Iron in PDB 6r63: Crystal Structure of Indoleamine 2,3-Dioxygenase 1 (IDO1) in Complex with Ferric Heme and Mmg-0358

All present enzymatic activity of Crystal Structure of Indoleamine 2,3-Dioxygenase 1 (IDO1) in Complex with Ferric Heme and Mmg-0358:
1.13.11.52;

The structure of Crystal Structure of Indoleamine 2,3-Dioxygenase 1 (IDO1) in Complex with Ferric Heme and Mmg-0358, PDB code: 6r63 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)	45.45 / 2.89
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	90.910, 97.870, 119.235, 90.00, 90.00, 90.00
R / Rfree (%)	23.4 / 28.7

The structure of Crystal Structure of Indoleamine 2,3-Dioxygenase 1 (IDO1) in Complex with Ferric Heme and Mmg-0358 also contains other interesting chemical elements:

Chlorine

(Cl)

3 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-0358 (pdb code 6r63). 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-0358, PDB code: 6r63:
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-0358


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-0358 within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe501 b:61.6 occ:0.92 FE A:HEM501 0.0 61.6 0.9 ND A:HEM501 1.9 66.8 0.9 NE2 A:HIS346 2.0 61.1 1.0 NA A:HEM501 2.0 65.2 0.9 NB A:HEM501 2.1 60.2 0.9 N2 A:JTB502 2.1 61.9 0.8 NC A:HEM501 2.1 61.0 0.9 CE1 A:HIS346 2.7 63.1 1.0 C4D A:HEM501 2.9 62.4 0.9 C1D A:HEM501 2.9 61.1 0.9 C1A A:HEM501 3.0 66.6 0.9 C1 A:JTB502 3.0 58.8 0.8 C4A A:HEM501 3.0 61.1 0.9 C1B A:HEM501 3.1 61.1 0.9 C4C A:HEM501 3.1 54.7 0.9 C4B A:HEM501 3.1 60.2 0.9 CD2 A:HIS346 3.1 61.6 1.0 C1C A:HEM501 3.1 60.1 0.9 N1 A:JTB502 3.3 63.3 0.8 CHA A:HEM501 3.3 61.4 0.9 CHD A:HEM501 3.4 50.5 0.9 CHB A:HEM501 3.5 60.7 0.9 CHC A:HEM501 3.5 57.1 0.9 ND1 A:HIS346 3.9 71.0 1.0 CG A:HIS346 4.1 64.6 1.0 C2D A:HEM501 4.1 62.5 0.9 C3D A:HEM501 4.1 57.9 0.9 C2A A:HEM501 4.2 66.2 0.9 C3A A:HEM501 4.2 60.8 0.9 C2 A:JTB502 4.2 61.3 0.8 C2B A:HEM501 4.3 58.0 0.9 C3C A:HEM501 4.3 54.0 0.9 C2C A:HEM501 4.3 54.0 0.9 N3 A:JTB502 4.3 64.9 0.8 C3B A:HEM501 4.3 60.5 0.9 CB A:ALA264 4.5 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-0358


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-0358 within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe501 b:60.8 occ:1.00 FE B:HEM501 0.0 60.8 1.0 ND B:HEM501 1.9 70.1 1.0 NA B:HEM501 2.0 62.0 1.0 NE2 B:HIS346 2.0 61.9 1.0 N2 B:JTB502 2.1 65.2 0.9 NC B:HEM501 2.1 64.3 1.0 NB B:HEM501 2.1 68.0 1.0 C1D B:HEM501 2.9 66.2 1.0 C4D B:HEM501 2.9 65.8 1.0 CE1 B:HIS346 2.9 61.4 1.0 C1A B:HEM501 3.0 64.6 1.0 C4C B:HEM501 3.0 64.5 1.0 CD2 B:HIS346 3.0 65.5 1.0 C4A B:HEM501 3.0 65.8 1.0 C1 B:JTB502 3.1 59.8 0.9 C4B B:HEM501 3.1 67.1 1.0 C1B B:HEM501 3.1 69.4 1.0 C1C B:HEM501 3.1 68.1 1.0 N1 B:JTB502 3.1 69.5 0.9 CHA B:HEM501 3.4 64.2 1.0 CHD B:HEM501 3.4 62.9 1.0 CHB B:HEM501 3.5 70.3 1.0 CHC B:HEM501 3.5 67.9 1.0 ND1 B:HIS346 4.0 59.2 1.0 CG B:HIS346 4.1 63.3 1.0 C2D B:HEM501 4.1 65.0 1.0 C3D B:HEM501 4.1 64.4 1.0 C2A B:HEM501 4.2 64.8 1.0 C3A B:HEM501 4.2 64.1 1.0 C3C B:HEM501 4.2 66.5 1.0 C2 B:JTB502 4.2 64.4 0.9 C2C B:HEM501 4.3 68.6 1.0 N3 B:JTB502 4.3 69.0 0.9 C2B B:HEM501 4.3 67.7 1.0 C3B B:HEM501 4.4 66.2 1.0 CB B:ALA264 4.8 60.5 1.0

U.F.Rohrig, A.Reynaud, S.R.Majjigapu, P.Vogel, F.Pojer, V.Zoete. Inhibition Mechanisms of Indoleamine 2,3-Dioxygenase 1 (IDO1). J.Med.Chem. V. 62 8784 2019.
ISSN: ISSN 0022-2623
PubMed: 31525930
DOI: 10.1021/ACS.JMEDCHEM.9B00942