Iron in PDB 1xk1: 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: 1xk1 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 / 2.08
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	54.103, 75.212, 107.380, 90.00, 90.00, 90.00
R / Rfree (%)	27.1 / n/a

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 1xk1). 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: 1xk1:
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:39.8 occ:1.00 FE A:HEM300 0.0 39.8 1.0 NE2 A:HIS143 1.9 41.3 1.0 NC A:HEM300 2.0 39.5 1.0 NA A:HEM300 2.0 40.3 1.0 ND A:HEM300 2.0 39.4 1.0 NB A:HEM300 2.0 40.9 1.0 NE2 A:HIS25 2.1 40.2 1.0 CE1 A:HIS143 2.3 41.1 1.0 C4C A:HEM300 3.0 39.8 1.0 C1C A:HEM300 3.0 40.5 1.0 C1D A:HEM300 3.0 37.8 1.0 C4A A:HEM300 3.1 40.8 1.0 C1B A:HEM300 3.1 41.0 1.0 C4D A:HEM300 3.1 38.8 1.0 CE1 A:HIS25 3.1 40.5 1.0 C1A A:HEM300 3.1 42.0 1.0 C4B A:HEM300 3.1 41.2 1.0 CD2 A:HIS25 3.1 39.0 1.0 CD2 A:HIS143 3.1 41.3 1.0 CHD A:HEM300 3.4 37.8 1.0 CHB A:HEM300 3.4 40.8 1.0 CHC A:HEM300 3.4 41.0 1.0 CHA A:HEM300 3.5 40.7 1.0 ND1 A:HIS143 3.6 42.4 1.0 CG A:HIS143 4.0 41.3 1.0 ND1 A:HIS25 4.2 40.9 1.0 CG A:HIS25 4.2 41.7 1.0 C3C A:HEM300 4.3 40.3 1.0 C2C A:HEM300 4.3 40.2 1.0 C3A A:HEM300 4.3 41.9 1.0 C2D A:HEM300 4.3 37.4 1.0 C3D A:HEM300 4.3 37.7 1.0 C2A A:HEM300 4.3 42.9 1.0 C2B A:HEM300 4.3 41.8 1.0 C3B A:HEM300 4.3 42.3 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:48.8 occ:1.00 FE B:HEM300 0.0 48.8 1.0 NC B:HEM300 2.0 47.7 1.0 NA B:HEM300 2.0 49.5 1.0 ND B:HEM300 2.0 48.1 1.0 NB B:HEM300 2.0 49.6 1.0 NE2 B:HIS25 2.1 48.3 1.0 CE1 B:HIS143 2.2 52.7 1.0 NE2 B:HIS143 2.2 50.6 1.0 C4C B:HEM300 3.0 46.6 1.0 C1C B:HEM300 3.0 48.0 1.0 C1D B:HEM300 3.0 46.1 1.0 C1A B:HEM300 3.1 50.5 1.0 C4D B:HEM300 3.1 47.9 1.0 C4B B:HEM300 3.1 48.6 1.0 C1B B:HEM300 3.1 49.0 1.0 C4A B:HEM300 3.1 50.1 1.0 CD2 B:HIS25 3.1 47.5 1.0 CE1 B:HIS25 3.1 47.8 1.0 CHD B:HEM300 3.4 46.3 1.0 ND1 B:HIS143 3.4 54.4 1.0 CHA B:HEM300 3.4 48.9 1.0 CHC B:HEM300 3.4 48.0 1.0 CHB B:HEM300 3.5 49.6 1.0 CD2 B:HIS143 3.5 53.7 1.0 CG B:HIS143 4.1 55.1 1.0 ND1 B:HIS25 4.2 47.1 1.0 CG B:HIS25 4.2 47.7 1.0 C3C B:HEM300 4.3 46.6 1.0 C2C B:HEM300 4.3 47.0 1.0 C2D B:HEM300 4.3 46.7 1.0 C2A B:HEM300 4.3 51.2 1.0 C3D B:HEM300 4.3 47.1 1.0 C2B B:HEM300 4.3 49.7 1.0 C3A B:HEM300 4.3 51.4 1.0 C3B B:HEM300 4.3 50.1 1.0 O B:GLY139 4.9 42.2 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