Iron in PDB 4u72: Crystal Structure of 4-Phenylimidazole Bound Form of Human Indoleamine 2,3-Dioxygenase (A260G Mutant)

All present enzymatic activity of Crystal Structure of 4-Phenylimidazole Bound Form of Human Indoleamine 2,3-Dioxygenase (A260G Mutant):
1.13.11.52;

The structure of Crystal Structure of 4-Phenylimidazole Bound Form of Human Indoleamine 2,3-Dioxygenase (A260G Mutant), PDB code: 4u72 was solved by H.Sugimoto, M.Horitani, E.Kometani, Y.Shiro, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	19.76 / 2.00
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	85.971, 98.890, 131.582, 90.00, 90.00, 90.00
R / Rfree (%)	18.6 / 23.1

The binding sites of Iron atom in the Crystal Structure of 4-Phenylimidazole Bound Form of Human Indoleamine 2,3-Dioxygenase (A260G Mutant) (pdb code 4u72). 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 4-Phenylimidazole Bound Form of Human Indoleamine 2,3-Dioxygenase (A260G Mutant), PDB code: 4u72:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in the Crystal Structure of 4-Phenylimidazole Bound Form of Human Indoleamine 2,3-Dioxygenase (A260G Mutant)


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 4-Phenylimidazole Bound Form of Human Indoleamine 2,3-Dioxygenase (A260G Mutant) within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe501 b:15.4 occ:1.00 FE A:HEM501 0.0 15.4 1.0 N3 A:PIM502 1.9 12.8 1.0 NA A:HEM501 2.0 15.7 1.0 ND A:HEM501 2.0 16.3 1.0 NE2 A:HIS346 2.0 17.0 1.0 NC A:HEM501 2.1 15.1 1.0 NB A:HEM501 2.1 16.3 1.0 C4 A:PIM502 2.9 12.0 1.0 C2 A:PIM502 3.0 12.5 1.0 C1B A:HEM501 3.0 16.1 1.0 CE1 A:HIS346 3.0 17.3 1.0 C4A A:HEM501 3.0 15.7 1.0 C1A A:HEM501 3.0 14.3 1.0 C1D A:HEM501 3.0 16.3 1.0 CD2 A:HIS346 3.0 14.8 1.0 C4B A:HEM501 3.0 15.5 1.0 C4D A:HEM501 3.0 14.4 1.0 C4C A:HEM501 3.1 16.4 1.0 C1C A:HEM501 3.1 16.8 1.0 CHB A:HEM501 3.4 15.1 1.0 CHA A:HEM501 3.4 15.1 1.0 CHD A:HEM501 3.5 16.0 1.0 CHC A:HEM501 3.5 15.6 1.0 C5 A:PIM502 4.1 12.8 1.0 N1 A:PIM502 4.1 13.7 1.0 ND1 A:HIS346 4.1 15.1 1.0 CG A:HIS346 4.1 14.9 1.0 C2A A:HEM501 4.2 15.3 1.0 C3A A:HEM501 4.2 16.1 1.0 C2B A:HEM501 4.2 18.6 1.0 C3C A:HEM501 4.3 16.3 1.0 C3B A:HEM501 4.3 16.1 1.0 C2C A:HEM501 4.3 14.4 1.0 C3D A:HEM501 4.3 15.8 1.0 C2D A:HEM501 4.3 15.7 1.0 CB A:ALA264 4.6 14.3 1.0

Iron binding site 2 out of 2 in the Crystal Structure of 4-Phenylimidazole Bound Form of Human Indoleamine 2,3-Dioxygenase (A260G Mutant)


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 4-Phenylimidazole Bound Form of Human Indoleamine 2,3-Dioxygenase (A260G Mutant) within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe501 b:18.0 occ:1.00 FE B:HEM501 0.0 18.0 1.0 N3 B:PIM502 2.0 14.3 1.0 ND B:HEM501 2.0 17.8 1.0 NA B:HEM501 2.0 17.8 1.0 NE2 B:HIS346 2.0 14.9 1.0 NC B:HEM501 2.1 16.7 1.0 NB B:HEM501 2.1 18.8 1.0 C2 B:PIM502 2.9 14.7 1.0 CE1 B:HIS346 3.0 16.0 1.0 C4 B:PIM502 3.0 14.4 1.0 C4D B:HEM501 3.0 16.5 1.0 C1D B:HEM501 3.0 17.9 1.0 C4C B:HEM501 3.0 16.1 1.0 C1B B:HEM501 3.0 18.4 1.0 C4A B:HEM501 3.0 18.9 1.0 C4B B:HEM501 3.0 19.1 1.0 C1A B:HEM501 3.0 18.1 1.0 CD2 B:HIS346 3.1 15.9 1.0 C1C B:HEM501 3.1 18.1 1.0 CHB B:HEM501 3.4 16.5 1.0 CHD B:HEM501 3.4 15.5 1.0 CHC B:HEM501 3.5 19.6 1.0 CHA B:HEM501 3.5 16.9 1.0 N1 B:PIM502 4.1 15.2 1.0 C5 B:PIM502 4.1 13.8 1.0 ND1 B:HIS346 4.1 16.7 1.0 CG B:HIS346 4.2 16.0 1.0 C3A B:HEM501 4.2 17.9 1.0 C2A B:HEM501 4.2 17.1 1.0 C3C B:HEM501 4.2 19.0 1.0 C3D B:HEM501 4.3 17.1 1.0 C2C B:HEM501 4.3 19.8 1.0 C2D B:HEM501 4.3 15.9 1.0 C2B B:HEM501 4.3 19.8 1.0 C3B B:HEM501 4.3 19.7 1.0 CB B:ALA264 4.6 15.2 1.0

M.Horitani, E.Kometani, E.Vottero, T.Otsuki, Y.Shiro, H.Sugimoto. Conformation and Mobility of Active Site Loop Is Critical For Substrate Binding and Inhibition in Human Indoleamine 2,3-Dioxygenase To Be Published.