Iron in PDB 1ix4: Crystal Structure of Rat Heme Oxygenase-1 in Complex with Heme Bound to Carbon Monoxide

All present enzymatic activity of Crystal Structure of Rat Heme Oxygenase-1 in Complex with Heme Bound to Carbon Monoxide:
1.14.99.3;

The structure of Crystal Structure of Rat Heme Oxygenase-1 in Complex with Heme Bound to Carbon Monoxide, PDB code: 1ix4 was solved by M.Sugishima, H.Sakamoto, Y.Omata, S.Hayashi, M.Noguchi, K.Fukuyama, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	50.00 / 1.80
Space group	P 32 2 1
Cell size a, b, c (Å), α, β, γ (°)	66.000, 66.000, 120.240, 90.00, 90.00, 120.00
R / Rfree (%)	19.5 / 21.4

The binding sites of Iron atom in the Crystal Structure of Rat Heme Oxygenase-1 in Complex with Heme Bound to Carbon Monoxide (pdb code 1ix4). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total only one binding site of Iron was determined in the Crystal Structure of Rat Heme Oxygenase-1 in Complex with Heme Bound to Carbon Monoxide, PDB code: 1ix4:

Iron binding site 1 out of 1 in the Crystal Structure of Rat Heme Oxygenase-1 in Complex with Heme Bound to Carbon Monoxide


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 Rat Heme Oxygenase-1 in Complex with Heme Bound to Carbon Monoxide within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe300 b:21.4 occ:1.00 FE A:HEM300 0.0 21.4 1.0 C A:CMO1001 2.0 22.8 1.0 NC A:HEM300 2.0 21.7 1.0 ND A:HEM300 2.0 21.0 1.0 NB A:HEM300 2.0 23.5 1.0 NA A:HEM300 2.0 23.4 1.0 NE2 A:HIS25 2.2 22.1 1.0 O A:CMO1001 3.0 25.8 1.0 C4D A:HEM300 3.0 21.9 1.0 C4C A:HEM300 3.1 21.0 1.0 C1D A:HEM300 3.1 20.3 1.0 C4B A:HEM300 3.1 23.6 1.0 C1B A:HEM300 3.1 25.0 1.0 C1A A:HEM300 3.1 23.7 1.0 C4A A:HEM300 3.1 24.2 1.0 C1C A:HEM300 3.1 22.6 1.0 CE1 A:HIS25 3.1 23.3 1.0 CD2 A:HIS25 3.2 21.0 1.0 CHA A:HEM300 3.4 23.9 1.0 CHD A:HEM300 3.4 19.3 1.0 CHB A:HEM300 3.4 24.0 1.0 CHC A:HEM300 3.4 22.2 1.0 ND1 A:HIS25 4.2 21.9 1.0 CG A:HIS25 4.3 20.8 1.0 C3C A:HEM300 4.3 22.8 1.0 C3D A:HEM300 4.3 20.8 1.0 C2C A:HEM300 4.3 22.0 1.0 C3B A:HEM300 4.3 26.6 1.0 C2B A:HEM300 4.3 25.7 1.0 C2A A:HEM300 4.3 25.7 1.0 C3A A:HEM300 4.3 25.0 1.0 C2D A:HEM300 4.3 21.1 1.0 CA A:GLY143 4.6 26.2 1.0 N A:GLY143 4.7 26.2 1.0 CA A:GLY139 4.8 20.6 1.0 O A:HOH1108 4.8 30.2 1.0 O A:HOH1154 5.0 43.9 1.0

M.Sugishima, H.Sakamoto, M.Noguchi, K.Fukuyama. Crystal Structures of Ferrous and Co-, Cn(-)-, and No-Bound Forms of Rat Heme Oxygenase-1 (Ho-1) in Complex with Heme: Structural Implications For Discrimination Between Co and O(2) in Ho-1. Biochemistry V. 42 9898 2003.
ISSN: ISSN 0006-2960
PubMed: 12924938
DOI: 10.1021/BI027268I