Iron in PDB 3wkt: Complex Structure of An Open Form of Nadph-Cytochrome P450 Reductase and Heme Oxygenase-1

All present enzymatic activity of Complex Structure of An Open Form of Nadph-Cytochrome P450 Reductase and Heme Oxygenase-1:
1.14.99.3; 1.6.2.4;

The structure of Complex Structure of An Open Form of Nadph-Cytochrome P450 Reductase and Heme Oxygenase-1, PDB code: 3wkt was solved by M.Sugishima, H.Sato, Y.Higashimoto, J.Harada, K.Wada, K.Fukuyama, M.Noguchi, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	41.34 / 4.30
Space group	P 61
Cell size a, b, c (Å), α, β, γ (°)	290.336, 290.336, 83.646, 90.00, 90.00, 120.00
R / Rfree (%)	22.2 / 25.6

The binding sites of Iron atom in the Complex Structure of An Open Form of Nadph-Cytochrome P450 Reductase and Heme Oxygenase-1 (pdb code 3wkt). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 2 binding sites of Iron where determined in the Complex Structure of An Open Form of Nadph-Cytochrome P450 Reductase and Heme Oxygenase-1, PDB code: 3wkt:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in the Complex Structure of An Open Form of Nadph-Cytochrome P450 Reductase and 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 Complex Structure of An Open Form of Nadph-Cytochrome P450 Reductase and Heme Oxygenase-1 within 5.0Å range: probe atom residue distance (Å) B Occ C:Fe300 b:0.5 occ:1.00 FE C:HEM300 0.0 0.5 1.0 ND C:HEM300 1.9 0.1 1.0 NA C:HEM300 2.0 0.8 1.0 NC C:HEM300 2.1 0.7 1.0 NB C:HEM300 2.1 0.1 1.0 NE2 C:HIS25 2.9 0.9 1.0 C4D C:HEM300 2.9 0.1 1.0 C1D C:HEM300 2.9 0.3 1.0 C1A C:HEM300 3.0 0.5 1.0 C4C C:HEM300 3.1 0.8 1.0 C4A C:HEM300 3.1 0.9 1.0 C4B C:HEM300 3.1 0.0 1.0 C1C C:HEM300 3.1 0.8 1.0 C1B C:HEM300 3.1 0.0 1.0 CD2 C:HIS25 3.3 0.8 1.0 CHA C:HEM300 3.4 0.2 1.0 CHD C:HEM300 3.4 0.5 1.0 CHC C:HEM300 3.5 0.7 1.0 CHB C:HEM300 3.5 0.8 1.0 CE1 C:HIS25 4.1 0.8 1.0 C3D C:HEM300 4.2 0.3 1.0 C2D C:HEM300 4.2 0.0 1.0 C2A C:HEM300 4.2 0.1 1.0 C2C C:HEM300 4.3 0.6 1.0 C3C C:HEM300 4.3 0.9 1.0 C3A C:HEM300 4.3 0.9 1.0 C2B C:HEM300 4.3 0.8 1.0 C3B C:HEM300 4.3 0.5 1.0 CB C:SER142 4.5 0.3 1.0 CG C:HIS25 4.6 0.0 1.0 N C:GLY143 4.7 0.6 1.0 CA C:GLY139 4.7 0.2 1.0 ND1 C:HIS25 4.9 0.1 1.0

Iron binding site 2 out of 2 in the Complex Structure of An Open Form of Nadph-Cytochrome P450 Reductase and 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 Complex Structure of An Open Form of Nadph-Cytochrome P450 Reductase and Heme Oxygenase-1 within 5.0Å range: probe atom residue distance (Å) B Occ D:Fe300 b:0.0 occ:1.00 FE D:HEM300 0.0 0.0 1.0 ND D:HEM300 1.9 0.3 1.0 NA D:HEM300 2.0 0.5 1.0 NB D:HEM300 2.1 0.4 1.0 NC D:HEM300 2.1 0.5 1.0 NE2 D:HIS25 2.8 0.9 1.0 C1D D:HEM300 2.9 0.6 1.0 C4D D:HEM300 2.9 0.4 1.0 C1A D:HEM300 3.0 1.0 1.0 C4A D:HEM300 3.0 0.4 1.0 C4B D:HEM300 3.1 0.9 1.0 C1B D:HEM300 3.1 0.9 1.0 C4C D:HEM300 3.1 0.7 1.0 C1C D:HEM300 3.1 0.7 1.0 CHA D:HEM300 3.4 0.3 1.0 CHD D:HEM300 3.4 0.4 1.0 CHB D:HEM300 3.4 0.5 1.0 CHC D:HEM300 3.5 0.8 1.0 CD2 D:HIS25 3.7 0.8 1.0 CE1 D:HIS25 3.7 0.7 1.0 C2D D:HEM300 4.1 0.6 1.0 C3D D:HEM300 4.2 0.9 1.0 C2A D:HEM300 4.2 0.4 1.0 C3A D:HEM300 4.2 0.6 1.0 C2B D:HEM300 4.3 0.6 1.0 C3C D:HEM300 4.3 0.0 1.0 C3B D:HEM300 4.3 0.6 1.0 C2C D:HEM300 4.3 0.8 1.0 CA D:GLY139 4.5 1.0 1.0 ND1 D:HIS25 4.8 0.2 1.0 CG D:HIS25 4.9 0.2 1.0 N D:GLY143 5.0 0.7 1.0

M.Sugishima, H.Sato, Y.Higashimoto, J.Harada, K.Wada, K.Fukuyama, M.Noguchi. Structural Basis For the Electron Transfer From An Open Form of Nadph-Cytochrome P450 Oxidoreductase to Heme Oxygenase To Be Published.