Iron in PDB 4g8w: Rat Heme Oxygenase-1 in Complex with Heme and O2 with 13 Hr Illumination: Laser on

All present enzymatic activity of Rat Heme Oxygenase-1 in Complex with Heme and O2 with 13 Hr Illumination: Laser on:
1.14.99.3;

The structure of Rat Heme Oxygenase-1 in Complex with Heme and O2 with 13 Hr Illumination: Laser on, PDB code: 4g8w was solved by M.Sugishima, K.Moffat, M.Noguchi, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	28.76 / 2.40
Space group	P 32 2 1
Cell size a, b, c (Å), α, β, γ (°)	65.300, 65.300, 121.465, 90.00, 90.00, 120.00
R / Rfree (%)	16.6 / 22.8

The binding sites of Iron atom in the Rat Heme Oxygenase-1 in Complex with Heme and O2 with 13 Hr Illumination: Laser on (pdb code 4g8w). 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 Rat Heme Oxygenase-1 in Complex with Heme and O2 with 13 Hr Illumination: Laser on, PDB code: 4g8w:

Iron binding site 1 out of 1 in the Rat Heme Oxygenase-1 in Complex with Heme and O2 with 13 Hr Illumination: Laser on


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Rat Heme Oxygenase-1 in Complex with Heme and O2 with 13 Hr Illumination: Laser on within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe301 b:42.8 occ:1.00 FE A:HEM301 0.0 42.8 1.0 NC A:HEM301 1.9 37.9 1.0 NA A:HEM301 2.0 41.3 1.0 NB A:HEM301 2.1 45.6 1.0 NE2 A:HIS25 2.1 43.3 1.0 ND A:HEM301 2.1 39.3 1.0 O1 A:OXY302 2.2 36.5 0.4 O2 A:OXY302 2.9 37.1 0.4 C4C A:HEM301 3.0 36.9 1.0 C1C A:HEM301 3.0 40.2 1.0 CD2 A:HIS25 3.1 43.8 1.0 C4A A:HEM301 3.1 42.3 1.0 C4B A:HEM301 3.1 46.4 1.0 CE1 A:HIS25 3.1 45.6 1.0 C1B A:HEM301 3.1 49.1 1.0 C1D A:HEM301 3.1 37.1 1.0 C1A A:HEM301 3.1 45.6 1.0 C4D A:HEM301 3.1 38.3 1.0 CHD A:HEM301 3.4 36.7 1.0 CHB A:HEM301 3.5 45.4 1.0 CHC A:HEM301 3.5 42.6 1.0 CHA A:HEM301 3.5 43.1 1.0 C3C A:HEM301 4.2 39.9 1.0 ND1 A:HIS25 4.2 48.9 1.0 CG A:HIS25 4.2 45.2 1.0 C2C A:HEM301 4.3 43.1 1.0 C3A A:HEM301 4.4 50.3 1.0 C3B A:HEM301 4.4 49.8 1.0 N A:GLY143 4.4 54.6 1.0 C2A A:HEM301 4.4 51.7 1.0 C3D A:HEM301 4.4 40.7 1.0 C2B A:HEM301 4.4 47.3 1.0 C2D A:HEM301 4.4 40.9 1.0 CA A:GLY139 4.5 37.6 1.0 O A:HOH455 4.5 58.6 1.0 CA A:GLY143 4.6 61.5 1.0 CB A:SER142 4.8 46.6 1.0 O A:GLY139 4.9 40.6 1.0

M.Sugishima, K.Moffat, M.Noguchi. Discrimination Between Co and O2 in Heme Oxygenase: Comparison of Static Structures and Dynamic Conformation Changes Following Co Photolysis Biochemistry 2012.
ISSN: ISSN 0006-2960
PubMed: 23043644
DOI: 10.1021/BI301175X