Iron in PDB 6cxv: Structure of the S167H Mutant of Human Indoleamine 2,3 Dioxygenase in Complex with Tryptophan and Cyanide

All present enzymatic activity of Structure of the S167H Mutant of Human Indoleamine 2,3 Dioxygenase in Complex with Tryptophan and Cyanide:
1.13.11.52;

The structure of Structure of the S167H Mutant of Human Indoleamine 2,3 Dioxygenase in Complex with Tryptophan and Cyanide, PDB code: 6cxv was solved by A.Lewis-Ballester, S.-R.Yeh, S.Karkashon, D.Batabyal, T.L.Poulos, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	30.00 / 2.60
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	88.660, 98.090, 126.740, 90.00, 90.00, 90.00
R / Rfree (%)	20.8 / 26.6

The binding sites of Iron atom in the Structure of the S167H Mutant of Human Indoleamine 2,3 Dioxygenase in Complex with Tryptophan and Cyanide (pdb code 6cxv). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 2 binding sites of Iron where determined in the Structure of the S167H Mutant of Human Indoleamine 2,3 Dioxygenase in Complex with Tryptophan and Cyanide, PDB code: 6cxv:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in the Structure of the S167H Mutant of Human Indoleamine 2,3 Dioxygenase in Complex with Tryptophan and Cyanide


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Structure of the S167H Mutant of Human Indoleamine 2,3 Dioxygenase in Complex with Tryptophan and Cyanide within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe501 b:59.8 occ:1.00 FE A:HEM501 0.0 59.8 1.0 C A:CYN502 1.9 59.5 1.0 ND A:HEM501 1.9 61.7 1.0 NE2 A:HIS346 1.9 56.2 1.0 NA A:HEM501 2.0 60.1 1.0 NC A:HEM501 2.1 60.2 1.0 NB A:HEM501 2.1 60.1 1.0 CE1 A:HIS346 2.9 54.6 1.0 C4D A:HEM501 2.9 60.7 1.0 C1D A:HEM501 2.9 60.3 1.0 CD2 A:HIS346 3.0 54.6 1.0 C1A A:HEM501 3.0 60.5 1.0 C4A A:HEM501 3.0 60.4 1.0 C1B A:HEM501 3.1 61.2 1.0 C4B A:HEM501 3.1 61.4 1.0 C4C A:HEM501 3.1 61.4 1.0 C1C A:HEM501 3.1 62.9 1.0 N A:CYN502 3.2 63.4 1.0 CHA A:HEM501 3.4 61.7 1.0 CHD A:HEM501 3.4 61.2 1.0 CHB A:HEM501 3.4 60.2 1.0 CHC A:HEM501 3.5 62.3 1.0 ND1 A:HIS346 4.0 52.6 1.0 CG A:HIS346 4.1 54.7 1.0 C2D A:HEM501 4.2 58.8 1.0 C3D A:HEM501 4.2 57.9 1.0 C2A A:HEM501 4.2 61.6 1.0 C3A A:HEM501 4.2 60.1 1.0 C2B A:HEM501 4.3 63.0 1.0 C3C A:HEM501 4.3 61.4 1.0 C2C A:HEM501 4.3 63.9 1.0 C3B A:HEM501 4.3 61.7 1.0 CB A:ALA264 4.4 65.7 1.0 CD1 A:TRP503 4.4 59.9 1.0 NE1 A:TRP503 4.6 58.8 1.0

Iron binding site 2 out of 2 in the Structure of the S167H Mutant of Human Indoleamine 2,3 Dioxygenase in Complex with Tryptophan and Cyanide


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Structure of the S167H Mutant of Human Indoleamine 2,3 Dioxygenase in Complex with Tryptophan and Cyanide within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe501 b:61.8 occ:1.00 FE B:HEM501 0.0 61.8 1.0 C B:CYN502 1.9 64.2 1.0 ND B:HEM501 1.9 62.0 1.0 NE2 B:HIS346 1.9 67.4 1.0 NA B:HEM501 2.0 59.9 1.0 NB B:HEM501 2.1 59.4 1.0 NC B:HEM501 2.1 59.1 1.0 CE1 B:HIS346 2.8 68.3 1.0 C1D B:HEM501 2.9 62.2 1.0 C4D B:HEM501 2.9 63.4 1.0 CD2 B:HIS346 3.0 68.6 1.0 C1A B:HEM501 3.0 62.6 1.0 C4A B:HEM501 3.0 60.1 1.0 N B:CYN502 3.0 61.5 1.0 C1B B:HEM501 3.1 59.4 1.0 C4B B:HEM501 3.1 58.9 1.0 C4C B:HEM501 3.1 59.4 1.0 C1C B:HEM501 3.1 59.3 1.0 CHD B:HEM501 3.4 60.9 1.0 CHA B:HEM501 3.4 62.7 1.0 CHB B:HEM501 3.4 58.9 1.0 CHC B:HEM501 3.5 58.2 1.0 ND1 B:HIS346 4.0 68.9 1.0 CG B:HIS346 4.1 70.3 1.0 C2D B:HEM501 4.2 63.0 1.0 C3D B:HEM501 4.2 63.4 1.0 C2A B:HEM501 4.2 62.4 1.0 C3A B:HEM501 4.2 61.7 1.0 C2B B:HEM501 4.3 60.4 1.0 C2C B:HEM501 4.3 58.9 1.0 C3C B:HEM501 4.3 60.4 1.0 C3B B:HEM501 4.3 59.8 1.0 CD1 B:TRP503 4.3 56.5 1.0 NE1 B:TRP503 4.5 55.7 1.0 CB B:ALA264 4.7 56.6 1.0

A.Lewis-Ballester, S.Karkashon, D.Batabyal, T.L.Poulos, S.R.Yeh. Inhibition Mechanisms of Human Indoleamine 2,3 Dioxygenase 1. J. Am. Chem. Soc. V. 140 8518 2018.
ISSN: ESSN 1520-5126
PubMed: 29897749
DOI: 10.1021/JACS.8B03691