Iron in PDB 1xjz: Crystal Structures of the G139A, G139A-No and G143H Mutants of Human Heme Oxygenase-1

All present enzymatic activity of Crystal Structures of the G139A, G139A-No and G143H Mutants of Human Heme Oxygenase-1:
1.14.99.3;

The structure of Crystal Structures of the G139A, G139A-No and G143H Mutants of Human Heme Oxygenase-1, PDB code: 1xjz was solved by L.Lad, P.R.Ortiz De Montellano, T.L.Poulos, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	50.00 / 1.88
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	54.251, 75.985, 106.859, 90.00, 90.00, 90.00
R / Rfree (%)	22.2 / 24.8

The binding sites of Iron atom in the Crystal Structures of the G139A, G139A-No and G143H Mutants of Human Heme Oxygenase-1 (pdb code 1xjz). 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 Structures of the G139A, G139A-No and G143H Mutants of Human Heme Oxygenase-1, PDB code: 1xjz:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in the Crystal Structures of the G139A, G139A-No and G143H Mutants of Human Heme Oxygenase-1


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Crystal Structures of the G139A, G139A-No and G143H Mutants of Human Heme Oxygenase-1 within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe300 b:38.4 occ:1.00 FE A:HEM300 0.0 38.4 1.0 NA A:HEM300 2.0 38.5 1.0 ND A:HEM300 2.0 38.2 1.0 NC A:HEM300 2.0 38.3 1.0 NB A:HEM300 2.0 38.4 1.0 O A:HOH363 2.1 38.3 1.0 NE2 A:HIS25 2.1 39.1 1.0 C1D A:HEM300 3.0 38.1 1.0 C1A A:HEM300 3.0 38.4 1.0 C4D A:HEM300 3.0 38.2 1.0 CE1 A:HIS25 3.0 39.7 1.0 C4A A:HEM300 3.0 38.5 1.0 C4C A:HEM300 3.0 38.2 1.0 C1C A:HEM300 3.1 38.2 1.0 C1B A:HEM300 3.1 38.5 1.0 C4B A:HEM300 3.1 38.4 1.0 CD2 A:HIS25 3.1 39.9 1.0 CHD A:HEM300 3.4 38.1 1.0 CHA A:HEM300 3.4 38.2 1.0 CHB A:HEM300 3.4 38.6 1.0 CHC A:HEM300 3.5 38.3 1.0 ND1 A:HIS25 4.2 40.0 1.0 CG A:HIS25 4.2 40.1 1.0 C2D A:HEM300 4.3 38.0 1.0 C2A A:HEM300 4.3 38.5 1.0 C3D A:HEM300 4.3 38.1 1.0 C3A A:HEM300 4.3 38.6 1.0 C2C A:HEM300 4.3 38.2 1.0 C3C A:HEM300 4.3 38.1 1.0 C2B A:HEM300 4.3 38.5 1.0 C3B A:HEM300 4.3 38.5 1.0 O A:HOH482 4.5 49.5 1.0 O A:HOH364 5.0 55.9 1.0

Iron binding site 2 out of 2 in the Crystal Structures of the G139A, G139A-No and G143H Mutants of Human Heme Oxygenase-1


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Crystal Structures of the G139A, G139A-No and G143H Mutants of Human Heme Oxygenase-1 within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe300 b:38.5 occ:1.00 FE B:HEM300 0.0 38.5 1.0 NB B:HEM300 2.0 38.6 1.0 NC B:HEM300 2.0 38.4 1.0 ND B:HEM300 2.0 38.5 1.0 NA B:HEM300 2.0 38.8 1.0 O B:HOH388 2.1 38.6 1.0 NE2 B:HIS25 2.1 38.8 1.0 C1B B:HEM300 3.0 38.8 1.0 C4B B:HEM300 3.0 38.6 1.0 C1C B:HEM300 3.0 38.4 1.0 C4C B:HEM300 3.0 38.3 1.0 C1D B:HEM300 3.0 38.4 1.0 C4A B:HEM300 3.1 38.9 1.0 C4D B:HEM300 3.1 38.6 1.0 CD2 B:HIS25 3.1 39.1 1.0 C1A B:HEM300 3.1 38.9 1.0 CE1 B:HIS25 3.1 39.0 1.0 CHB B:HEM300 3.4 38.9 1.0 CHD B:HEM300 3.4 38.3 1.0 CHC B:HEM300 3.4 38.5 1.0 CHA B:HEM300 3.5 38.7 1.0 ND1 B:HIS25 4.2 39.0 1.0 CG B:HIS25 4.2 39.2 1.0 C2B B:HEM300 4.2 38.7 1.0 C3B B:HEM300 4.3 38.7 1.0 C2D B:HEM300 4.3 38.4 1.0 C2C B:HEM300 4.3 38.3 1.0 C3C B:HEM300 4.3 38.3 1.0 C3D B:HEM300 4.3 38.5 1.0 C3A B:HEM300 4.3 39.0 1.0 C2A B:HEM300 4.3 39.0 1.0

L.Lad, A.Koshkin, P.R.Ortiz De Montellano, T.L.Poulos. Crystal Structures of the G139A, G139A-No and G143H Mutants of Human Heme Oxygenase-1. A Finely Tuned Hydrogen-Bonding Network Controls Oxygenase Versus Peroxidase Activity. J.Biol.Inorg.Chem. V. 10 138 2005.
ISSN: ISSN 0949-8257
PubMed: 15690204
DOI: 10.1007/S00775-004-0620-6