Iron in PDB 4g99: Rat Heme Oxygenase-1 in Complex with Heme and Co at 100 K After Warming to 160 K

All present enzymatic activity of Rat Heme Oxygenase-1 in Complex with Heme and Co at 100 K After Warming to 160 K:
1.14.99.3;

The structure of Rat Heme Oxygenase-1 in Complex with Heme and Co at 100 K After Warming to 160 K, PDB code: 4g99 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)	32.97 / 2.30
Space group	P 32 2 1
Cell size a, b, c (Å), α, β, γ (°)	65.939, 65.939, 120.119, 90.00, 90.00, 120.00
R / Rfree (%)	16.1 / 22.1

The binding sites of Iron atom in the Rat Heme Oxygenase-1 in Complex with Heme and Co at 100 K After Warming to 160 K (pdb code 4g99). 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 Co at 100 K After Warming to 160 K, PDB code: 4g99:

Iron binding site 1 out of 1 in the Rat Heme Oxygenase-1 in Complex with Heme and Co at 100 K After Warming to 160 K


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 Co at 100 K After Warming to 160 K within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe301 b:32.0 occ:1.00 FE A:HEM301 0.0 32.0 1.0 C A:CMO302 1.8 27.6 1.0 NC A:HEM301 1.9 30.4 1.0 NA A:HEM301 2.0 33.1 1.0 NE2 A:HIS25 2.0 32.2 1.0 ND A:HEM301 2.1 28.6 1.0 NB A:HEM301 2.1 32.4 1.0 C4C A:HEM301 2.9 27.8 1.0 CD2 A:HIS25 3.0 30.5 1.0 O A:CMO302 3.0 30.1 1.0 CE1 A:HIS25 3.0 29.6 1.0 C1A A:HEM301 3.0 33.0 1.0 C1D A:HEM301 3.0 26.9 1.0 C1C A:HEM301 3.1 31.2 1.0 C4D A:HEM301 3.1 30.2 1.0 C4B A:HEM301 3.1 33.1 1.0 C4A A:HEM301 3.1 34.3 1.0 C1B A:HEM301 3.2 32.1 1.0 CHD A:HEM301 3.3 25.1 1.0 CHA A:HEM301 3.5 30.4 1.0 CHC A:HEM301 3.5 31.2 1.0 CHB A:HEM301 3.6 33.4 1.0 ND1 A:HIS25 4.1 33.3 1.0 CG A:HIS25 4.1 34.4 1.0 C3C A:HEM301 4.2 29.7 1.0 C2C A:HEM301 4.3 31.7 1.0 C2A A:HEM301 4.3 32.7 1.0 C3A A:HEM301 4.4 36.2 1.0 C3D A:HEM301 4.4 28.9 1.0 C2D A:HEM301 4.4 27.3 1.0 C3B A:HEM301 4.4 30.9 1.0 C2B A:HEM301 4.5 32.9 1.0 O A:HOH500 4.7 33.2 1.0 O A:HOH533 4.7 56.2 1.0 CA A:GLY143 4.7 35.6 1.0 CA A:GLY139 4.8 26.0 1.0 N A:GLY143 4.9 30.6 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