Iron in PDB 1xk3: Nadph- and Ascorbate-Supported Heme Oxygenase Reactions Are Distinct. Regiospecificity of Heme Cleavage By the R183E Mutant

All present enzymatic activity of Nadph- and Ascorbate-Supported Heme Oxygenase Reactions Are Distinct. Regiospecificity of Heme Cleavage By the R183E Mutant:
1.14.99.3;

The structure of Nadph- and Ascorbate-Supported Heme Oxygenase Reactions Are Distinct. Regiospecificity of Heme Cleavage By the R183E Mutant, PDB code: 1xk3 was solved by J.Wang, L.Lad, T.L.Poulos, P.R.Ortiz De Montellano, 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 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	61.215, 54.483, 70.885, 90.00, 98.75, 90.00
R / Rfree (%)	21 / 23

The binding sites of Iron atom in the Nadph- and Ascorbate-Supported Heme Oxygenase Reactions Are Distinct. Regiospecificity of Heme Cleavage By the R183E Mutant (pdb code 1xk3). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 2 binding sites of Iron where determined in the Nadph- and Ascorbate-Supported Heme Oxygenase Reactions Are Distinct. Regiospecificity of Heme Cleavage By the R183E Mutant, PDB code: 1xk3:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in the Nadph- and Ascorbate-Supported Heme Oxygenase Reactions Are Distinct. Regiospecificity of Heme Cleavage By the R183E Mutant


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Nadph- and Ascorbate-Supported Heme Oxygenase Reactions Are Distinct. Regiospecificity of Heme Cleavage By the R183E Mutant within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe300 b:60.5 occ:1.00 FE A:HEM300 0.0 60.5 1.0 NC A:HEM300 2.0 60.5 1.0 NB A:HEM300 2.0 60.7 1.0 NA A:HEM300 2.0 60.7 1.0 ND A:HEM300 2.0 60.6 1.0 NE2 A:HIS25 2.1 59.2 1.0 N A:NO400 2.2 60.7 1.0 C4C A:HEM300 3.0 60.5 1.0 C1C A:HEM300 3.0 60.5 1.0 CE1 A:HIS25 3.0 58.0 1.0 C1B A:HEM300 3.1 61.0 1.0 C4B A:HEM300 3.1 60.8 1.0 C4A A:HEM300 3.1 60.9 1.0 C1A A:HEM300 3.1 60.9 1.0 C4D A:HEM300 3.1 60.8 1.0 C1D A:HEM300 3.1 60.6 1.0 CD2 A:HIS25 3.2 57.7 1.0 O A:NO400 3.2 60.8 1.0 CHC A:HEM300 3.4 60.7 1.0 CHD A:HEM300 3.4 60.5 1.0 CHB A:HEM300 3.4 60.9 1.0 CHA A:HEM300 3.4 60.8 1.0 ND1 A:HIS25 4.2 57.8 1.0 CG A:HIS25 4.3 57.3 1.0 C2C A:HEM300 4.3 60.5 1.0 C3A A:HEM300 4.3 60.9 1.0 C3C A:HEM300 4.3 60.4 1.0 C2A A:HEM300 4.3 60.9 1.0 C2B A:HEM300 4.3 61.0 1.0 C3B A:HEM300 4.3 61.0 1.0 C2D A:HEM300 4.3 60.7 1.0 C3D A:HEM300 4.3 60.8 1.0 O A:GLY139 4.7 40.4 1.0

Iron binding site 2 out of 2 in the Nadph- and Ascorbate-Supported Heme Oxygenase Reactions Are Distinct. Regiospecificity of Heme Cleavage By the R183E Mutant


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Nadph- and Ascorbate-Supported Heme Oxygenase Reactions Are Distinct. Regiospecificity of Heme Cleavage By the R183E Mutant within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe300 b:75.7 occ:1.00 FE B:HEM300 0.0 75.7 1.0 NA B:HEM300 2.0 75.9 1.0 ND B:HEM300 2.0 75.7 1.0 NB B:HEM300 2.0 75.9 1.0 NC B:HEM300 2.0 75.7 1.0 NE2 B:HIS25 2.1 74.3 1.0 CE1 B:HIS25 2.9 73.1 1.0 C1A B:HEM300 3.0 76.0 1.0 C4D B:HEM300 3.0 75.9 1.0 C4A B:HEM300 3.0 76.1 1.0 C1B B:HEM300 3.1 76.1 1.0 C4B B:HEM300 3.1 76.1 1.0 C1D B:HEM300 3.1 75.8 1.0 C1C B:HEM300 3.1 75.9 1.0 C4C B:HEM300 3.1 75.8 1.0 CD2 B:HIS25 3.3 72.7 1.0 CHA B:HEM300 3.4 75.9 1.0 CHD B:HEM300 3.4 75.8 1.0 CHC B:HEM300 3.4 76.0 1.0 CHB B:HEM300 3.5 76.1 1.0 ND1 B:HIS25 4.1 72.7 1.0 C2A B:HEM300 4.3 76.1 0.2 C3A B:HEM300 4.3 76.1 1.0 CG B:HIS25 4.3 72.1 1.0 C3D B:HEM300 4.3 75.9 1.0 C2B B:HEM300 4.3 76.2 1.0 C2D B:HEM300 4.3 75.8 1.0 C2C B:HEM300 4.3 75.8 1.0 C3B B:HEM300 4.3 76.2 1.0 C3C B:HEM300 4.3 75.8 1.0 OE1 B:GLU29 4.7 69.1 1.0 O B:GLY139 4.9 38.8 1.0

J.Wang, L.Lad, T.L.Poulos, P.R.Ortiz De Montellano. Regiospecificity Determinants of Human Heme Oxygenase: Differential Nadph- and Ascorbate-Dependent Heme Cleavage By the R183E Mutant. J.Biol.Chem. V. 280 2797 2005.
ISSN: ISSN 0021-9258
PubMed: 15525643
DOI: 10.1074/JBC.M411229200