Iron in PDB 5wmv: 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: 5wmv 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)	38.88 / 2.60
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	89.092, 97.705, 127.108, 90.00, 90.00, 90.00
R / Rfree (%)	22 / 26

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 5wmv). 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: 5wmv:
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:70.8 occ:1.00 FE A:HEM501 0.0 70.8 1.0 NE2 A:HIS346 1.9 69.2 1.0 C A:CYN500 1.9 73.9 1.0 ND A:HEM501 1.9 69.5 1.0 NA A:HEM501 2.0 71.4 1.0 NC A:HEM501 2.1 70.8 1.0 NB A:HEM501 2.1 72.5 1.0 CE1 A:HIS346 2.7 68.4 1.0 C4D A:HEM501 2.9 69.5 1.0 C1D A:HEM501 2.9 68.8 1.0 CD2 A:HIS346 3.0 68.4 1.0 C1A A:HEM501 3.0 71.2 1.0 N A:CYN500 3.0 75.8 1.0 C4A A:HEM501 3.0 72.6 1.0 C4B A:HEM501 3.1 73.2 1.0 C1B A:HEM501 3.1 73.5 1.0 C4C A:HEM501 3.1 70.2 1.0 C1C A:HEM501 3.1 72.0 1.0 CHA A:HEM501 3.4 70.2 1.0 CHD A:HEM501 3.4 69.0 1.0 CHB A:HEM501 3.4 73.6 1.0 CHC A:HEM501 3.5 73.2 1.0 ND1 A:HIS346 3.9 67.8 1.0 CG A:HIS346 4.1 67.8 1.0 C2D A:HEM501 4.2 67.8 1.0 C3D A:HEM501 4.2 68.5 1.0 C2A A:HEM501 4.2 72.4 1.0 C3A A:HEM501 4.2 73.1 1.0 C3C A:HEM501 4.3 71.2 1.0 C2C A:HEM501 4.3 72.4 1.0 C2B A:HEM501 4.3 75.1 1.0 C3B A:HEM501 4.3 74.9 1.0 CD1 A:TRP502 4.4 95.0 1.0 CB A:ALA264 4.7 77.6 1.0 NE1 A:TRP502 4.7 94.7 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:71.5 occ:1.00 FE B:HEM501 0.0 71.5 1.0 NE2 B:HIS346 1.9 71.6 1.0 C B:CYN500 1.9 71.4 1.0 ND B:HEM501 1.9 70.6 1.0 NA B:HEM501 2.0 73.1 1.0 NC B:HEM501 2.1 70.1 1.0 NB B:HEM501 2.1 72.7 1.0 CE1 B:HIS346 2.7 72.2 1.0 C1D B:HEM501 2.9 69.9 1.0 C4D B:HEM501 2.9 71.4 1.0 C1A B:HEM501 3.0 73.6 1.0 C4A B:HEM501 3.0 74.8 1.0 CD2 B:HIS346 3.0 71.8 1.0 C4B B:HEM501 3.1 72.3 1.0 C1B B:HEM501 3.1 74.2 1.0 C4C B:HEM501 3.1 69.5 1.0 C1C B:HEM501 3.1 70.3 1.0 N B:CYN500 3.1 72.4 1.0 CHA B:HEM501 3.4 72.7 1.0 CHD B:HEM501 3.4 69.6 1.0 CHB B:HEM501 3.4 75.3 1.0 CHC B:HEM501 3.5 71.1 1.0 ND1 B:HIS346 3.9 73.4 1.0 CG B:HIS346 4.1 73.1 1.0 C2D B:HEM501 4.2 69.9 1.0 C3D B:HEM501 4.2 70.6 1.0 C3A B:HEM501 4.2 76.0 1.0 C2A B:HEM501 4.2 75.2 1.0 C3C B:HEM501 4.3 69.4 1.0 C2B B:HEM501 4.3 75.0 1.0 C2C B:HEM501 4.3 69.6 1.0 C3B B:HEM501 4.3 74.2 1.0 CD1 B:TRP502 4.3 77.8 1.0 NE1 B:TRP502 4.6 76.3 1.0 CB B:ALA264 4.7 70.8 1.0 O1 B:ZCW503 4.9 93.0 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