Iron in PDB 4u74: Crystal Structure of 4-Phenylimidazole Bound Form of Human Indoleamine 2,3-Dioxygenase (G262A Mutant)

All present enzymatic activity of Crystal Structure of 4-Phenylimidazole Bound Form of Human Indoleamine 2,3-Dioxygenase (G262A Mutant):
1.13.11.52;

The structure of Crystal Structure of 4-Phenylimidazole Bound Form of Human Indoleamine 2,3-Dioxygenase (G262A Mutant), PDB code: 4u74 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)	19.89 / 2.31
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	85.884, 99.539, 132.343, 90.00, 90.00, 90.00
R / Rfree (%)	17.1 / 22

The binding sites of Iron atom in the Crystal Structure of 4-Phenylimidazole Bound Form of Human Indoleamine 2,3-Dioxygenase (G262A Mutant) (pdb code 4u74). 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 (G262A Mutant), PDB code: 4u74:
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 (G262A 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 (G262A Mutant) within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe501 b:19.4 occ:1.00 FE A:HEM501 0.0 19.4 1.0 ND A:HEM501 1.9 22.6 1.0 N3 A:PIM502 1.9 15.6 1.0 NA A:HEM501 2.0 19.7 1.0 NE2 A:HIS346 2.0 20.8 1.0 NC A:HEM501 2.0 20.6 1.0 NB A:HEM501 2.1 20.0 1.0 C2 A:PIM502 2.9 18.2 1.0 CE1 A:HIS346 2.9 22.2 1.0 C4D A:HEM501 3.0 20.1 1.0 C1D A:HEM501 3.0 20.6 1.0 C4B A:HEM501 3.0 21.8 1.0 C1A A:HEM501 3.0 20.5 1.0 C1B A:HEM501 3.0 20.7 1.0 C4A A:HEM501 3.0 20.4 1.0 C4 A:PIM502 3.0 17.5 1.0 C1C A:HEM501 3.0 21.8 1.0 C4C A:HEM501 3.1 20.9 1.0 CD2 A:HIS346 3.1 21.1 1.0 CHC A:HEM501 3.4 22.8 1.0 CHA A:HEM501 3.4 21.8 1.0 CHB A:HEM501 3.4 17.9 1.0 CHD A:HEM501 3.5 19.8 1.0 ND1 A:HIS346 4.0 20.9 1.0 N1 A:PIM502 4.1 18.1 1.0 C5 A:PIM502 4.1 18.7 1.0 CG A:HIS346 4.2 21.1 1.0 C3A A:HEM501 4.2 20.8 1.0 C2A A:HEM501 4.2 20.4 1.0 C3D A:HEM501 4.2 19.5 1.0 C2B A:HEM501 4.2 21.6 1.0 C2D A:HEM501 4.2 19.0 1.0 C3C A:HEM501 4.2 22.0 1.0 C2C A:HEM501 4.3 22.1 1.0 C3B A:HEM501 4.3 23.8 1.0 CB A:ALA264 4.6 17.3 1.0

Iron binding site 2 out of 2 in the Crystal Structure of 4-Phenylimidazole Bound Form of Human Indoleamine 2,3-Dioxygenase (G262A 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 (G262A Mutant) within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe501 b:23.2 occ:1.00 FE B:HEM501 0.0 23.2 1.0 N3 B:PIM502 1.9 20.5 1.0 ND B:HEM501 1.9 23.4 1.0 NA B:HEM501 2.0 21.3 1.0 NB B:HEM501 2.0 22.0 1.0 NC B:HEM501 2.1 20.3 1.0 NE2 B:HIS346 2.1 19.2 1.0 C2 B:PIM502 2.9 18.9 1.0 C4 B:PIM502 2.9 16.7 1.0 C4D B:HEM501 3.0 20.3 1.0 C1A B:HEM501 3.0 22.9 1.0 CE1 B:HIS346 3.0 19.6 1.0 C1B B:HEM501 3.0 22.1 1.0 C4A B:HEM501 3.0 22.5 1.0 C1D B:HEM501 3.0 21.0 1.0 C4B B:HEM501 3.0 23.3 1.0 C4C B:HEM501 3.0 20.8 1.0 CD2 B:HIS346 3.1 17.6 1.0 C1C B:HEM501 3.1 23.9 1.0 CHB B:HEM501 3.4 22.2 1.0 CHA B:HEM501 3.4 22.9 1.0 CHC B:HEM501 3.5 24.4 1.0 CHD B:HEM501 3.5 19.9 1.0 C5 B:PIM502 4.0 18.9 1.0 N1 B:PIM502 4.0 19.9 1.0 ND1 B:HIS346 4.1 20.4 1.0 C2A B:HEM501 4.2 20.8 1.0 C3A B:HEM501 4.2 23.1 1.0 CG B:HIS346 4.2 19.7 1.0 C3C B:HEM501 4.2 21.8 1.0 C3D B:HEM501 4.3 20.2 1.0 C2B B:HEM501 4.3 23.5 1.0 C2D B:HEM501 4.3 19.2 1.0 C3B B:HEM501 4.3 23.4 1.0 C2C B:HEM501 4.3 22.2 1.0 CB B:ALA264 4.6 20.9 1.0 CG2 B:VAL350 4.9 25.9 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.