Iron in PDB 7ah6: Crystal Structure of Indoleamine 2,3-Dioxygenase 1 (IDO1) in Complex with Ferric Heme and Mmg-0752

All present enzymatic activity of Crystal Structure of Indoleamine 2,3-Dioxygenase 1 (IDO1) in Complex with Ferric Heme and Mmg-0752:
1.13.11.52;

The structure of Crystal Structure of Indoleamine 2,3-Dioxygenase 1 (IDO1) in Complex with Ferric Heme and Mmg-0752, PDB code: 7ah6 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)	45.86 / 3.00
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	85.811, 91.723, 127.31, 90, 90, 90
R / Rfree (%)	22.2 / 27.6

The structure of Crystal Structure of Indoleamine 2,3-Dioxygenase 1 (IDO1) in Complex with Ferric Heme and Mmg-0752 also contains other interesting chemical elements:

Bromine

(Br)

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-0752 (pdb code 7ah6). 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-0752, PDB code: 7ah6:
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-0752


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-0752 within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe501 b:49.3 occ:1.00 FE A:HEM501 0.0 49.3 1.0 N9 A:RCW502 1.9 51.6 0.8 ND A:HEM501 2.0 46.3 1.0 NB A:HEM501 2.1 50.6 1.0 NC A:HEM501 2.1 51.3 1.0 NA A:HEM501 2.1 49.0 1.0 NE2 A:HIS346 2.5 47.1 1.0 N8 A:RCW502 2.8 47.4 0.8 C10 A:RCW502 3.0 49.7 0.8 C4D A:HEM501 3.0 46.1 1.0 C1D A:HEM501 3.0 50.1 1.0 C1A A:HEM501 3.1 48.8 1.0 C1C A:HEM501 3.1 50.3 1.0 C4B A:HEM501 3.1 51.2 1.0 C4A A:HEM501 3.1 49.1 1.0 C4C A:HEM501 3.1 49.1 1.0 C1B A:HEM501 3.1 46.8 1.0 CHA A:HEM501 3.4 44.8 1.0 CD2 A:HIS346 3.4 50.8 1.0 CHD A:HEM501 3.4 48.1 1.0 CE1 A:HIS346 3.4 53.6 1.0 CHC A:HEM501 3.4 46.6 1.0 CHB A:HEM501 3.5 46.4 1.0 C7 A:RCW502 3.9 45.7 0.8 N11 A:RCW502 4.0 47.3 0.8 C2D A:HEM501 4.2 46.5 1.0 C3D A:HEM501 4.2 46.9 1.0 C2A A:HEM501 4.3 50.4 1.0 C3A A:HEM501 4.3 50.5 1.0 C2C A:HEM501 4.3 50.6 1.0 C3C A:HEM501 4.3 46.9 1.0 C3B A:HEM501 4.3 57.8 1.0 C2B A:HEM501 4.3 52.8 1.0 ND1 A:HIS346 4.5 59.4 1.0 CG A:HIS346 4.5 59.8 1.0 CB A:ALA264 4.6 49.2 1.0 CG1 A:VAL350 5.0 53.6 1.0 N13 A:RCW502 5.0 42.1 0.8

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-0752


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-0752 within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe501 b:60.9 occ:1.00 FE B:HEM501 0.0 60.9 1.0 N9 B:RCW502 1.9 64.0 0.9 NC B:HEM501 2.0 57.1 1.0 ND B:HEM501 2.0 60.4 1.0 NA B:HEM501 2.0 59.2 1.0 NB B:HEM501 2.1 66.0 1.0 NE2 B:HIS346 2.5 60.6 1.0 N8 B:RCW502 2.8 57.6 0.9 C10 B:RCW502 2.9 58.1 0.9 C1C B:HEM501 3.0 56.1 1.0 C1D B:HEM501 3.0 62.3 1.0 C4D B:HEM501 3.0 61.3 1.0 C4A B:HEM501 3.1 62.8 1.0 C4C B:HEM501 3.1 58.3 1.0 C1A B:HEM501 3.1 61.8 1.0 C1B B:HEM501 3.1 68.0 1.0 C4B B:HEM501 3.1 61.9 1.0 CE1 B:HIS346 3.4 63.9 1.0 CD2 B:HIS346 3.4 61.0 1.0 CHD B:HEM501 3.4 59.8 1.0 CHA B:HEM501 3.4 62.2 1.0 CHB B:HEM501 3.4 66.7 1.0 CHC B:HEM501 3.4 57.8 1.0 C7 B:RCW502 3.9 54.5 0.9 N11 B:RCW502 4.0 57.1 0.9 C2C B:HEM501 4.2 58.6 1.0 C2D B:HEM501 4.2 64.5 1.0 C3D B:HEM501 4.2 61.2 1.0 C3C B:HEM501 4.2 56.9 1.0 C3A B:HEM501 4.3 64.7 1.0 C2A B:HEM501 4.3 62.7 1.0 C2B B:HEM501 4.3 66.9 1.0 C3B B:HEM501 4.3 65.3 1.0 ND1 B:HIS346 4.4 69.8 1.0 CG B:HIS346 4.5 70.0 1.0 CB B:ALA264 4.6 58.0 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