Iron in PDB 5ek2: Crystal Structure of the Indoleamine 2,3-Dioxygenagse 1 (IDO1) Complexed with NLG919 Analogue

All present enzymatic activity of Crystal Structure of the Indoleamine 2,3-Dioxygenagse 1 (IDO1) Complexed with NLG919 Analogue:
1.13.11.52;

The structure of Crystal Structure of the Indoleamine 2,3-Dioxygenagse 1 (IDO1) Complexed with NLG919 Analogue, PDB code: 5ek2 was solved by Y.H.Peng, J.S.Wu, S.Y.Wu, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	29.49 / 2.68
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	86.005, 96.985, 131.206, 90.00, 90.00, 90.00
R / Rfree (%)	17.1 / 23.1

The structure of Crystal Structure of the Indoleamine 2,3-Dioxygenagse 1 (IDO1) Complexed with NLG919 Analogue also contains other interesting chemical elements:

Fluorine

(F)

2 atoms

The binding sites of Iron atom in the Crystal Structure of the Indoleamine 2,3-Dioxygenagse 1 (IDO1) Complexed with NLG919 Analogue (pdb code 5ek2). 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 the Indoleamine 2,3-Dioxygenagse 1 (IDO1) Complexed with NLG919 Analogue, PDB code: 5ek2:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in the Crystal Structure of the Indoleamine 2,3-Dioxygenagse 1 (IDO1) Complexed with NLG919 Analogue


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 the Indoleamine 2,3-Dioxygenagse 1 (IDO1) Complexed with NLG919 Analogue within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe501 b:49.6 occ:1.00 FE A:HEM501 0.0 49.6 1.0 NB A:HEM501 2.0 52.0 1.0 NC A:HEM501 2.0 55.6 1.0 NA A:HEM501 2.0 49.6 1.0 ND A:HEM501 2.1 51.1 1.0 NAP A:5PJ502 2.2 49.6 1.0 NE2 A:HIS346 2.2 46.5 1.0 C4B A:HEM501 3.0 52.0 1.0 C1C A:HEM501 3.0 52.6 1.0 C1B A:HEM501 3.0 49.6 1.0 CD2 A:HIS346 3.0 44.8 1.0 C4A A:HEM501 3.0 49.6 1.0 CAO A:5PJ502 3.1 50.4 1.0 C4C A:HEM501 3.1 50.1 1.0 C1A A:HEM501 3.1 49.6 1.0 C1D A:HEM501 3.1 49.6 1.0 C4D A:HEM501 3.1 49.6 1.0 CAQ A:5PJ502 3.3 49.6 1.0 CE1 A:HIS346 3.3 50.9 1.0 CHC A:HEM501 3.4 49.6 1.0 CHB A:HEM501 3.4 49.6 1.0 CHD A:HEM501 3.5 49.6 1.0 CHA A:HEM501 3.5 49.6 1.0 C3B A:HEM501 4.2 52.5 1.0 C2B A:HEM501 4.2 50.9 1.0 NAK A:5PJ502 4.2 51.1 1.0 C2C A:HEM501 4.2 49.6 1.0 CG A:HIS346 4.3 46.8 1.0 C3C A:HEM501 4.3 49.6 1.0 C3A A:HEM501 4.3 49.6 1.0 C2A A:HEM501 4.3 49.6 1.0 CAL A:5PJ502 4.3 49.6 1.0 ND1 A:HIS346 4.4 49.7 1.0 C3D A:HEM501 4.4 49.6 1.0 C2D A:HEM501 4.4 49.6 1.0 CB A:ALA264 4.5 48.9 1.0

Iron binding site 2 out of 2 in the Crystal Structure of the Indoleamine 2,3-Dioxygenagse 1 (IDO1) Complexed with NLG919 Analogue


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 the Indoleamine 2,3-Dioxygenagse 1 (IDO1) Complexed with NLG919 Analogue within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe501 b:49.6 occ:1.00 FE B:HEM501 0.0 49.6 1.0 NC B:HEM501 2.0 49.6 1.0 NB B:HEM501 2.0 49.6 1.0 NA B:HEM501 2.0 49.6 1.0 ND B:HEM501 2.1 51.3 1.0 NE2 B:HIS346 2.3 55.2 1.0 NAP B:5PJ502 2.3 49.6 1.0 C1C B:HEM501 3.0 49.6 1.0 C4C B:HEM501 3.0 49.6 1.0 C4B B:HEM501 3.0 49.6 1.0 C1B B:HEM501 3.0 49.6 1.0 CD2 B:HIS346 3.1 51.4 1.0 C1A B:HEM501 3.1 50.9 1.0 C4A B:HEM501 3.1 49.6 1.0 C1D B:HEM501 3.1 49.6 1.0 C4D B:HEM501 3.1 51.9 1.0 CAO B:5PJ502 3.1 49.6 1.0 CAQ B:5PJ502 3.3 49.6 1.0 CE1 B:HIS346 3.4 58.7 1.0 CHC B:HEM501 3.4 49.6 1.0 CHD B:HEM501 3.4 49.6 1.0 CHB B:HEM501 3.4 49.6 1.0 CHA B:HEM501 3.4 55.1 1.0 C2C B:HEM501 4.2 49.6 1.0 C3C B:HEM501 4.2 49.6 1.0 C3B B:HEM501 4.3 49.6 1.0 C2B B:HEM501 4.3 49.6 1.0 NAK B:5PJ502 4.3 49.8 1.0 CG B:HIS346 4.3 60.8 1.0 C3A B:HEM501 4.3 49.6 1.0 C2A B:HEM501 4.3 49.6 1.0 C3D B:HEM501 4.3 49.6 1.0 C2D B:HEM501 4.3 49.6 1.0 CAL B:5PJ502 4.4 51.2 1.0 ND1 B:HIS346 4.4 61.8 1.0 CB B:ALA264 4.4 49.8 1.0

Y.H.Peng, S.H.Ueng, C.T.Tseng, M.S.Hung, J.S.Song, J.S.Wu, F.Y.Liao, Y.S.Fan, M.H.Wu, W.C.Hsiao, C.C.Hsueh, S.Y.Lin, C.Y.Cheng, C.H.Tu, L.C.Lee, M.F.Cheng, K.S.Shia, C.Shih, S.Y.Wu. Important Hydrogen Bond Networks in Indoleamine 2,3-Dioxygenase 1 (IDO1) Inhibitor Design Revealed By Crystal Structures of Imidazoleisoindole Derivatives with IDO1 J.Med.Chem. V. 59 282 2016.
ISSN: ISSN 0022-2623
PubMed: 26642377
DOI: 10.1021/ACS.JMEDCHEM.5B01390