Iron in PDB 1xk0: 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: 1xk0 was solved by L.Lad, A.Koshkin, 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 / 2.18
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	54.060, 75.968, 105.299, 90.00, 90.00, 90.00
R / Rfree (%)	22.4 / 26.6

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 1xk0). 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: 1xk0:
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:53.0 occ:1.00 FE A:HEM300 0.0 53.0 1.0 NA A:HEM300 2.0 53.4 1.0 N A:NO400 2.0 53.2 1.0 NC A:HEM300 2.0 52.8 1.0 ND A:HEM300 2.0 52.8 1.0 NB A:HEM300 2.0 53.4 1.0 NE2 A:HIS25 2.1 54.2 1.0 O A:NO400 3.0 53.8 1.0 CE1 A:HIS25 3.0 55.3 1.0 C1A A:HEM300 3.0 53.7 1.0 C4A A:HEM300 3.0 53.7 1.0 C1D A:HEM300 3.0 52.1 1.0 C4C A:HEM300 3.0 52.4 1.0 C4D A:HEM300 3.1 52.6 1.0 C1C A:HEM300 3.1 52.6 1.0 C1B A:HEM300 3.1 53.4 1.0 C4B A:HEM300 3.1 53.2 1.0 CD2 A:HIS25 3.2 55.5 1.0 CHD A:HEM300 3.4 52.3 1.0 CHA A:HEM300 3.4 53.1 1.0 CHB A:HEM300 3.4 53.7 1.0 CHC A:HEM300 3.5 52.9 1.0 ND1 A:HIS25 4.1 55.7 1.0 CG A:HIS25 4.2 55.5 1.0 C2A A:HEM300 4.2 54.3 1.0 C3A A:HEM300 4.2 54.1 1.0 C2D A:HEM300 4.3 52.0 1.0 C3C A:HEM300 4.3 52.5 1.0 C3D A:HEM300 4.3 52.1 1.0 C2C A:HEM300 4.3 52.5 1.0 C2B A:HEM300 4.3 53.7 1.0 C3B A:HEM300 4.4 53.6 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:53.4 occ:1.00 FE B:HEM300 0.0 53.4 1.0 NB B:HEM300 2.0 53.7 1.0 ND B:HEM300 2.0 53.4 1.0 NC B:HEM300 2.0 53.0 1.0 NA B:HEM300 2.0 54.3 1.0 NE2 B:HIS25 2.1 53.5 1.0 CE1 B:HIS25 3.0 53.1 1.0 C1D B:HEM300 3.0 53.1 1.0 C4D B:HEM300 3.0 53.6 1.0 C4B B:HEM300 3.0 53.6 1.0 C1B B:HEM300 3.0 53.8 1.0 C4C B:HEM300 3.0 52.8 1.0 C1C B:HEM300 3.1 52.9 1.0 C4A B:HEM300 3.1 54.5 1.0 C1A B:HEM300 3.1 54.6 1.0 CD2 B:HIS25 3.1 53.0 1.0 CHD B:HEM300 3.4 52.8 1.0 CHC B:HEM300 3.4 53.0 1.0 CHA B:HEM300 3.4 54.1 1.0 CHB B:HEM300 3.5 54.1 1.0 ND1 B:HIS25 4.1 53.1 1.0 CG B:HIS25 4.2 52.7 1.0 C2D B:HEM300 4.3 53.3 1.0 C3D B:HEM300 4.3 53.6 1.0 C3B B:HEM300 4.3 53.9 1.0 C2B B:HEM300 4.3 53.8 1.0 C3A B:HEM300 4.3 55.1 1.0 C3C B:HEM300 4.3 52.7 1.0 C2C B:HEM300 4.3 52.6 1.0 C2A B:HEM300 4.3 55.3 1.0 O B:HOH359 4.9 44.6 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