Iron in PDB 8dyc: Human CYP3A4 Bound to A Substrate

All present enzymatic activity of Human CYP3A4 Bound to A Substrate:
1.14.14.1; 1.14.14.55; 1.14.14.56; 1.14.14.73;

The structure of Human CYP3A4 Bound to A Substrate, PDB code: 8dyc was solved by I.F.Sevrioukova, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	44.82 / 2.40
Space group	I 2 2 2
Cell size a, b, c (Å), α, β, γ (°)	78.069, 101.239, 130.16, 90, 90, 90
R / Rfree (%)	18.4 / 24.6

The binding sites of Iron atom in the Human CYP3A4 Bound to A Substrate (pdb code 8dyc). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total only one binding site of Iron was determined in the Human CYP3A4 Bound to A Substrate, PDB code: 8dyc:

Iron binding site 1 out of 1 in the Human CYP3A4 Bound to A Substrate


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Human CYP3A4 Bound to A Substrate within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe601 b:57.0 occ:1.00 FE A:HEM601 0.0 57.0 1.0 NB A:HEM601 1.9 54.8 1.0 NC A:HEM601 2.0 57.8 1.0 ND A:HEM601 2.0 51.6 1.0 NA A:HEM601 2.1 47.7 1.0 O A:HOH703 2.3 56.6 1.0 SG A:CYS442 2.5 60.3 1.0 C4B A:HEM601 2.9 57.9 1.0 C1B A:HEM601 3.0 59.3 1.0 C1C A:HEM601 3.0 58.8 1.0 C1D A:HEM601 3.0 58.4 1.0 C4C A:HEM601 3.0 64.2 1.0 C4D A:HEM601 3.1 62.2 1.0 C4A A:HEM601 3.1 48.2 1.0 C1A A:HEM601 3.2 54.1 1.0 CB A:CYS442 3.2 66.0 1.0 CHC A:HEM601 3.3 52.3 1.0 CHB A:HEM601 3.4 47.5 1.0 CHD A:HEM601 3.4 52.4 1.0 CHA A:HEM601 3.5 65.0 1.0 CA A:CYS442 4.0 65.8 1.0 C3B A:HEM601 4.2 60.7 1.0 C2B A:HEM601 4.2 62.8 1.0 C2C A:HEM601 4.2 61.1 1.0 C3C A:HEM601 4.2 62.0 1.0 C2D A:HEM601 4.3 63.8 1.0 C3D A:HEM601 4.3 59.0 1.0 C3A A:HEM601 4.3 51.4 1.0 C2A A:HEM601 4.4 56.4 1.0 O A:ALA305 4.6 65.0 1.0 O2 A:GOL603 4.7 90.2 1.0 C A:CYS442 4.7 67.0 1.0 CB A:ALA305 4.8 53.0 1.0 N A:GLY444 5.0 44.8 1.0

I.F.Sevrioukova, I.F.Sevrioukova. N/A N/A.
ISSN: ESSN 1422-0067
PubMed: 36293445
DOI: 10.3390/IJMS232012591