5 57.5 0.9 CHA B:HEM501 3.5 51.7 0.9 CE1 B:HIS346 3.5 49.2 1.0 N04 B:RCQ502 3.9 54.2 0.9 C07 B:RCQ502 3.9 57.4 0.9 C3C B:HEM501 4.2 53.5 0.9 C2C B:HEM501 4.2 54.7 0.9 C3A B:HEM501 4.2 54.0 0.9 C2D B:HEM501 4.3 49.2 0.9 C2A B:HEM501 4.3 56.3 0.9 C2B B:HEM501 4.3 58.9 0.9 C3B B:HEM501 4.3 63.3 0.9 C3D B:HEM501 4.3 48.9 0.9 CG B:HIS346 4.5 59.9 1.0 ND1 B:HIS346 4.5 58.7 1.0 CB B:ALA264 4.6 54.8 1.0

U.F.Rohrig, S.R.Majjigapu, A.Reynaud, F.Pojer, N.Dilek, P.Reichenbach, K.Ascencao, M.Irving, G.Coukos, P.Vogel, O.Michielin, V.Zoete. Azole-Based Indoleamine 2,3-Dioxygenase 1 (IDO1) Inhibitors J.Med.Chem. 2021.
ISSN: ISSN 0022-2623
DOI: 10.1021/ACS.JMEDCHEM.0C01968