Iron in PDB 5vc0: Crystal Structure of Human CYP3A4 Bound to Ritonavir

All present enzymatic activity of Crystal Structure of Human CYP3A4 Bound to Ritonavir:
1.14.13.157; 1.14.13.32; 1.14.13.67; 1.14.13.9;

The structure of Crystal Structure of Human CYP3A4 Bound to Ritonavir, PDB code: 5vc0 was solved by I.Sevrioukova, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	78.17 / 2.70
Space group	I 2 2 2
Cell size a, b, c (Å), α, β, γ (°)	76.579, 100.069, 125.220, 90.00, 90.00, 90.00
R / Rfree (%)	20.8 / 28.3

The binding sites of Iron atom in the Crystal Structure of Human CYP3A4 Bound to Ritonavir (pdb code 5vc0). 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 Crystal Structure of Human CYP3A4 Bound to Ritonavir, PDB code: 5vc0:

Iron binding site 1 out of 1 in the Crystal Structure of Human CYP3A4 Bound to Ritonavir


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Crystal Structure of Human CYP3A4 Bound to Ritonavir within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe601 b:75.7 occ:1.00 FE A:HEM601 0.0 75.7 1.0 ND A:HEM601 1.9 85.2 1.0 NA A:HEM601 2.0 75.0 1.0 SG A:CYS442 2.1 75.5 1.0 NC A:HEM601 2.1 81.5 1.0 NB A:HEM601 2.1 77.4 1.0 N5 A:RIT602 2.2 66.3 1.0 C1D A:HEM601 2.9 83.6 1.0 C4D A:HEM601 2.9 80.6 1.0 C4 A:RIT602 2.9 67.5 1.0 C1A A:HEM601 3.0 78.1 1.0 C4A A:HEM601 3.0 76.4 1.0 C4C A:HEM601 3.0 82.9 1.0 C1B A:HEM601 3.0 73.4 1.0 C4B A:HEM601 3.1 77.7 1.0 C1C A:HEM601 3.1 84.9 1.0 C1 A:RIT602 3.1 71.4 1.0 CB A:CYS442 3.4 78.8 1.0 CHA A:HEM601 3.4 79.2 1.0 CHD A:HEM601 3.4 82.1 1.0 CHB A:HEM601 3.4 75.5 1.0 CHC A:HEM601 3.5 79.7 1.0 CA A:CYS442 4.1 82.2 1.0 C2A A:HEM601 4.2 77.3 1.0 C2D A:HEM601 4.2 89.6 1.0 C3D A:HEM601 4.2 86.3 1.0 C3A A:HEM601 4.2 75.3 1.0 C3C A:HEM601 4.3 86.3 1.0 C2B A:HEM601 4.3 77.9 1.0 C2C A:HEM601 4.3 86.6 1.0 C3B A:HEM601 4.3 80.9 1.0 C2 A:RIT602 4.3 71.9 1.0 S3 A:RIT602 4.5 68.0 1.0 N A:GLY444 4.8 92.8 1.0 C A:CYS442 4.8 88.8 1.0 N A:ILE443 4.9 87.9 1.0

I.F.Sevrioukova, I.Sevrioukova. N/A N/A.
ISSN: ISSN 1520-4995
PubMed: 28590129
DOI: 10.1021/ACS.BIOCHEM.7B00334