Iron in PDB 5wmu: Structural Insights Into Substrate and Inhibitor Binding Sites in Human Indoleamine 2,3-Dioxygenase I

All present enzymatic activity of Structural Insights Into Substrate and Inhibitor Binding Sites in Human Indoleamine 2,3-Dioxygenase I:
1.13.11.52;

The structure of Structural Insights Into Substrate and Inhibitor Binding Sites in Human Indoleamine 2,3-Dioxygenase I, PDB code: 5wmu was solved by A.Lewis-Ballester, S.R.Yeh, K.N.Pham, D.Batabyal, S.Karkashon, J.B.Bonanno, T.L.Poulos, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	38.65 / 2.40
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	89.301, 97.768, 125.643, 90.00, 90.00, 90.00
R / Rfree (%)	21.4 / 25.8

The binding sites of Iron atom in the Structural Insights Into Substrate and Inhibitor Binding Sites in Human Indoleamine 2,3-Dioxygenase I (pdb code 5wmu). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 2 binding sites of Iron where determined in the Structural Insights Into Substrate and Inhibitor Binding Sites in Human Indoleamine 2,3-Dioxygenase I, PDB code: 5wmu:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in the Structural Insights Into Substrate and Inhibitor Binding Sites in Human Indoleamine 2,3-Dioxygenase I


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Structural Insights Into Substrate and Inhibitor Binding Sites in Human Indoleamine 2,3-Dioxygenase I within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe501 b:58.6 occ:1.00 FE A:HEM501 0.0 58.6 1.0 C A:CYN502 1.9 57.8 1.0 ND A:HEM501 1.9 60.1 1.0 NE2 A:HIS346 1.9 54.5 1.0 NA A:HEM501 2.0 61.2 1.0 NC A:HEM501 2.1 62.5 1.0 NB A:HEM501 2.1 61.7 1.0 CE1 A:HIS346 2.8 54.4 1.0 C1D A:HEM501 2.9 58.8 1.0 C4D A:HEM501 2.9 59.4 1.0 CD2 A:HIS346 3.0 53.6 1.0 N A:CYN502 3.0 61.6 1.0 C1A A:HEM501 3.0 60.2 1.0 C4A A:HEM501 3.0 60.6 1.0 C1B A:HEM501 3.0 61.3 1.0 C4B A:HEM501 3.1 62.1 1.0 C4C A:HEM501 3.1 63.7 1.0 C1C A:HEM501 3.1 62.8 1.0 CHA A:HEM501 3.4 60.8 1.0 CHD A:HEM501 3.4 61.4 1.0 CHB A:HEM501 3.4 60.9 1.0 CHC A:HEM501 3.5 62.9 1.0 ND1 A:HIS346 4.0 53.6 1.0 CG A:HIS346 4.1 52.4 1.0 C2D A:HEM501 4.2 57.9 1.0 C3D A:HEM501 4.2 58.2 1.0 C2A A:HEM501 4.2 60.6 1.0 C3A A:HEM501 4.2 60.6 1.0 C2C A:HEM501 4.3 64.8 1.0 C2B A:HEM501 4.3 62.6 1.0 C3C A:HEM501 4.3 65.6 1.0 C3B A:HEM501 4.3 62.7 1.0 CD1 A:TRP503 4.4 64.9 1.0 CB A:ALA264 4.6 62.9 1.0 NE1 A:TRP503 4.7 63.6 1.0

Iron binding site 2 out of 2 in the Structural Insights Into Substrate and Inhibitor Binding Sites in Human Indoleamine 2,3-Dioxygenase I


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Structural Insights Into Substrate and Inhibitor Binding Sites in Human Indoleamine 2,3-Dioxygenase I 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 C B:CYN502 1.9 60.6 1.0 ND B:HEM501 1.9 58.1 1.0 NE2 B:HIS346 1.9 66.0 1.0 NA B:HEM501 2.0 58.3 1.0 NC B:HEM501 2.1 57.5 1.0 NB B:HEM501 2.1 59.1 1.0 CE1 B:HIS346 2.8 66.8 1.0 C1D B:HEM501 2.9 57.7 1.0 C4D B:HEM501 2.9 59.1 1.0 N B:CYN502 3.0 60.7 1.0 CD2 B:HIS346 3.0 66.2 1.0 C1A B:HEM501 3.0 60.1 1.0 C4A B:HEM501 3.0 58.4 1.0 C1B B:HEM501 3.1 59.3 1.0 C4B B:HEM501 3.1 58.3 1.0 C4C B:HEM501 3.1 57.9 1.0 C1C B:HEM501 3.1 59.0 1.0 CHA B:HEM501 3.4 60.2 1.0 CHD B:HEM501 3.4 57.5 1.0 CHB B:HEM501 3.4 58.7 1.0 CHC B:HEM501 3.5 58.3 1.0 ND1 B:HIS346 4.0 66.9 1.0 CG B:HIS346 4.1 66.3 1.0 C2D B:HEM501 4.2 58.9 1.0 C3D B:HEM501 4.2 58.2 1.0 C2A B:HEM501 4.2 59.4 1.0 C3A B:HEM501 4.2 61.0 1.0 C2C B:HEM501 4.3 58.0 1.0 C3C B:HEM501 4.3 57.8 1.0 C2B B:HEM501 4.3 60.2 1.0 CD1 B:TRP503 4.3 60.1 1.0 C3B B:HEM501 4.3 58.9 1.0 CB B:ALA264 4.5 60.1 1.0 NE1 B:TRP503 4.6 60.1 1.0

A.Lewis-Ballester, K.N.Pham, D.Batabyal, S.Karkashon, J.B.Bonanno, T.L.Poulos, S.R.Yeh. Structural Insights Into Substrate and Inhibitor Binding Sites in Human Indoleamine 2,3-Dioxygenase 1. Nat Commun V. 8 1693 2017.
ISSN: ESSN 2041-1723
PubMed: 29167421
DOI: 10.1038/S41467-017-01725-8