Iron in PDB 4k9w: Complex of Human CYP3A4 with A Desoxyritonavir Analog

All present enzymatic activity of Complex of Human CYP3A4 with A Desoxyritonavir Analog:
1.14.13.157; 1.14.13.32; 1.14.13.67; 1.14.13.97;

The structure of Complex of Human CYP3A4 with A Desoxyritonavir Analog, PDB code: 4k9w was solved by I.F.Sevrioukova, T.L.Poulos, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	47.01 / 2.40
Space group	P 31
Cell size a, b, c (Å), α, β, γ (°)	94.020, 94.020, 199.412, 90.00, 90.00, 120.00
R / Rfree (%)	16.4 / 19.8

The binding sites of Iron atom in the Complex of Human CYP3A4 with A Desoxyritonavir Analog (pdb code 4k9w). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 4 binding sites of Iron where determined in the Complex of Human CYP3A4 with A Desoxyritonavir Analog, PDB code: 4k9w:
Jump to Iron binding site number: 1; 2; 3; 4;

Iron binding site 1 out of 4 in the Complex of Human CYP3A4 with A Desoxyritonavir Analog


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Complex of Human CYP3A4 with A Desoxyritonavir Analog within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe601 b:37.2 occ:1.00 FE A:HEM601 0.0 37.2 1.0 NA A:HEM601 2.0 34.9 1.0 NC A:HEM601 2.0 35.7 1.0 SG A:CYS442 2.1 31.4 1.0 ND A:HEM601 2.1 34.7 1.0 NB A:HEM601 2.1 35.3 1.0 N43 A:7AW602 2.2 51.9 1.0 C4C A:HEM601 3.0 35.3 1.0 C42 A:7AW602 3.0 54.1 1.0 C1A A:HEM601 3.0 34.5 1.0 C4A A:HEM601 3.1 34.3 1.0 C1C A:HEM601 3.1 35.3 1.0 C1D A:HEM601 3.1 36.1 1.0 C4B A:HEM601 3.1 36.3 1.0 C4D A:HEM601 3.1 35.4 1.0 C1B A:HEM601 3.2 36.5 1.0 CB A:CYS442 3.2 34.2 1.0 C44 A:7AW602 3.3 57.8 1.0 CHD A:HEM601 3.4 35.3 1.0 CHB A:HEM601 3.5 34.7 1.0 CHA A:HEM601 3.5 35.2 1.0 CHC A:HEM601 3.5 36.1 1.0 CA A:CYS442 3.9 35.6 1.0 C3C A:HEM601 4.3 35.4 1.0 C2A A:HEM601 4.3 35.0 1.0 C41 A:7AW602 4.3 52.9 1.0 C3A A:HEM601 4.3 35.2 1.0 C2C A:HEM601 4.3 34.8 1.0 C2D A:HEM601 4.4 36.1 1.0 C3D A:HEM601 4.5 35.8 1.0 C3B A:HEM601 4.5 36.7 1.0 C2B A:HEM601 4.5 37.7 1.0 S45 A:7AW602 4.7 59.0 1.0 C A:CYS442 4.7 38.0 1.0 N A:GLY444 4.9 38.3 1.0 N A:ILE443 4.9 40.0 1.0

Iron binding site 2 out of 4 in the Complex of Human CYP3A4 with A Desoxyritonavir Analog


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Complex of Human CYP3A4 with A Desoxyritonavir Analog within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe601 b:45.4 occ:1.00 FE B:HEM601 0.0 45.4 1.0 NC B:HEM601 1.9 45.9 1.0 NA B:HEM601 2.0 43.2 1.0 SG B:CYS442 2.1 39.0 1.0 NB B:HEM601 2.1 42.2 1.0 ND B:HEM601 2.1 46.5 1.0 N43 B:7AW602 2.3 55.1 1.0 C4C B:HEM601 2.9 45.3 1.0 C1C B:HEM601 3.0 43.2 1.0 C4A B:HEM601 3.1 43.6 1.0 C1A B:HEM601 3.1 44.0 1.0 C1D B:HEM601 3.1 47.6 1.0 C4B B:HEM601 3.2 42.6 1.0 C1B B:HEM601 3.2 43.1 1.0 CB B:CYS442 3.2 40.8 1.0 C42 B:7AW602 3.2 57.6 1.0 C4D B:HEM601 3.2 45.9 1.0 C44 B:7AW602 3.2 58.7 1.0 CHD B:HEM601 3.4 48.3 1.0 CHC B:HEM601 3.5 41.9 1.0 CHB B:HEM601 3.5 45.6 1.0 CHA B:HEM601 3.6 46.7 1.0 CA B:CYS442 3.9 43.1 1.0 C3C B:HEM601 4.1 47.2 1.0 C2C B:HEM601 4.2 43.9 1.0 C2A B:HEM601 4.4 44.4 1.0 C3A B:HEM601 4.4 43.8 1.0 C41 B:7AW602 4.4 58.2 1.0 C2D B:HEM601 4.5 48.2 1.0 C3B B:HEM601 4.5 40.8 1.0 C3D B:HEM601 4.5 45.3 1.0 C2B B:HEM601 4.5 43.0 1.0 C B:CYS442 4.6 44.1 1.0 N B:ILE443 4.7 42.9 1.0 S45 B:7AW602 4.7 59.0 1.0 N B:GLY444 4.7 43.2 1.0

Iron binding site 3 out of 4 in the Complex of Human CYP3A4 with A Desoxyritonavir Analog


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 3 of Complex of Human CYP3A4 with A Desoxyritonavir Analog within 5.0Å range: probe atom residue distance (Å) B Occ C:Fe601 b:39.2 occ:1.00 FE C:HEM601 0.0 39.2 1.0 NC C:HEM601 2.0 39.6 1.0 NA C:HEM601 2.0 39.1 1.0 SG C:CYS442 2.0 35.4 1.0 N43 C:7AW602 2.1 42.5 1.0 ND C:HEM601 2.1 40.4 1.0 NB C:HEM601 2.1 40.2 1.0 C44 C:7AW602 2.9 47.3 1.0 C4C C:HEM601 3.0 40.6 1.0 C1C C:HEM601 3.0 39.0 1.0 C4A C:HEM601 3.1 40.5 1.0 C1A C:HEM601 3.1 41.4 1.0 CB C:CYS442 3.1 36.2 1.0 C42 C:7AW602 3.1 51.0 1.0 C1D C:HEM601 3.1 41.1 1.0 C4B C:HEM601 3.1 39.4 1.0 C4D C:HEM601 3.2 40.7 1.0 C1B C:HEM601 3.2 40.2 1.0 CHD C:HEM601 3.5 40.9 1.0 CHC C:HEM601 3.5 38.1 1.0 CHA C:HEM601 3.5 41.8 1.0 CHB C:HEM601 3.6 41.4 1.0 CA C:CYS442 3.8 37.2 1.0 C3C C:HEM601 4.3 39.7 1.0 C2C C:HEM601 4.3 39.2 1.0 C3A C:HEM601 4.3 39.2 1.0 C2A C:HEM601 4.3 40.6 1.0 C41 C:7AW602 4.3 49.4 1.0 C3B C:HEM601 4.5 42.3 1.0 C2D C:HEM601 4.5 41.0 1.0 C3D C:HEM601 4.5 41.5 1.0 C C:CYS442 4.5 37.6 1.0 S45 C:7AW602 4.5 49.0 1.0 C2B C:HEM601 4.6 43.6 1.0 N C:ILE443 4.6 38.0 1.0 N C:GLY444 4.8 39.0 1.0

Iron binding site 4 out of 4 in the Complex of Human CYP3A4 with A Desoxyritonavir Analog


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 4 of Complex of Human CYP3A4 with A Desoxyritonavir Analog within 5.0Å range: probe atom residue distance (Å) B Occ D:Fe601 b:47.2 occ:1.00 FE D:HEM601 0.0 47.2 1.0 NC D:HEM601 2.0 45.4 1.0 NA D:HEM601 2.0 46.3 1.0 ND D:HEM601 2.1 44.5 1.0 SG D:CYS442 2.1 48.8 1.0 NB D:HEM601 2.1 45.2 1.0 N43 D:7AW602 2.3 53.3 1.0 C4C D:HEM601 2.9 44.8 1.0 C1C D:HEM601 3.1 43.8 1.0 C4A D:HEM601 3.1 44.4 1.0 C1A D:HEM601 3.1 45.8 1.0 C1D D:HEM601 3.1 44.9 1.0 C4D D:HEM601 3.1 45.3 1.0 C1B D:HEM601 3.2 46.5 1.0 C4B D:HEM601 3.2 46.9 1.0 C42 D:7AW602 3.2 55.5 1.0 CB D:CYS442 3.2 49.7 1.0 C44 D:7AW602 3.3 54.6 1.0 CHD D:HEM601 3.4 44.3 1.0 CHB D:HEM601 3.5 47.4 1.0 CHA D:HEM601 3.6 45.1 1.0 CHC D:HEM601 3.6 44.4 1.0 CA D:CYS442 3.8 51.9 1.0 C3C D:HEM601 4.2 44.5 1.0 C2C D:HEM601 4.3 43.7 1.0 C3A D:HEM601 4.3 46.5 1.0 C2A D:HEM601 4.3 46.3 1.0 C2D D:HEM601 4.4 43.7 1.0 C3D D:HEM601 4.4 43.9 1.0 C41 D:7AW602 4.5 54.4 1.0 C3B D:HEM601 4.5 45.7 1.0 C2B D:HEM601 4.5 46.8 1.0 C D:CYS442 4.6 54.1 1.0 N D:GLY444 4.7 52.3 1.0 N D:ILE443 4.7 55.2 1.0 S45 D:7AW602 4.8 53.9 1.0 N D:CYS442 5.0 51.1 1.0

I.F.Sevrioukova, T.L.Poulos. Dissecting Cytochrome P450 3A4-Ligand Interactions Using Ritonavir Analogues. Biochemistry V. 52 4474 2013.
ISSN: ISSN 0006-2960
PubMed: 23746300
DOI: 10.1021/BI4005396