Iron in PDB 3tgm: X-Ray Crystal Structure of Human Heme Oxygenase-1 in Complex with 1- (1H-Imidazol-1-Yl)-4,4-Diphenyl-2 Butanone

All present enzymatic activity of X-Ray Crystal Structure of Human Heme Oxygenase-1 in Complex with 1- (1H-Imidazol-1-Yl)-4,4-Diphenyl-2 Butanone:
1.14.99.3;

The structure of X-Ray Crystal Structure of Human Heme Oxygenase-1 in Complex with 1- (1H-Imidazol-1-Yl)-4,4-Diphenyl-2 Butanone, PDB code: 3tgm was solved by M.N.Rahman, Z.Jia, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	19.82 / 2.85
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	54.610, 74.980, 115.280, 90.00, 90.00, 90.00
R / Rfree (%)	22.3 / 26.4

The binding sites of Iron atom in the X-Ray Crystal Structure of Human Heme Oxygenase-1 in Complex with 1- (1H-Imidazol-1-Yl)-4,4-Diphenyl-2 Butanone (pdb code 3tgm). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 2 binding sites of Iron where determined in the X-Ray Crystal Structure of Human Heme Oxygenase-1 in Complex with 1- (1H-Imidazol-1-Yl)-4,4-Diphenyl-2 Butanone, PDB code: 3tgm:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in the X-Ray Crystal Structure of Human Heme Oxygenase-1 in Complex with 1- (1H-Imidazol-1-Yl)-4,4-Diphenyl-2 Butanone


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of X-Ray Crystal Structure of Human Heme Oxygenase-1 in Complex with 1- (1H-Imidazol-1-Yl)-4,4-Diphenyl-2 Butanone within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe300 b:65.2 occ:1.00 FE A:HEM300 0.0 65.2 1.0 NC A:HEM300 2.0 65.2 1.0 NB A:HEM300 2.1 65.9 1.0 ND A:HEM300 2.1 65.0 1.0 NE2 A:HIS25 2.1 81.5 1.0 NA A:HEM300 2.1 65.7 1.0 NAQ A:3TG301 2.2 73.1 1.0 CAN A:3TG301 3.0 73.0 1.0 C4C A:HEM300 3.0 65.1 1.0 CE1 A:HIS25 3.0 81.5 1.0 C1C A:HEM300 3.1 65.3 1.0 C1B A:HEM300 3.1 66.2 1.0 C4A A:HEM300 3.1 66.1 1.0 C1D A:HEM300 3.1 64.7 1.0 C4B A:HEM300 3.1 66.0 1.0 C1A A:HEM300 3.1 65.8 1.0 C4D A:HEM300 3.1 65.1 1.0 CD2 A:HIS25 3.1 81.7 1.0 CAH A:3TG301 3.2 73.1 1.0 CHD A:HEM300 3.4 64.9 1.0 CHB A:HEM300 3.4 66.3 1.0 CHC A:HEM300 3.4 65.8 1.0 CHA A:HEM300 3.4 65.5 1.0 N A:3TG301 4.1 73.0 1.0 ND1 A:HIS25 4.2 81.8 1.0 CAM A:3TG301 4.2 73.1 1.0 CG A:HIS25 4.2 82.0 1.0 C3C A:HEM300 4.3 65.2 1.0 C3A A:HEM300 4.3 66.2 1.0 C2A A:HEM300 4.3 66.3 1.0 C2C A:HEM300 4.3 65.3 1.0 C2B A:HEM300 4.3 66.3 1.0 C3B A:HEM300 4.3 66.3 1.0 C2D A:HEM300 4.3 64.6 1.0 C3D A:HEM300 4.3 64.8 1.0

Iron binding site 2 out of 2 in the X-Ray Crystal Structure of Human Heme Oxygenase-1 in Complex with 1- (1H-Imidazol-1-Yl)-4,4-Diphenyl-2 Butanone


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of X-Ray Crystal Structure of Human Heme Oxygenase-1 in Complex with 1- (1H-Imidazol-1-Yl)-4,4-Diphenyl-2 Butanone within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe300 b:53.3 occ:1.00 FE B:HEM300 0.0 53.3 1.0 NC B:HEM300 2.0 53.2 1.0 ND B:HEM300 2.1 53.0 1.0 NB B:HEM300 2.1 53.8 1.0 NAQ B:3TG301 2.1 55.7 1.0 NA B:HEM300 2.1 53.9 1.0 NE2 B:HIS25 2.4 64.1 1.0 CE1 B:HIS25 3.0 64.0 1.0 C4C B:HEM300 3.0 53.0 1.0 CAN B:3TG301 3.0 55.8 1.0 C1C B:HEM300 3.0 53.5 1.0 C1D B:HEM300 3.1 52.6 1.0 C1B B:HEM300 3.1 54.4 1.0 C4D B:HEM300 3.1 52.9 1.0 C4B B:HEM300 3.1 54.1 1.0 C4A B:HEM300 3.1 54.0 1.0 CAH B:3TG301 3.1 55.8 1.0 C1A B:HEM300 3.1 54.0 1.0 CHD B:HEM300 3.4 52.6 1.0 CHC B:HEM300 3.4 54.0 1.0 CHB B:HEM300 3.4 54.1 1.0 CHA B:HEM300 3.4 53.5 1.0 CD2 B:HIS25 3.5 64.2 1.0 ND1 B:HIS25 4.1 64.3 1.0 N B:3TG301 4.2 55.8 1.0 CAM B:3TG301 4.2 55.8 1.0 C3C B:HEM300 4.2 53.4 1.0 C2C B:HEM300 4.3 53.6 1.0 C2B B:HEM300 4.3 54.6 1.0 C3B B:HEM300 4.3 54.5 1.0 C2D B:HEM300 4.3 52.3 1.0 C3D B:HEM300 4.3 52.5 1.0 C3A B:HEM300 4.3 54.3 1.0 C2A B:HEM300 4.3 54.5 1.0 CG B:HIS25 4.4 64.4 1.0

M.N.Rahman, J.Z.Vlahakis, D.Vukomanovic, W.Lee, W.A.Szarek, K.Nakatsu, Z.Jia. A Novel, "Double-Clamp" Binding Mode For Human Heme Oxygenase-1 Inhibition. Plos One V. 7 29514 2012.
ISSN: ESSN 1932-6203
PubMed: 22276118
DOI: 10.1371/JOURNAL.PONE.0029514