Iron in PDB 3czy: Crystal Structure of Human Heme Oxygenase-1 in Complex with 1-(Adamantan-1-Yl)-2-(1H-Imidazol-1-Yl)Ethanone

All present enzymatic activity of Crystal Structure of Human Heme Oxygenase-1 in Complex with 1-(Adamantan-1-Yl)-2-(1H-Imidazol-1-Yl)Ethanone:
1.14.99.3;

The structure of Crystal Structure of Human Heme Oxygenase-1 in Complex with 1-(Adamantan-1-Yl)-2-(1H-Imidazol-1-Yl)Ethanone, PDB code: 3czy was solved by Z.Jia, M.N.Rahman, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	50.00 / 1.54
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	52.000, 52.446, 74.488, 90.00, 90.00, 90.00
R / Rfree (%)	19.4 / 22.6

The binding sites of Iron atom in the Crystal Structure of Human Heme Oxygenase-1 in Complex with 1-(Adamantan-1-Yl)-2-(1H-Imidazol-1-Yl)Ethanone (pdb code 3czy). 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 Human Heme Oxygenase-1 in Complex with 1-(Adamantan-1-Yl)-2-(1H-Imidazol-1-Yl)Ethanone, PDB code: 3czy:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in the Crystal Structure of Human Heme Oxygenase-1 in Complex with 1-(Adamantan-1-Yl)-2-(1H-Imidazol-1-Yl)Ethanone


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 Human Heme Oxygenase-1 in Complex with 1-(Adamantan-1-Yl)-2-(1H-Imidazol-1-Yl)Ethanone within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe300 b:10.8 occ:1.00 FE A:HEM300 0.0 10.8 1.0 NC A:HEM300 2.0 11.4 1.0 NA A:HEM300 2.0 12.6 1.0 ND A:HEM300 2.0 12.2 1.0 NE2 A:HIS25 2.0 13.2 1.0 NB A:HEM300 2.1 14.8 1.0 NAP A:AD8901 2.1 11.6 1.0 CD2 A:HIS25 3.0 11.6 1.0 CAO A:AD8901 3.0 12.1 1.0 CAQ A:AD8901 3.0 12.4 1.0 C1C A:HEM300 3.0 13.1 1.0 CE1 A:HIS25 3.0 14.0 1.0 C4C A:HEM300 3.0 11.8 1.0 C4D A:HEM300 3.1 10.6 1.0 C1A A:HEM300 3.1 13.7 1.0 C4A A:HEM300 3.1 15.5 1.0 C1D A:HEM300 3.1 10.4 1.0 C4B A:HEM300 3.1 15.1 1.0 C1B A:HEM300 3.1 16.0 1.0 CHA A:HEM300 3.4 13.8 1.0 CHC A:HEM300 3.4 14.2 1.0 CHD A:HEM300 3.4 13.1 1.0 CHB A:HEM300 3.4 16.6 1.0 ND1 A:HIS25 4.1 13.8 1.0 N A:AD8901 4.1 12.5 1.0 CG A:HIS25 4.1 13.0 1.0 CAN A:AD8901 4.2 12.0 1.0 C2C A:HEM300 4.2 13.6 1.0 C3C A:HEM300 4.3 13.1 1.0 C3A A:HEM300 4.3 16.4 1.0 C2D A:HEM300 4.3 11.0 1.0 C2A A:HEM300 4.3 16.2 1.0 C3D A:HEM300 4.3 12.4 1.0 C3B A:HEM300 4.3 16.7 1.0 C2B A:HEM300 4.3 16.6 1.0

Iron binding site 2 out of 2 in the Crystal Structure of Human Heme Oxygenase-1 in Complex with 1-(Adamantan-1-Yl)-2-(1H-Imidazol-1-Yl)Ethanone


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 Human Heme Oxygenase-1 in Complex with 1-(Adamantan-1-Yl)-2-(1H-Imidazol-1-Yl)Ethanone within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe300 b:10.9 occ:1.00 FE B:HEM300 0.0 10.9 1.0 NE2 B:HIS25 2.0 12.9 1.0 NC B:HEM300 2.0 10.6 1.0 ND B:HEM300 2.0 11.8 1.0 NAP B:AD8901 2.1 10.9 1.0 NA B:HEM300 2.1 12.1 1.0 NB B:HEM300 2.1 14.4 1.0 CE1 B:HIS25 2.9 12.6 1.0 CAQ B:AD8901 3.0 11.6 1.0 C4C B:HEM300 3.0 11.3 1.0 CD2 B:HIS25 3.0 12.0 1.0 CAO B:AD8901 3.0 11.8 1.0 C1D B:HEM300 3.1 9.9 1.0 C4D B:HEM300 3.1 11.5 1.0 C4A B:HEM300 3.1 15.5 1.0 C1C B:HEM300 3.1 13.3 1.0 C1B B:HEM300 3.1 15.7 1.0 C1A B:HEM300 3.1 14.0 1.0 C4B B:HEM300 3.1 15.1 1.0 CHD B:HEM300 3.4 11.4 1.0 CHA B:HEM300 3.4 13.1 1.0 CHB B:HEM300 3.4 16.1 1.0 CHC B:HEM300 3.5 13.9 1.0 ND1 B:HIS25 4.1 13.4 1.0 N B:AD8901 4.1 12.2 1.0 CG B:HIS25 4.1 11.9 1.0 CAN B:AD8901 4.2 11.8 1.0 C3C B:HEM300 4.3 13.3 1.0 C2C B:HEM300 4.3 14.2 1.0 C2D B:HEM300 4.3 11.9 1.0 C3A B:HEM300 4.3 16.3 1.0 C3D B:HEM300 4.3 12.9 1.0 C2A B:HEM300 4.3 16.3 1.0 C2B B:HEM300 4.3 16.8 1.0 C3B B:HEM300 4.3 16.8 1.0

M.N.Rahman, J.Z.Vlahakis, W.A.Szarek, K.Nakatsu, Z.Jia. X-Ray Crystal Structure of Human Heme Oxygenase-1 in Complex with 1-(Adamantan-1-Yl)-2-(1H-Imidazol-1-Yl)Ethanone: A Common Binding Mode For Imidazole-Based Heme Oxygenase-1 Inhibitors. J.Med.Chem. V. 51 5943 2008.
ISSN: ISSN 0022-2623
PubMed: 18798608
DOI: 10.1021/JM800505M