Iron in PDB 7zv3: Crystal Structure of Indoleamine 2,3-Dioxygenase 1 (IDO1) in Complex with Ferric Heme and Mmg-0472

All present enzymatic activity of Crystal Structure of Indoleamine 2,3-Dioxygenase 1 (IDO1) in Complex with Ferric Heme and Mmg-0472:
1.13.11.52;

The structure of Crystal Structure of Indoleamine 2,3-Dioxygenase 1 (IDO1) in Complex with Ferric Heme and Mmg-0472, PDB code: 7zv3 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 / 2.55
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	86.65, 97.419, 131.996, 90, 90, 90
R / Rfree (%)	19.1 / 24.1

The structure of Crystal Structure of Indoleamine 2,3-Dioxygenase 1 (IDO1) in Complex with Ferric Heme and Mmg-0472 also contains other interesting chemical elements:

Chlorine

(Cl)

2 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-0472 (pdb code 7zv3). 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-0472, PDB code: 7zv3:
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-0472


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-0472 within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe501 b:64.0 occ:0.87 FE A:HEM501 0.0 64.0 0.9 N11 A:RCT502 2.0 68.7 1.0 NB A:HEM501 2.0 64.0 0.9 NA A:HEM501 2.1 59.8 0.9 NC A:HEM501 2.1 58.4 0.9 ND A:HEM501 2.2 61.1 0.9 NE2 A:HIS346 2.3 58.7 1.0 N12 A:RCT502 2.9 65.3 1.0 C1B A:HEM501 3.0 64.2 0.9 C4B A:HEM501 3.0 64.2 0.9 C10 A:RCT502 3.0 64.7 1.0 C4A A:HEM501 3.1 62.3 0.9 C1C A:HEM501 3.1 61.2 0.9 CD2 A:HIS346 3.1 57.3 1.0 C4C A:HEM501 3.1 61.1 0.9 C1A A:HEM501 3.1 64.6 0.9 C4D A:HEM501 3.2 62.3 0.9 C1D A:HEM501 3.2 59.8 0.9 CHB A:HEM501 3.4 63.5 0.9 CE1 A:HIS346 3.4 63.7 1.0 CHC A:HEM501 3.4 62.4 0.9 CHA A:HEM501 3.5 65.4 0.9 CHD A:HEM501 3.5 56.4 0.9 N13 A:RCT502 4.0 66.3 1.0 C9 A:RCT502 4.1 65.5 1.0 C2B A:HEM501 4.2 65.3 0.9 C3B A:HEM501 4.2 63.8 0.9 C2C A:HEM501 4.3 58.4 0.9 C3A A:HEM501 4.3 63.2 0.9 CG A:HIS346 4.3 65.1 1.0 C3C A:HEM501 4.3 62.5 0.9 C2A A:HEM501 4.3 66.0 0.9 ND1 A:HIS346 4.4 68.1 1.0 C3D A:HEM501 4.4 57.3 0.9 C2D A:HEM501 4.4 59.0 0.9 CB A:ALA264 4.5 53.2 1.0 CG2 A:VAL350 4.7 62.9 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-0472


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-0472 within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe501 b:50.8 occ:0.86 FE B:HEM501 0.0 50.8 0.9 N11 B:RCT502 2.0 58.7 1.0 NA B:HEM501 2.0 51.2 0.9 NB B:HEM501 2.0 54.0 0.9 NC B:HEM501 2.1 54.0 0.9 ND B:HEM501 2.2 53.7 0.9 NE2 B:HIS346 2.2 47.3 1.0 N12 B:RCT502 2.9 55.8 1.0 C4A B:HEM501 3.0 56.1 0.9 C1B B:HEM501 3.0 52.8 0.9 C10 B:RCT502 3.0 58.2 1.0 CD2 B:HIS346 3.0 49.2 1.0 C1A B:HEM501 3.1 53.6 0.9 C4B B:HEM501 3.1 51.7 0.9 C1C B:HEM501 3.1 53.3 0.9 C4C B:HEM501 3.1 54.2 0.9 C4D B:HEM501 3.2 51.2 0.9 C1D B:HEM501 3.2 51.0 0.9 CE1 B:HIS346 3.2 52.4 1.0 CHB B:HEM501 3.3 57.6 0.9 CHA B:HEM501 3.5 53.5 0.9 CHC B:HEM501 3.5 50.6 0.9 CHD B:HEM501 3.5 51.2 0.9 N13 B:RCT502 4.0 57.2 1.0 C9 B:RCT502 4.1 57.7 1.0 C3A B:HEM501 4.2 54.6 0.9 CG B:HIS346 4.2 49.7 1.0 C2B B:HEM501 4.2 52.6 0.9 C2A B:HEM501 4.3 52.8 0.9 ND1 B:HIS346 4.3 56.8 1.0 C3B B:HEM501 4.3 51.3 0.9 C2C B:HEM501 4.3 55.5 0.9 C3C B:HEM501 4.3 53.4 0.9 CB B:ALA264 4.4 48.2 1.0 C3D B:HEM501 4.4 50.8 0.9 C2D B:HEM501 4.4 50.8 0.9

U.F.Rohrig, S.R.Majjigapu, P.Vogel, A.Reynaud, F.Pojer, N.Dilek, P.Reichenbach, K.Ascencao, M.Irving, G.Coukos, O.Michielin, V.Zoete. Structure-Based Optimization of Type III Indoleamine 2,3-Dioxygenase 1 (IDO1) Inhibitors J Enzyme Inhib Med Chem V. 37 1773 2022.
ISSN: ESSN 1475-6374
DOI: 10.1080/14756366.2022.2089665