Iron in PDB 5a1r: Crystal Structure of Cytochrome P450 3A4 Bound to Progesterone

All present enzymatic activity of Crystal Structure of Cytochrome P450 3A4 Bound to Progesterone:
1.14.13.157; 1.14.13.32; 1.14.13.67; 1.14.13.9;

The structure of Crystal Structure of Cytochrome P450 3A4 Bound to Progesterone, PDB code: 5a1r 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)	66.642 / 2.45
Space group	I 2 2 2
Cell size a, b, c (Å), α, β, γ (°)	77.750, 102.140, 129.380, 90.00, 90.00, 90.00
R / Rfree (%)	19.17 / 26.17

The binding sites of Iron atom in the Crystal Structure of Cytochrome P450 3A4 Bound to Progesterone (pdb code 5a1r). 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 Cytochrome P450 3A4 Bound to Progesterone, PDB code: 5a1r:

Iron binding site 1 out of 1 in the Crystal Structure of Cytochrome P450 3A4 Bound to Progesterone


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 Cytochrome P450 3A4 Bound to Progesterone within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe1500 b:42.5 occ:1.00 FE A:HEM1500 0.0 42.5 1.0 NB A:HEM1500 2.0 42.8 1.0 NC A:HEM1500 2.0 39.7 1.0 NA A:HEM1500 2.1 50.5 1.0 ND A:HEM1500 2.1 34.6 1.0 O A:HOH2005 2.4 62.9 1.0 SG A:CYS442 2.4 47.8 1.0 C4B A:HEM1500 3.0 49.9 1.0 C1C A:HEM1500 3.0 41.0 1.0 C1B A:HEM1500 3.0 42.8 1.0 C4C A:HEM1500 3.1 44.4 1.0 C4A A:HEM1500 3.1 40.5 1.0 C1A A:HEM1500 3.1 44.4 1.0 C1D A:HEM1500 3.1 50.8 1.0 C4D A:HEM1500 3.1 43.1 1.0 CHC A:HEM1500 3.3 46.5 1.0 CHB A:HEM1500 3.4 38.6 1.0 CB A:CYS442 3.4 58.2 1.0 CHD A:HEM1500 3.5 35.8 1.0 CHA A:HEM1500 3.5 44.0 1.0 CA A:CYS442 4.1 53.4 1.0 C3B A:HEM1500 4.2 51.5 1.0 C2B A:HEM1500 4.2 55.7 1.0 C2C A:HEM1500 4.2 46.3 1.0 C3C A:HEM1500 4.3 47.3 1.0 C3A A:HEM1500 4.3 43.6 1.0 C2A A:HEM1500 4.3 45.8 1.0 C2D A:HEM1500 4.4 51.9 1.0 C3D A:HEM1500 4.4 45.4 1.0 O A:ALA305 4.7 54.5 1.0 CB A:ALA305 4.8 43.9 1.0 C A:CYS442 4.8 52.0 1.0 N A:GLY444 5.0 40.2 1.0

I.F.Sevrioukova, T.L.Poulos. Anion-Dependent Stimulation of CYP3A4 Monooxygenase Biochemistry V. 54 4083 2015.
ISSN: ISSN 0006-2960
PubMed: 26066995
DOI: 10.1021/ACS.BIOCHEM.5B00510