Iron in PDB 5tfu: Structure of Cytochrome P450 2D6 (CYP2D6) BACE1 Inhibitor Complex

All present enzymatic activity of Structure of Cytochrome P450 2D6 (CYP2D6) BACE1 Inhibitor Complex:
1.14.14.1;

The structure of Structure of Cytochrome P450 2D6 (CYP2D6) BACE1 Inhibitor Complex, PDB code: 5tfu was solved by M.H.Hsu, E.F.Johnson, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	39.07 / 2.75
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	57.105, 191.756, 246.838, 90.00, 90.00, 90.00
R / Rfree (%)	21.2 / 25

The structure of Structure of Cytochrome P450 2D6 (CYP2D6) BACE1 Inhibitor Complex also contains other interesting chemical elements:

Fluorine	(F)	20 atoms
Zinc	(Zn)	5 atoms

The binding sites of Iron atom in the Structure of Cytochrome P450 2D6 (CYP2D6) BACE1 Inhibitor Complex (pdb code 5tfu). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 4 binding sites of Iron where determined in the Structure of Cytochrome P450 2D6 (CYP2D6) BACE1 Inhibitor Complex, PDB code: 5tfu:
Jump to Iron binding site number: 1; 2; 3; 4;

Iron binding site 1 out of 4 in the Structure of Cytochrome P450 2D6 (CYP2D6) BACE1 Inhibitor Complex


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Structure of Cytochrome P450 2D6 (CYP2D6) BACE1 Inhibitor Complex within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe601 b:27.4 occ:1.00 FE A:HEM601 0.0 27.4 1.0 NB A:HEM601 2.0 30.4 1.0 NA A:HEM601 2.0 27.0 1.0 NC A:HEM601 2.1 30.8 1.0 ND A:HEM601 2.1 29.0 1.0 SG A:CYS443 2.3 21.3 1.0 C4B A:HEM601 3.1 32.8 1.0 C1B A:HEM601 3.1 31.3 1.0 C1C A:HEM601 3.1 30.3 1.0 C4A A:HEM601 3.1 26.1 1.0 C1A A:HEM601 3.1 27.6 1.0 C4C A:HEM601 3.1 29.1 1.0 C4D A:HEM601 3.1 27.8 1.0 C1D A:HEM601 3.1 28.3 1.0 CB A:CYS443 3.4 25.2 1.0 CHC A:HEM601 3.4 31.9 1.0 CHB A:HEM601 3.4 27.5 1.0 CHA A:HEM601 3.4 30.9 1.0 CHD A:HEM601 3.5 28.2 1.0 CA A:CYS443 4.2 23.0 1.0 C2C A:HEM601 4.3 31.3 1.0 C3C A:HEM601 4.3 35.4 1.0 C2B A:HEM601 4.3 26.2 1.0 C2A A:HEM601 4.3 29.2 1.0 C3A A:HEM601 4.3 25.1 1.0 C3B A:HEM601 4.3 28.4 1.0 C3D A:HEM601 4.3 30.5 1.0 C2D A:HEM601 4.3 29.5 1.0 CB A:ALA305 4.9 37.8 1.0 C A:CYS443 5.0 26.6 1.0 N A:GLY445 5.0 25.2 1.0

Iron binding site 2 out of 4 in the Structure of Cytochrome P450 2D6 (CYP2D6) BACE1 Inhibitor Complex


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Structure of Cytochrome P450 2D6 (CYP2D6) BACE1 Inhibitor Complex within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe601 b:26.1 occ:1.00 FE B:HEM601 0.0 26.1 1.0 NB B:HEM601 2.0 30.7 1.0 NA B:HEM601 2.0 25.2 1.0 NC B:HEM601 2.1 40.0 1.0 ND B:HEM601 2.1 32.0 1.0 SG B:CYS443 2.3 28.6 1.0 C4B B:HEM601 3.0 30.8 1.0 C1C B:HEM601 3.0 36.9 1.0 C1B B:HEM601 3.1 32.6 1.0 C4C B:HEM601 3.1 38.8 1.0 C1A B:HEM601 3.1 25.3 1.0 C4A B:HEM601 3.1 34.3 1.0 C4D B:HEM601 3.1 33.0 1.0 C1D B:HEM601 3.1 26.1 1.0 CB B:CYS443 3.3 25.3 1.0 CHC B:HEM601 3.4 28.3 1.0 CHB B:HEM601 3.4 30.5 1.0 CHA B:HEM601 3.4 32.8 1.0 CHD B:HEM601 3.4 38.8 1.0 CA B:CYS443 4.1 28.9 1.0 C2C B:HEM601 4.3 31.2 1.0 C3C B:HEM601 4.3 35.5 1.0 C2B B:HEM601 4.3 31.5 1.0 C3B B:HEM601 4.3 34.7 1.0 C2A B:HEM601 4.3 32.8 1.0 C3A B:HEM601 4.3 29.0 1.0 C3D B:HEM601 4.3 36.8 1.0 C2D B:HEM601 4.3 37.9 1.0 C B:CYS443 4.9 29.1 1.0

Iron binding site 3 out of 4 in the Structure of Cytochrome P450 2D6 (CYP2D6) BACE1 Inhibitor Complex


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 3 of Structure of Cytochrome P450 2D6 (CYP2D6) BACE1 Inhibitor Complex within 5.0Å range: probe atom residue distance (Å) B Occ C:Fe601 b:28.2 occ:1.00 FE C:HEM601 0.0 28.2 1.0 NA C:HEM601 2.0 26.7 1.0 NB C:HEM601 2.0 37.4 1.0 ND C:HEM601 2.1 37.9 1.0 NC C:HEM601 2.1 34.4 1.0 SG C:CYS443 2.3 26.9 1.0 C1A C:HEM601 3.0 29.0 1.0 C1C C:HEM601 3.1 38.5 1.0 C4A C:HEM601 3.1 33.6 1.0 C4B C:HEM601 3.1 33.0 1.0 C4C C:HEM601 3.1 35.9 1.0 C1B C:HEM601 3.1 32.8 1.0 C4D C:HEM601 3.1 31.6 1.0 C1D C:HEM601 3.1 32.7 1.0 CB C:CYS443 3.2 31.2 1.0 CHA C:HEM601 3.4 32.4 1.0 CHC C:HEM601 3.4 36.2 1.0 CHB C:HEM601 3.4 34.1 1.0 CHD C:HEM601 3.5 38.3 1.0 CA C:CYS443 4.0 32.6 1.0 C2A C:HEM601 4.3 34.6 1.0 C2C C:HEM601 4.3 37.8 1.0 C3A C:HEM601 4.3 27.3 1.0 C3C C:HEM601 4.3 39.7 1.0 C3B C:HEM601 4.3 33.6 1.0 C2B C:HEM601 4.3 33.1 1.0 C3D C:HEM601 4.3 34.0 1.0 C2D C:HEM601 4.3 38.1 1.0 CB C:ALA305 4.9 40.4 1.0 C C:CYS443 4.9 34.5 1.0

Iron binding site 4 out of 4 in the Structure of Cytochrome P450 2D6 (CYP2D6) BACE1 Inhibitor Complex


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 4 of Structure of Cytochrome P450 2D6 (CYP2D6) BACE1 Inhibitor Complex within 5.0Å range: probe atom residue distance (Å) B Occ D:Fe601 b:30.6 occ:1.00 FE D:HEM601 0.0 30.6 1.0 NA D:HEM601 2.0 34.6 1.0 NB D:HEM601 2.0 39.1 1.0 ND D:HEM601 2.1 42.7 1.0 NC D:HEM601 2.1 36.1 1.0 SG D:CYS443 2.3 27.5 1.0 C1C D:HEM601 3.1 39.5 1.0 C1A D:HEM601 3.1 31.0 1.0 C4B D:HEM601 3.1 37.5 1.0 C4C D:HEM601 3.1 38.1 1.0 C1B D:HEM601 3.1 37.9 1.0 C4A D:HEM601 3.1 33.2 1.0 C4D D:HEM601 3.1 35.6 1.0 C1D D:HEM601 3.1 31.9 1.0 CB D:CYS443 3.3 31.5 1.0 CHC D:HEM601 3.4 41.1 1.0 CHA D:HEM601 3.4 32.8 1.0 CHB D:HEM601 3.4 33.0 1.0 CHD D:HEM601 3.4 35.4 1.0 CA D:CYS443 4.1 34.5 1.0 C2C D:HEM601 4.3 44.7 1.0 C3C D:HEM601 4.3 49.5 1.0 C2A D:HEM601 4.3 33.3 1.0 C3A D:HEM601 4.3 32.9 1.0 C2B D:HEM601 4.3 35.8 1.0 C3B D:HEM601 4.3 36.5 1.0 C3D D:HEM601 4.3 37.9 1.0 C2D D:HEM601 4.3 39.4 1.0 CB D:ALA305 4.9 36.5 1.0 O D:ALA305 4.9 54.0 1.0 C D:CYS443 5.0 36.1 1.0 CG2 D:THR309 5.0 38.9 1.0

C.R.Butler, K.Ogilvie, L.Martinez-Alsina, G.Barreiro, E.M.Beck, C.E.Nolan, K.Atchison, E.Benvenuti, L.Buzon, S.Doran, C.Gonzales, C.J.Helal, X.Hou, M.H.Hsu, E.F.Johnson, K.Lapham, L.Lanyon, K.Parris, B.T.O'neill, D.Riddell, A.Robshaw, F.Vajdos, M.A.Brodney. Aminomethyl-Derived Beta Secretase (BACE1) Inhibitors: Engaging GLY230 Without An Anilide Functionality. J. Med. Chem. V. 60 386 2017.
ISSN: ISSN 1520-4804
PubMed: 27997172
DOI: 10.1021/ACS.JMEDCHEM.6B01451