Iron in PDB 2qpp: Crystal Structure of Human Heme Oxygenase-2 C127A (Ho-2) with Bound Heme

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

The structure of Crystal Structure of Human Heme Oxygenase-2 C127A (Ho-2) with Bound Heme, PDB code: 2qpp 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)	40.96 / 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 (%)	20.2 / 25.6

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

Iron binding site 1 out of 2 in the 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 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:56.9 occ:1.00 FE A:HEM300 0.0 56.9 1.0 NC A:HEM300 2.0 58.0 1.0 ND A:HEM300 2.1 56.8 1.0 NE2 A:HIS45 2.1 63.4 1.0 NA A:HEM300 2.1 58.6 1.0 NB A:HEM300 2.1 58.6 1.0 O A:HOH319 2.4 78.3 1.0 CE1 A:HIS45 2.9 64.0 1.0 C4C A:HEM300 3.0 57.4 1.0 C1D A:HEM300 3.1 56.1 1.0 C4D A:HEM300 3.1 56.8 1.0 C1B A:HEM300 3.1 58.9 1.0 C4A A:HEM300 3.1 59.7 1.0 C1C A:HEM300 3.1 58.3 1.0 C1A A:HEM300 3.1 59.7 1.0 C4B A:HEM300 3.1 58.6 1.0 CD2 A:HIS45 3.2 63.4 1.0 CHD A:HEM300 3.4 57.0 1.0 CHA A:HEM300 3.4 58.6 1.0 CHB A:HEM300 3.4 59.7 1.0 CHC A:HEM300 3.5 58.4 1.0 ND1 A:HIS45 4.1 63.4 1.0 CG A:HIS45 4.2 63.0 1.0 C3C A:HEM300 4.3 57.7 1.0 C3D A:HEM300 4.3 56.0 1.0 C2D A:HEM300 4.3 55.7 1.0 C2C A:HEM300 4.3 57.7 1.0 C3A A:HEM300 4.3 61.0 1.0 C2B A:HEM300 4.3 59.6 1.0 C2A A:HEM300 4.3 61.1 1.0 C3B A:HEM300 4.3 59.2 1.0 CA A:GLY159 4.6 55.4 1.0

Iron binding site 2 out of 2 in the 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 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:Fe300 b:79.3 occ:0.75 FE B:HEM300 0.0 79.3 0.8 NB B:HEM300 2.0 80.0 0.8 NC B:HEM300 2.1 79.8 0.8 ND B:HEM300 2.1 79.7 0.8 NA B:HEM300 2.1 80.0 0.8 NE2 B:HIS45 2.4 84.3 1.0 C4B B:HEM300 3.1 80.0 0.8 C4C B:HEM300 3.1 79.6 0.8 C1C B:HEM300 3.1 79.6 0.8 C1B B:HEM300 3.1 80.3 0.8 C1D B:HEM300 3.1 79.4 0.8 C4D B:HEM300 3.1 79.4 0.8 C4A B:HEM300 3.1 80.1 0.8 C1A B:HEM300 3.1 79.9 0.8 CE1 B:HIS45 3.2 84.3 1.0 CHC B:HEM300 3.4 79.9 0.8 CHD B:HEM300 3.4 79.4 0.8 CHA B:HEM300 3.5 79.7 0.8 CHB B:HEM300 3.5 80.2 0.8 CD2 B:HIS45 3.5 84.3 1.0 C3B B:HEM300 4.3 80.2 0.8 C3C B:HEM300 4.3 79.5 0.8 C2B B:HEM300 4.3 80.5 0.8 C2C B:HEM300 4.3 79.8 0.8 C3D B:HEM300 4.3 79.4 0.8 C2D B:HEM300 4.3 79.2 0.8 C3A B:HEM300 4.3 80.2 0.8 ND1 B:HIS45 4.3 84.3 1.0 C2A B:HEM300 4.4 80.1 0.8 CG B:HIS45 4.5 84.2 1.0 CA B:GLY159 4.6 70.6 1.0 O B:HOH324 4.8 63.8 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