Iron in PDB 1ulx: Partially Photolyzed Structure of Co-Bound Heme-Heme Oxygenase Complex

All present enzymatic activity of Partially Photolyzed Structure of Co-Bound Heme-Heme Oxygenase Complex:
1.14.99.3;

The structure of Partially Photolyzed Structure of Co-Bound Heme-Heme Oxygenase Complex, PDB code: 1ulx was solved by M.Sugishima, H.Sakamoto, M.Noguchi, K.Fukuyama, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	20.00 / 2.00
Space group	P 32 2 1
Cell size a, b, c (Å), α, β, γ (°)	65.900, 65.900, 120.100, 90.00, 90.00, 120.00
R / Rfree (%)	20.7 / 23.9

The binding sites of Iron atom in the Partially Photolyzed Structure of Co-Bound Heme-Heme Oxygenase Complex (pdb code 1ulx). 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 Partially Photolyzed Structure of Co-Bound Heme-Heme Oxygenase Complex, PDB code: 1ulx:

Iron binding site 1 out of 1 in the Partially Photolyzed Structure of Co-Bound Heme-Heme Oxygenase Complex


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Partially Photolyzed Structure of Co-Bound Heme-Heme Oxygenase Complex within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe300 b:27.2 occ:1.00 FE A:HEM300 0.0 27.2 1.0 C A:CMO301 1.8 25.8 0.7 ND A:HEM300 2.0 25.5 1.0 NC A:HEM300 2.0 26.4 1.0 NB A:HEM300 2.0 28.1 1.0 NA A:HEM300 2.0 28.1 1.0 NE2 A:HIS25 2.2 25.1 1.0 O A:CMO301 2.9 25.3 0.7 C4D A:HEM300 3.0 27.2 1.0 C1D A:HEM300 3.1 24.2 1.0 C4C A:HEM300 3.1 24.3 1.0 C1B A:HEM300 3.1 27.8 1.0 C4B A:HEM300 3.1 28.2 1.0 C4A A:HEM300 3.1 29.8 1.0 C1A A:HEM300 3.1 28.2 1.0 C1C A:HEM300 3.1 25.9 1.0 CE1 A:HIS25 3.1 26.0 1.0 CD2 A:HIS25 3.2 24.2 1.0 C A:CMO302 3.4 25.1 0.1 CHD A:HEM300 3.4 23.9 1.0 CHA A:HEM300 3.4 28.0 1.0 CHB A:HEM300 3.4 28.3 1.0 CHC A:HEM300 3.4 27.6 1.0 O A:CMO302 4.2 25.2 0.1 ND1 A:HIS25 4.2 27.5 1.0 CG A:HIS25 4.3 25.8 1.0 C3C A:HEM300 4.3 25.4 1.0 C3D A:HEM300 4.3 25.2 1.0 C2A A:HEM300 4.3 30.8 1.0 C3B A:HEM300 4.3 28.5 1.0 C3A A:HEM300 4.3 29.3 1.0 C2B A:HEM300 4.3 27.9 1.0 C2C A:HEM300 4.3 27.2 1.0 C2D A:HEM300 4.3 23.7 1.0 CA A:GLY143 4.6 29.4 1.0 CA A:GLY139 4.7 23.4 1.0 N A:GLY143 4.8 28.7 1.0 O A:HOH382 4.9 27.7 1.0

M.Sugishima, H.Sakamoto, M.Noguchi, K.Fukuyama. Co-Trapping Site in Heme Oxygenase Revealed By Photolysis of Its Co-Bound Heme Complex: Mechanism of Escaping From Product Inhibition J.Mol.Biol. V. 341 7 2004.
ISSN: ISSN 0022-2836
PubMed: 15312758
DOI: 10.1016/J.JMB.2004.05.048