Iron in PDB 7ah4: Crystal Structure of Indoleamine 2,3-Dioxygenase 1 (IDO1) in Complex with Ferric Heme and Mmg-0363

All present enzymatic activity of Crystal Structure of Indoleamine 2,3-Dioxygenase 1 (IDO1) in Complex with Ferric Heme and Mmg-0363:
1.13.11.52;

The structure of Crystal Structure of Indoleamine 2,3-Dioxygenase 1 (IDO1) in Complex with Ferric Heme and Mmg-0363, PDB code: 7ah4 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)	48.71 / 2.40
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	86.571, 97.422, 131.739, 90, 90, 90
R / Rfree (%)	21.4 / 24.9

The structure of Crystal Structure of Indoleamine 2,3-Dioxygenase 1 (IDO1) in Complex with Ferric Heme and Mmg-0363 also contains other interesting chemical elements:

Chlorine

(Cl)

6 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-0363 (pdb code 7ah4). 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-0363, PDB code: 7ah4:
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-0363


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-0363 within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe501 b:54.0 occ:0.96 FE A:HEM501 0.0 54.0 1.0 N9 A:RCN502 1.9 49.2 0.8 NA A:HEM501 2.0 52.4 1.0 ND A:HEM501 2.0 51.3 1.0 NB A:HEM501 2.1 51.8 1.0 NC A:HEM501 2.1 48.8 1.0 NE2 A:HIS346 2.6 56.7 1.0 N10 A:RCN502 2.8 47.8 0.8 C8 A:RCN502 2.9 45.9 0.8 C4A A:HEM501 3.0 51.8 1.0 C1D A:HEM501 3.0 49.2 1.0 C1B A:HEM501 3.0 48.8 1.0 C4C A:HEM501 3.0 49.1 1.0 C1C A:HEM501 3.1 49.1 1.0 C4D A:HEM501 3.1 51.6 1.0 C1A A:HEM501 3.1 52.3 1.0 C4B A:HEM501 3.1 50.1 1.0 CHB A:HEM501 3.4 48.1 1.0 CHD A:HEM501 3.4 47.0 1.0 CD2 A:HIS346 3.4 49.3 1.0 CHA A:HEM501 3.5 51.5 1.0 CHC A:HEM501 3.5 47.1 1.0 CE1 A:HIS346 3.7 50.5 1.0 N11 A:RCN502 4.0 55.7 0.8 C7 A:RCN502 4.1 53.1 0.8 C3A A:HEM501 4.2 51.6 1.0 C2D A:HEM501 4.2 47.6 1.0 C3C A:HEM501 4.3 48.0 1.0 C2C A:HEM501 4.3 50.5 1.0 C3D A:HEM501 4.3 48.3 1.0 C2B A:HEM501 4.3 50.6 1.0 C2A A:HEM501 4.3 54.5 1.0 C3B A:HEM501 4.3 49.1 1.0 CB A:ALA264 4.6 50.6 1.0 CG A:HIS346 4.7 52.2 1.0 ND1 A:HIS346 4.7 60.2 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-0363


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-0363 within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe501 b:42.6 occ:0.95 FE B:HEM501 0.0 42.6 0.9 N9 B:RCN502 1.8 45.1 0.9 ND B:HEM501 2.0 48.7 0.9 NB B:HEM501 2.0 48.7 0.9 NC B:HEM501 2.1 43.7 0.9 NA B:HEM501 2.1 45.4 0.9 NE2 B:HIS346 2.5 45.4 1.0 C8 B:RCN502 2.8 38.5 0.9 N10 B:RCN502 2.8 40.2 0.9 C1D B:HEM501 3.0 45.8 0.9 C4A B:HEM501 3.1 45.9 0.9 C4C B:HEM501 3.1 47.0 0.9 C1C B:HEM501 3.1 47.1 0.9 C1B B:HEM501 3.1 45.1 0.9 C4D B:HEM501 3.1 43.1 0.9 C4B B:HEM501 3.1 39.4 0.9 C1A B:HEM501 3.1 47.7 0.9 CHD B:HEM501 3.4 47.7 0.9 CE1 B:HIS346 3.4 42.1 1.0 CHB B:HEM501 3.4 40.5 0.9 CD2 B:HIS346 3.4 44.8 1.0 CHC B:HEM501 3.5 44.2 0.9 CHA B:HEM501 3.5 45.4 0.9 N11 B:RCN502 3.9 51.1 0.9 C7 B:RCN502 3.9 46.9 0.9 C2D B:HEM501 4.3 46.3 0.9 C2C B:HEM501 4.3 49.0 0.9 C3C B:HEM501 4.3 47.9 0.9 C3A B:HEM501 4.3 45.3 0.9 C3D B:HEM501 4.3 43.8 0.9 C2B B:HEM501 4.3 45.7 0.9 C3B B:HEM501 4.3 43.0 0.9 C2A B:HEM501 4.3 45.1 0.9 ND1 B:HIS346 4.5 41.4 1.0 CG B:HIS346 4.6 40.6 1.0 CB B:ALA264 4.9 44.0 1.0 O B:HOH603 5.0 47.2 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