Iron in PDB 5etw: 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: 5etw was solved by S.Y.Wu, Y.H.Peng, J.S.Wu, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	28.74 / 2.70
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	85.674, 91.432, 128.373, 90.00, 90.00, 90.00
R / Rfree (%)	18.9 / 21.6

The binding sites of Iron atom in the Crystal Structure of the Indoleamine 2,3-Dioxygenagse 1 (IDO1) Complexed with NLG919 Analogue (pdb code 5etw). 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: 5etw:
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:80.4 occ:1.00 FE A:HEM501 0.0 80.4 1.0 ND A:HEM501 1.8 84.7 1.0 NA A:HEM501 1.9 78.1 1.0 NC A:HEM501 2.0 78.6 1.0 NB A:HEM501 2.1 78.7 1.0 NAO A:XNL502 2.4 58.3 0.8 NE2 A:HIS346 2.7 67.4 1.0 C4D A:HEM501 2.8 72.7 1.0 C1D A:HEM501 2.8 74.8 1.0 C1A A:HEM501 2.9 80.5 1.0 C4C A:HEM501 3.0 81.1 1.0 C4A A:HEM501 3.0 80.9 1.0 C4B A:HEM501 3.0 76.6 1.0 C1B A:HEM501 3.0 73.3 1.0 CAN A:XNL502 3.1 65.7 0.8 C1C A:HEM501 3.1 86.5 1.0 CD2 A:HIS346 3.2 67.1 1.0 CHA A:HEM501 3.3 79.4 1.0 CHD A:HEM501 3.3 74.9 1.0 CHB A:HEM501 3.4 70.7 1.0 CHC A:HEM501 3.5 81.3 1.0 CAP A:XNL502 3.5 54.5 0.8 CE1 A:HIS346 3.8 78.8 1.0 C2D A:HEM501 4.1 78.0 1.0 C3D A:HEM501 4.1 68.5 1.0 C2A A:HEM501 4.1 78.5 1.0 CB A:ALA264 4.1 61.9 1.0 C3A A:HEM501 4.1 75.9 1.0 C3C A:HEM501 4.2 81.6 1.0 C2B A:HEM501 4.2 76.0 1.0 C2C A:HEM501 4.2 88.9 1.0 C3B A:HEM501 4.2 74.4 1.0 CAJ A:XNL502 4.3 64.3 0.8 CG A:HIS346 4.4 67.4 1.0 ND1 A:HIS346 4.6 77.5 1.0 CAQ A:XNL502 4.6 66.7 0.8 CAK A:XNL502 5.0 75.2 0.8

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:67.8 occ:1.00 FE B:HEM501 0.0 67.8 1.0 ND B:HEM501 2.0 55.8 1.0 NC B:HEM501 2.0 62.0 1.0 NB B:HEM501 2.1 58.6 1.0 NA B:HEM501 2.1 54.5 1.0 NAO B:XNL502 2.5 71.9 0.8 NE2 B:HIS346 2.6 53.5 1.0 CAN B:XNL502 2.9 75.7 0.8 C1D B:HEM501 3.0 57.6 1.0 C1C B:HEM501 3.0 67.7 1.0 C4C B:HEM501 3.0 67.5 1.0 C4D B:HEM501 3.0 54.5 1.0 C4B B:HEM501 3.1 62.9 1.0 CD2 B:HIS346 3.1 52.0 1.0 C1A B:HEM501 3.1 55.4 1.0 C1B B:HEM501 3.1 54.5 1.0 C4A B:HEM501 3.1 54.5 1.0 CHD B:HEM501 3.4 55.0 1.0 CHC B:HEM501 3.4 62.4 1.0 CHA B:HEM501 3.4 54.5 1.0 CHB B:HEM501 3.5 56.1 1.0 CAP B:XNL502 3.7 67.5 0.8 CE1 B:HIS346 3.7 71.4 1.0 CB B:ALA264 4.2 52.2 1.0 CAJ B:XNL502 4.2 67.1 0.8 C2C B:HEM501 4.2 73.3 1.0 C2D B:HEM501 4.2 62.6 1.0 C3C B:HEM501 4.2 58.3 1.0 C3D B:HEM501 4.2 56.4 1.0 C3B B:HEM501 4.3 62.1 1.0 C2B B:HEM501 4.3 59.7 1.0 CG B:HIS346 4.3 59.0 1.0 C2A B:HEM501 4.3 67.1 1.0 C3A B:HEM501 4.3 60.7 1.0 ND1 B:HIS346 4.6 62.1 1.0 CAQ B:XNL502 4.8 68.7 0.8 CAK B:XNL502 4.9 70.9 0.8

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