Iron in PDB 3ebs: Human Cytochrome P450 2A6 I208S/I300F/G301A/S369G in Complex with Phenacetin

All present enzymatic activity of Human Cytochrome P450 2A6 I208S/I300F/G301A/S369G in Complex with Phenacetin:
1.14.14.1;

The structure of Human Cytochrome P450 2A6 I208S/I300F/G301A/S369G in Complex with Phenacetin, PDB code: 3ebs was solved by N.M.Devore, E.E.Scott, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	87.04 / 2.15
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	70.850, 159.126, 103.993, 90.00, 92.08, 90.00
R / Rfree (%)	21.1 / 26.9

The binding sites of Iron atom in the Human Cytochrome P450 2A6 I208S/I300F/G301A/S369G in Complex with Phenacetin (pdb code 3ebs). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 4 binding sites of Iron where determined in the Human Cytochrome P450 2A6 I208S/I300F/G301A/S369G in Complex with Phenacetin, PDB code: 3ebs:
Jump to Iron binding site number: 1; 2; 3; 4;

Iron binding site 1 out of 4 in the Human Cytochrome P450 2A6 I208S/I300F/G301A/S369G in Complex with Phenacetin


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Human Cytochrome P450 2A6 I208S/I300F/G301A/S369G in Complex with Phenacetin within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe500 b:2.5 occ:1.00 FE A:HEM500 0.0 2.5 1.0 NC A:HEM500 2.0 19.6 1.0 NA A:HEM500 2.0 19.2 1.0 NB A:HEM500 2.0 20.5 1.0 ND A:HEM500 2.2 22.6 1.0 SG A:CYS439 2.5 26.6 1.0 C4A A:HEM500 3.0 18.9 1.0 C1C A:HEM500 3.0 18.8 1.0 C4C A:HEM500 3.0 18.3 1.0 C1B A:HEM500 3.0 20.4 1.0 C1A A:HEM500 3.1 17.2 1.0 C4B A:HEM500 3.1 18.0 1.0 C1D A:HEM500 3.1 18.7 1.0 C4D A:HEM500 3.2 21.9 1.0 CB A:CYS439 3.3 26.0 1.0 CHB A:HEM500 3.4 20.8 1.0 CHD A:HEM500 3.4 20.2 1.0 CHC A:HEM500 3.4 19.4 1.0 CHA A:HEM500 3.5 19.4 1.0 CA A:CYS439 4.1 27.4 1.0 C2C A:HEM500 4.2 19.6 1.0 C3A A:HEM500 4.2 21.7 1.0 C3C A:HEM500 4.2 18.7 1.0 C2A A:HEM500 4.3 19.5 1.0 C2B A:HEM500 4.3 19.6 1.0 C3B A:HEM500 4.3 20.6 1.0 C2D A:HEM500 4.4 23.4 1.0 C3D A:HEM500 4.4 21.6 1.0 C12 A:N4E1 4.5 72.0 1.0 O4 A:N4E1 4.8 72.0 1.0 CB A:ALA301 4.8 29.4 1.0 C A:CYS439 4.9 26.2 1.0 N A:GLY441 4.9 29.4 1.0

Iron binding site 2 out of 4 in the Human Cytochrome P450 2A6 I208S/I300F/G301A/S369G in Complex with Phenacetin


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Human Cytochrome P450 2A6 I208S/I300F/G301A/S369G in Complex with Phenacetin within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe500 b:15.3 occ:1.00 FE B:HEM500 0.0 15.3 1.0 NC B:HEM500 1.9 28.2 1.0 NB B:HEM500 2.0 26.6 1.0 NA B:HEM500 2.1 26.7 1.0 ND B:HEM500 2.1 26.7 1.0 SG B:CYS439 2.6 33.3 1.0 C4C B:HEM500 3.0 27.0 1.0 C1C B:HEM500 3.0 28.4 1.0 C4B B:HEM500 3.0 26.6 1.0 C1B B:HEM500 3.1 26.5 1.0 C1A B:HEM500 3.1 23.8 1.0 C4D B:HEM500 3.1 24.9 1.0 C1D B:HEM500 3.1 24.3 1.0 C4A B:HEM500 3.1 26.8 1.0 C13 B:N4E1 3.2 55.0 1.0 CB B:CYS439 3.3 32.9 1.0 CHC B:HEM500 3.4 27.3 1.0 CHD B:HEM500 3.4 27.6 1.0 CHA B:HEM500 3.4 25.6 1.0 CHB B:HEM500 3.5 27.2 1.0 C12 B:N4E1 4.0 56.0 1.0 C3C B:HEM500 4.2 29.2 1.0 C2C B:HEM500 4.2 28.1 1.0 CA B:CYS439 4.2 33.3 1.0 C3B B:HEM500 4.3 26.9 1.0 C2B B:HEM500 4.3 27.2 1.0 C2A B:HEM500 4.3 26.8 1.0 C3D B:HEM500 4.3 26.1 1.0 C3A B:HEM500 4.4 27.0 1.0 C2D B:HEM500 4.4 24.1 1.0 O4 B:N4E1 4.6 58.1 1.0 N B:GLY441 4.9 32.5 1.0 C B:CYS439 4.9 32.8 1.0 C5 B:N4E1 4.9 58.3 1.0 CB B:ALA301 4.9 38.8 1.0

Iron binding site 3 out of 4 in the Human Cytochrome P450 2A6 I208S/I300F/G301A/S369G in Complex with Phenacetin


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 3 of Human Cytochrome P450 2A6 I208S/I300F/G301A/S369G in Complex with Phenacetin within 5.0Å range: probe atom residue distance (Å) B Occ C:Fe500 b:10.6 occ:1.00 FE C:HEM500 0.0 10.6 1.0 ND C:HEM500 2.0 25.6 1.0 NC C:HEM500 2.0 25.6 1.0 NB C:HEM500 2.1 22.6 1.0 NA C:HEM500 2.1 24.9 1.0 SG C:CYS439 2.5 35.1 1.0 C1D C:HEM500 3.0 24.6 1.0 C4D C:HEM500 3.0 25.5 1.0 C4C C:HEM500 3.0 25.0 1.0 C1C C:HEM500 3.0 25.1 1.0 C4B C:HEM500 3.1 22.2 1.0 C1A C:HEM500 3.1 26.1 1.0 C1B C:HEM500 3.2 24.0 1.0 C4A C:HEM500 3.2 25.6 1.0 CHD C:HEM500 3.4 25.8 1.0 CB C:CYS439 3.4 32.2 1.0 CHA C:HEM500 3.4 24.6 1.0 CHC C:HEM500 3.4 25.6 1.0 CHB C:HEM500 3.5 23.9 1.0 CA C:CYS439 4.2 33.0 1.0 C3D C:HEM500 4.2 26.8 1.0 C2D C:HEM500 4.2 26.9 1.0 C2C C:HEM500 4.3 27.8 1.0 C3C C:HEM500 4.3 27.5 1.0 C3B C:HEM500 4.3 25.0 1.0 C2B C:HEM500 4.4 24.3 1.0 C2A C:HEM500 4.4 26.8 1.0 C3A C:HEM500 4.4 26.9 1.0 N C:GLY441 4.7 33.5 1.0 CB C:ALA301 4.9 31.9 1.0 CA C:GLY441 4.9 33.8 1.0 C C:CYS439 4.9 31.8 1.0

Iron binding site 4 out of 4 in the Human Cytochrome P450 2A6 I208S/I300F/G301A/S369G in Complex with Phenacetin


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 4 of Human Cytochrome P450 2A6 I208S/I300F/G301A/S369G in Complex with Phenacetin within 5.0Å range: probe atom residue distance (Å) B Occ D:Fe500 b:15.9 occ:1.00 FE D:HEM500 0.0 15.9 1.0 NA D:HEM500 1.9 26.7 1.0 NB D:HEM500 2.1 27.4 1.0 NC D:HEM500 2.1 27.6 1.0 ND D:HEM500 2.1 27.6 1.0 SG D:CYS439 2.6 34.0 1.0 C4A D:HEM500 3.0 25.0 1.0 C1A D:HEM500 3.0 26.6 1.0 C1B D:HEM500 3.1 26.1 1.0 C1C D:HEM500 3.1 27.4 1.0 C4D D:HEM500 3.1 25.8 1.0 C4C D:HEM500 3.1 25.2 1.0 C1D D:HEM500 3.1 27.1 1.0 C4B D:HEM500 3.1 26.6 1.0 C13 D:N4E1 3.1 69.3 1.0 CB D:CYS439 3.3 33.5 1.0 CHB D:HEM500 3.4 25.9 1.0 CHA D:HEM500 3.4 25.8 1.0 CHD D:HEM500 3.5 26.9 1.0 CHC D:HEM500 3.5 28.0 1.0 C3A D:HEM500 4.2 27.3 1.0 C2A D:HEM500 4.2 26.8 1.0 C12 D:N4E1 4.3 69.5 1.0 CA D:CYS439 4.3 33.0 1.0 C2B D:HEM500 4.3 26.8 1.0 C2C D:HEM500 4.3 27.7 1.0 C3C D:HEM500 4.3 28.4 1.0 C3B D:HEM500 4.4 27.7 1.0 C3D D:HEM500 4.4 28.2 1.0 C2D D:HEM500 4.4 28.1 1.0 N D:GLY441 4.8 33.2 1.0 O4 D:N4E1 4.9 69.9 1.0 CA D:GLY441 4.9 33.3 1.0

N.M.Devore, B.D.Smith, M.J.Urban, E.E.Scott. Key Residues Controlling Phenacetin Metabolism By Human Cytochrome P4502A Enzymes. Drug Metab.Dispos. V. 36 2582 2008.
PubMed: 18779312
DOI: 10.1124/DMD.108.023770