Iron in PDB 1n45: X-Ray Crystal Structure of Human Heme Oxygenase-1 (Ho-1) in Complex with Its Substrate Heme

All present enzymatic activity of X-Ray Crystal Structure of Human Heme Oxygenase-1 (Ho-1) in Complex with Its Substrate Heme:
1.14.99.3;

The structure of X-Ray Crystal Structure of Human Heme Oxygenase-1 (Ho-1) in Complex with Its Substrate Heme, PDB code: 1n45 was solved by D.J.Schuller, A.Wilks, P.R.Ortiz De Montellano, T.L.Poulos, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	50.00 / 1.50
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	61.441, 54.534, 70.969, 90.00, 99.05, 90.00
R / Rfree (%)	14.9 / 21.7

The binding sites of Iron atom in the X-Ray Crystal Structure of Human Heme Oxygenase-1 (Ho-1) in Complex with Its Substrate Heme (pdb code 1n45). 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 (Ho-1) in Complex with Its Substrate Heme, PDB code: 1n45:
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 (Ho-1) in Complex with Its Substrate Heme


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 (Ho-1) in Complex with Its Substrate Heme within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe300 b:27.8 occ:1.00 FE A:HEM300 0.0 27.8 1.0 ND A:HEM300 2.0 22.3 1.0 NA A:HEM300 2.0 37.6 1.0 NC A:HEM300 2.0 23.9 1.0 NE2 A:HIS25 2.0 23.1 1.0 NB A:HEM300 2.0 38.1 1.0 O A:HOH301 2.0 40.2 1.0 CD2 A:HIS25 3.0 24.6 1.0 CE1 A:HIS25 3.0 25.2 1.0 C4A A:HEM300 3.0 38.3 1.0 C4C A:HEM300 3.0 22.8 1.0 C1D A:HEM300 3.0 20.1 1.0 C4D A:HEM300 3.0 24.7 1.0 C1B A:HEM300 3.0 40.1 1.0 C1C A:HEM300 3.0 26.2 1.0 C1A A:HEM300 3.0 34.9 1.0 C4B A:HEM300 3.1 34.7 1.0 CHB A:HEM300 3.4 37.8 1.0 CHA A:HEM300 3.4 28.8 1.0 CHD A:HEM300 3.4 22.3 1.0 CHC A:HEM300 3.4 32.3 1.0 ND1 A:HIS25 4.1 26.1 1.0 CG A:HIS25 4.1 27.8 1.0 C3A A:HEM300 4.2 40.6 1.0 C2A A:HEM300 4.2 43.1 1.0 C3C A:HEM300 4.2 25.1 1.0 C2D A:HEM300 4.2 22.5 1.0 C3D A:HEM300 4.2 22.9 1.0 C2C A:HEM300 4.3 26.9 1.0 C2B A:HEM300 4.3 39.6 1.0 C3B A:HEM300 4.3 36.8 1.0 O A:HOH444 4.6 40.4 1.0 O A:GLY139 4.7 24.1 1.0 CA A:GLY139 4.9 22.4 1.0

Iron binding site 2 out of 2 in the X-Ray Crystal Structure of Human Heme Oxygenase-1 (Ho-1) in Complex with Its Substrate Heme


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 (Ho-1) in Complex with Its Substrate Heme within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe300 b:33.6 occ:1.00 FE B:HEM300 0.0 33.6 1.0 NE2 B:HIS25 1.9 43.8 1.0 NA B:HEM300 2.0 46.9 1.0 ND B:HEM300 2.0 29.0 1.0 NC B:HEM300 2.0 34.0 1.0 NB B:HEM300 2.0 44.4 1.0 O B:HOH301 2.1 42.9 1.0 CE1 B:HIS25 2.7 45.1 1.0 C1B B:HEM300 3.0 49.4 1.0 C1D B:HEM300 3.0 26.3 1.0 C4A B:HEM300 3.0 56.7 1.0 C4C B:HEM300 3.0 33.3 1.0 C1A B:HEM300 3.0 46.5 1.0 C4D B:HEM300 3.0 27.9 1.0 C1C B:HEM300 3.0 37.0 1.0 C4B B:HEM300 3.0 42.2 1.0 CD2 B:HIS25 3.1 43.2 1.0 CHD B:HEM300 3.3 28.6 1.0 CHB B:HEM300 3.4 57.5 1.0 CHA B:HEM300 3.4 39.9 1.0 CHC B:HEM300 3.4 38.5 1.0 ND1 B:HIS25 3.9 45.2 1.0 CG B:HIS25 4.1 42.0 1.0 C3D B:HEM300 4.2 27.0 1.0 C2B B:HEM300 4.2 47.2 1.0 C2D B:HEM300 4.2 26.1 1.0 C2A B:HEM300 4.2 58.0 1.0 C3C B:HEM300 4.2 35.5 1.0 C3A B:HEM300 4.2 61.6 1.0 C2C B:HEM300 4.3 38.6 1.0 C3B B:HEM300 4.3 44.4 1.0 O B:HOH442 4.4 47.8 1.0 O B:HOH480 4.7 65.9 1.0 O B:GLY139 5.0 24.7 1.0

L.Lad, D.J.Schuller, H.Shimizu, J.Friedman, H.Li, P.R.Ortiz De Montellano, T.L.Poulos. Comparison of the Heme-Free and -Bound Crystal Structures of Human Heme Oxygenase-1. J. Biol. Chem. V. 278 7834 2003.
ISSN: ISSN 0021-9258
PubMed: 12500973
DOI: 10.1074/JBC.M211450200