Iron in PDB 5wmw: Structural Insights Into Substrate and Inhibitor Binding Sites in Human Indoleamine 2,3-Dioxygenase 1

All present enzymatic activity of Structural Insights Into Substrate and Inhibitor Binding Sites in Human Indoleamine 2,3-Dioxygenase 1:
1.13.11.52;

The structure of Structural Insights Into Substrate and Inhibitor Binding Sites in Human Indoleamine 2,3-Dioxygenase 1, PDB code: 5wmw 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)	39.08 / 3.03
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	88.192, 97.907, 127.863, 90.00, 90.00, 90.00
R / Rfree (%)	21.2 / 25.9

The binding sites of Iron atom in the Structural Insights Into Substrate and Inhibitor Binding Sites in Human Indoleamine 2,3-Dioxygenase 1 (pdb code 5wmw). 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 1, PDB code: 5wmw:
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 1


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 1 within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe501 b:82.2 occ:1.00 FE A:HEM501 0.0 82.2 1.0 NE2 A:HIS346 1.9 79.2 1.0 ND A:HEM501 1.9 80.7 1.0 C A:CYN502 1.9 84.5 1.0 NA A:HEM501 2.0 83.3 1.0 NC A:HEM501 2.1 82.0 1.0 NB A:HEM501 2.1 83.9 1.0 CE1 A:HIS346 2.9 78.6 1.0 CD2 A:HIS346 2.9 78.2 1.0 C1D A:HEM501 2.9 79.7 1.0 C4D A:HEM501 2.9 80.5 1.0 C1A A:HEM501 3.0 83.0 1.0 C4A A:HEM501 3.0 84.8 1.0 C4B A:HEM501 3.1 84.5 1.0 N A:CYN502 3.1 85.2 1.0 C1B A:HEM501 3.1 85.3 1.0 C4C A:HEM501 3.1 81.4 1.0 C1C A:HEM501 3.1 83.1 1.0 CHA A:HEM501 3.4 82.0 1.0 CHD A:HEM501 3.4 80.2 1.0 CHB A:HEM501 3.4 85.8 1.0 CHC A:HEM501 3.5 84.0 1.0 ND1 A:HIS346 4.0 78.0 1.0 CG A:HIS346 4.0 77.8 1.0 C3D A:HEM501 4.2 78.5 1.0 C2D A:HEM501 4.2 78.4 1.0 C2A A:HEM501 4.2 84.5 1.0 C3A A:HEM501 4.2 85.5 1.0 C3C A:HEM501 4.3 82.7 1.0 C2B A:HEM501 4.3 86.8 1.0 C2C A:HEM501 4.3 83.5 1.0 C3B A:HEM501 4.3 86.4 1.0 CB A:ALA264 4.5 87.6 1.0 CD1 A:TRP503 4.5 98.3 1.0 NE1 A:TRP503 4.7 97.7 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 1


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 1 within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe501 b:94.3 occ:1.00 FE B:HEM501 0.0 94.3 1.0 NE2 B:HIS346 1.9 97.6 1.0 ND B:HEM501 1.9 93.7 1.0 C B:CYN502 1.9 95.3 1.0 NA B:HEM501 2.0 96.8 1.0 NC B:HEM501 2.1 93.2 1.0 NB B:HEM501 2.1 96.1 1.0 CE1 B:HIS346 2.9 99.2 1.0 CD2 B:HIS346 2.9 98.2 1.0 C4D B:HEM501 2.9 94.3 1.0 C1D B:HEM501 2.9 92.5 1.0 C1A B:HEM501 3.0 97.3 1.0 C4A B:HEM501 3.0 98.6 1.0 C4B B:HEM501 3.1 95.8 1.0 C1B B:HEM501 3.1 98.0 1.0 C4C B:HEM501 3.1 92.6 1.0 N B:CYN502 3.1 96.0 1.0 C1C B:HEM501 3.1 93.4 1.0 CHA B:HEM501 3.4 96.1 1.0 CHD B:HEM501 3.4 92.2 1.0 CHB B:HEM501 3.4 99.4 1.0 CHC B:HEM501 3.5 94.5 1.0 ND1 B:HIS346 4.0 0.8 1.0 CG B:HIS346 4.0 0.3 1.0 C3D B:HEM501 4.2 92.8 1.0 C2D B:HEM501 4.2 91.7 1.0 C2A B:HEM501 4.2 99.0 1.0 C3A B:HEM501 4.2 99.6 1.0 C3C B:HEM501 4.3 92.7 1.0 C2B B:HEM501 4.3 98.6 1.0 C2C B:HEM501 4.3 92.7 1.0 C3B B:HEM501 4.3 97.2 1.0 CB B:ALA264 4.5 90.7 1.0 CD1 B:TRP503 4.5 0.8 1.0 NE1 B:TRP503 4.7 99.0 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