Iron in PDB 2rgz: Ensemble Refinement of the Protein Crystal Structure of Human Heme Oxygenase-2 C127A (Ho-2) with Bound Heme

All present enzymatic activity of Ensemble Refinement of the Protein Crystal Structure of Human Heme Oxygenase-2 C127A (Ho-2) with Bound Heme:
1.14.99.3;

The structure of Ensemble Refinement of the Protein Crystal Structure of Human Heme Oxygenase-2 C127A (Ho-2) with Bound Heme, PDB code: 2rgz was solved by C.M.Bianchetti, C.A.Bingman, E.Bitto, G.E.Wesenberg, G.N.Phillips Jr., Center For Eukaryotic Structural Genomics (Cesg), with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	39.02 / 2.61
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	74.977, 85.094, 97.846, 90.00, 90.00, 90.00
R / Rfree (%)	16.1 / 24.9

The binding sites of Iron atom in the Ensemble Refinement of the Protein Crystal Structure of Human Heme Oxygenase-2 C127A (Ho-2) with Bound Heme (pdb code 2rgz). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 2 binding sites of Iron where determined in the Ensemble Refinement of the Protein Crystal Structure of Human Heme Oxygenase-2 C127A (Ho-2) with Bound Heme, PDB code: 2rgz:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in the Ensemble Refinement of the Protein Crystal Structure of Human Heme Oxygenase-2 C127A (Ho-2) with Bound Heme


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Ensemble Refinement of the Protein Crystal Structure of Human Heme Oxygenase-2 C127A (Ho-2) with Bound Heme within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe300 b:50.1 occ:0.06 FE A:HEM300 0.0 50.1 0.1 NC A:HEM300 2.0 52.8 0.1 ND A:HEM300 2.0 51.3 0.1 NA A:HEM300 2.0 53.4 0.1 NB A:HEM300 2.0 55.2 0.1 NE2 A:HIS45 2.1 54.8 0.1 O A:HOH319 2.9 70.1 1.0 CE1 A:HIS45 2.9 56.8 0.1 C4D A:HEM300 3.0 52.0 0.1 C1A A:HEM300 3.0 55.6 0.1 C4C A:HEM300 3.0 51.0 0.1 C1C A:HEM300 3.0 53.8 0.1 C4A A:HEM300 3.0 53.6 0.1 C1D A:HEM300 3.0 49.5 0.1 C1B A:HEM300 3.0 55.5 0.1 C4B A:HEM300 3.0 55.2 0.1 CD2 A:HIS45 3.3 57.5 0.1 CHA A:HEM300 3.4 55.5 0.1 CHD A:HEM300 3.4 49.7 0.1 CHC A:HEM300 3.4 55.5 0.1 CHB A:HEM300 3.4 56.1 0.1 ND1 A:HIS45 4.1 57.7 0.1 C3D A:HEM300 4.2 50.4 0.1 C2C A:HEM300 4.2 52.5 0.1 C2A A:HEM300 4.2 56.1 0.1 C3A A:HEM300 4.3 55.7 0.1 C3C A:HEM300 4.3 52.0 0.1 C2D A:HEM300 4.3 49.8 0.1 C2B A:HEM300 4.3 55.9 0.1 C3B A:HEM300 4.3 55.7 0.1 CG A:HIS45 4.3 57.4 0.1 CA A:GLY159 4.7 43.1 0.1 CB A:SER162 4.9 46.7 0.1

Iron binding site 2 out of 2 in the Ensemble Refinement of the Protein Crystal Structure of Human Heme Oxygenase-2 C127A (Ho-2) with Bound Heme


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Ensemble Refinement of the Protein Crystal Structure of Human Heme Oxygenase-2 C127A (Ho-2) with Bound Heme within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe265 b:64.2 occ:0.06 FE B:HEM265 0.0 64.2 0.1 NC B:HEM265 2.0 64.3 0.1 ND B:HEM265 2.0 64.2 0.1 NB B:HEM265 2.0 65.0 0.1 NA B:HEM265 2.0 64.0 0.1 NE2 B:HIS45 2.1 64.3 0.1 C1C B:HEM265 3.0 64.3 0.1 C4C B:HEM265 3.0 64.8 0.1 C4B B:HEM265 3.0 63.8 0.1 C4D B:HEM265 3.0 64.0 0.1 C1A B:HEM265 3.0 63.7 0.1 C1D B:HEM265 3.0 64.0 0.1 C1B B:HEM265 3.0 65.8 0.1 C4A B:HEM265 3.0 64.3 0.1 CE1 B:HIS45 3.1 63.3 0.1 CD2 B:HIS45 3.1 64.1 0.1 CHC B:HEM265 3.4 64.0 0.1 CHA B:HEM265 3.4 63.7 0.1 CHD B:HEM265 3.4 64.1 0.1 CHB B:HEM265 3.4 65.0 0.1 ND1 B:HIS45 4.2 62.3 0.1 C2C B:HEM265 4.3 65.7 0.1 C3C B:HEM265 4.3 64.0 0.1 C2D B:HEM265 4.3 64.1 0.1 CG B:HIS45 4.3 63.0 0.1 C3D B:HEM265 4.3 64.1 0.1 C3B B:HEM265 4.3 64.3 0.1 C2B B:HEM265 4.3 65.4 0.1 C3A B:HEM265 4.3 64.1 0.1 C2A B:HEM265 4.3 63.7 0.1 O B:HOH289 4.8 67.0 1.0

C.M.Bianchetti, L.Yi, S.W.Ragsdale, G.N.Phillips Jr.. Comparison of Apo- and Heme-Bound Crystal Structures of A Truncated Human Heme Oxygenase-2. J.Biol.Chem. V. 282 37624 2007.
ISSN: ISSN 0021-9258
PubMed: 17965015
DOI: 10.1074/JBC.M707396200