Iron in PDB 8ss0: Human Sterol 14 Alpha-Demethylase (CYP51) in Complex with the Reaction Intermediate 14 Alpha-Aldehyde Dihydrolanosterol

All present enzymatic activity of Human Sterol 14 Alpha-Demethylase (CYP51) in Complex with the Reaction Intermediate 14 Alpha-Aldehyde Dihydrolanosterol:
1.14.14.154;

The structure of Human Sterol 14 Alpha-Demethylase (CYP51) in Complex with the Reaction Intermediate 14 Alpha-Aldehyde Dihydrolanosterol, PDB code: 8ss0 was solved by T.Y.Hargrove, Z.Wawrzak, F.P.Guengerich, G.I.Lepesheva, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	19.89 / 2.25
Space group	P 62 2 2
Cell size a, b, c (Å), α, β, γ (°)	145.803, 145.803, 261.161, 90, 90, 120
R / Rfree (%)	21.9 / 24.9

The binding sites of Iron atom in the Human Sterol 14 Alpha-Demethylase (CYP51) in Complex with the Reaction Intermediate 14 Alpha-Aldehyde Dihydrolanosterol (pdb code 8ss0). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 2 binding sites of Iron where determined in the Human Sterol 14 Alpha-Demethylase (CYP51) in Complex with the Reaction Intermediate 14 Alpha-Aldehyde Dihydrolanosterol, PDB code: 8ss0:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in the Human Sterol 14 Alpha-Demethylase (CYP51) in Complex with the Reaction Intermediate 14 Alpha-Aldehyde Dihydrolanosterol


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Human Sterol 14 Alpha-Demethylase (CYP51) in Complex with the Reaction Intermediate 14 Alpha-Aldehyde Dihydrolanosterol within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe601 b:25.1 occ:1.00 FE A:HEM601 0.0 25.1 1.0 ND A:HEM601 1.9 25.7 1.0 NA A:HEM601 2.0 22.9 1.0 NB A:HEM601 2.1 20.1 1.0 NC A:HEM601 2.1 25.1 1.0 SG A:CYS449 2.4 29.9 1.0 C1D A:HEM601 2.9 26.9 1.0 C4D A:HEM601 2.9 26.2 1.0 C1A A:HEM601 3.0 21.6 1.0 C4C A:HEM601 3.0 26.6 1.0 C1B A:HEM601 3.0 19.1 1.0 C4A A:HEM601 3.0 21.1 1.0 C4B A:HEM601 3.1 21.1 1.0 C1C A:HEM601 3.1 25.3 1.0 CHD A:HEM601 3.3 26.6 1.0 CHA A:HEM601 3.4 23.5 1.0 O32 A:WQR602 3.4 23.2 1.0 CHB A:HEM601 3.4 21.1 1.0 CHC A:HEM601 3.5 22.3 1.0 CB A:CYS449 3.6 32.5 1.0 C8 A:WQR602 3.7 28.8 1.0 C2D A:HEM601 4.1 29.9 1.0 C3D A:HEM601 4.1 28.5 1.0 C2A A:HEM601 4.2 21.1 1.0 CA A:CYS449 4.2 32.8 1.0 C3A A:HEM601 4.2 19.7 1.0 C3C A:HEM601 4.2 27.0 1.0 C2B A:HEM601 4.2 19.1 1.0 C3B A:HEM601 4.3 20.0 1.0 C2C A:HEM601 4.3 26.4 1.0 O A:HOH707 4.5 31.7 1.0 C12 A:WQR602 4.8 29.4 1.0 C21 A:WQR602 4.8 30.0 1.0 C7 A:WQR602 5.0 29.4 1.0

Iron binding site 2 out of 2 in the Human Sterol 14 Alpha-Demethylase (CYP51) in Complex with the Reaction Intermediate 14 Alpha-Aldehyde Dihydrolanosterol


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Human Sterol 14 Alpha-Demethylase (CYP51) in Complex with the Reaction Intermediate 14 Alpha-Aldehyde Dihydrolanosterol within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe601 b:24.7 occ:1.00 FE B:HEM601 0.0 24.7 1.0 ND B:HEM601 1.9 25.4 1.0 NA B:HEM601 2.0 23.0 1.0 NC B:HEM601 2.1 24.6 1.0 NB B:HEM601 2.1 21.4 1.0 SG B:CYS449 2.4 25.0 1.0 C1D B:HEM601 2.9 26.0 1.0 C4D B:HEM601 2.9 27.3 1.0 C4C B:HEM601 3.0 25.6 1.0 C1A B:HEM601 3.0 21.8 1.0 C1B B:HEM601 3.0 20.3 1.0 C4A B:HEM601 3.1 21.4 1.0 C4B B:HEM601 3.1 22.0 1.0 C1C B:HEM601 3.1 23.4 1.0 CHD B:HEM601 3.3 26.1 1.0 CHA B:HEM601 3.4 24.2 1.0 CHB B:HEM601 3.4 20.8 1.0 O32 B:WQR602 3.5 22.4 1.0 CHC B:HEM601 3.5 22.3 1.0 CB B:CYS449 3.6 29.6 1.0 C8 B:WQR602 3.8 23.6 1.0 O B:HOH705 3.8 34.0 1.0 C2D B:HEM601 4.1 29.0 1.0 C3D B:HEM601 4.1 30.1 1.0 CA B:CYS449 4.2 32.7 1.0 C2A B:HEM601 4.2 20.5 1.0 C3A B:HEM601 4.2 20.4 1.0 C3C B:HEM601 4.2 24.3 1.0 C2B B:HEM601 4.3 20.1 1.0 C2C B:HEM601 4.3 24.4 1.0 C3B B:HEM601 4.3 20.6 1.0 C12 B:WQR602 4.9 25.1 1.0

K.D.Mccarty, Y.Tateishi, T.Y.Hargrove, G.I.Lepesheva, F.P.Guengerich. Oxygen-18 Labeling Reveals A Mixed Fe-O Mechanism in the Last Step of Cytochrome P450 51 Sterol 14 Alpha-Demethylation. Angew.Chem.Int.Ed.Engl. 17711 2024.
ISSN: ESSN 1521-3773
PubMed: 38206808
DOI: 10.1002/ANIE.202317711