Iron in PDB 7ufa: CYP3A4 Bound to An Inhibitor

All present enzymatic activity of CYP3A4 Bound to An Inhibitor:
1.14.14.1; 1.14.14.55; 1.14.14.56; 1.14.14.73;

The structure of CYP3A4 Bound to An Inhibitor, PDB code: 7ufa was solved by I.Sevrioukova, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	40.14 / 2.50
Space group	I 2 2 2
Cell size a, b, c (Å), α, β, γ (°)	76.58, 101.73, 125.51, 90, 90, 90
R / Rfree (%)	24.7 / 28.4

The binding sites of Iron atom in the CYP3A4 Bound to An Inhibitor (pdb code 7ufa). 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 CYP3A4 Bound to An Inhibitor, PDB code: 7ufa:

Iron binding site 1 out of 1 in the CYP3A4 Bound to An Inhibitor


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of CYP3A4 Bound to An Inhibitor within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe601 b:61.0 occ:1.00 FE A:HEM601 0.0 61.0 1.0 ND A:HEM601 2.0 78.1 1.0 NA A:HEM601 2.0 71.3 1.0 NB A:HEM601 2.1 66.2 1.0 NC A:HEM601 2.1 59.8 1.0 N29 A:NI6602 2.1 50.8 1.0 SG A:CYS442 2.3 73.4 1.0 C28 A:NI6602 3.0 69.1 1.0 C1C A:HEM601 3.1 56.6 1.0 C30 A:NI6602 3.1 69.3 1.0 C1A A:HEM601 3.1 62.4 1.0 C4D A:HEM601 3.1 50.8 1.0 C1D A:HEM601 3.1 64.2 1.0 C4B A:HEM601 3.1 52.0 1.0 C4A A:HEM601 3.1 61.0 1.0 C4C A:HEM601 3.1 59.3 1.0 C1B A:HEM601 3.1 62.3 1.0 CB A:CYS442 3.3 74.7 1.0 CHC A:HEM601 3.4 50.3 1.0 CHA A:HEM601 3.4 59.6 1.0 CHD A:HEM601 3.4 53.1 1.0 CHB A:HEM601 3.4 67.6 1.0 CA A:CYS442 4.0 80.2 1.0 C2C A:HEM601 4.3 71.9 1.0 C3C A:HEM601 4.3 70.0 1.0 C2A A:HEM601 4.3 62.0 1.0 C3A A:HEM601 4.3 70.4 1.0 C3D A:HEM601 4.3 71.0 1.0 C2D A:HEM601 4.3 79.5 1.0 C3B A:HEM601 4.3 68.7 1.0 C2B A:HEM601 4.3 72.8 1.0 C27 A:NI6602 4.3 64.2 1.0 C31 A:NI6602 4.4 57.0 1.0 C A:CYS442 4.8 79.8 1.0 N A:GLY444 4.9 59.7 1.0 C26 A:NI6602 4.9 71.3 1.0 N A:ILE443 4.9 70.6 1.0

E.R.Samuels, I.F.Sevrioukova. Interaction of CYP3A4 with Rationally Designed Ritonavir Analogues: Impact of Steric Constraints Imposed on the Heme-Ligating Group and the End-Pyridine Attachment. Int J Mol Sci V. 23 2022.
ISSN: ESSN 1422-0067
PubMed: 35806297
DOI: 10.3390/IJMS23137291