Silicon in PDB 6c6n: Human Squalene Epoxidase (Sqle, Squalene Monooxygenase) Structure with Fad and Cmpd-4"

All present enzymatic activity of Human Squalene Epoxidase (Sqle, Squalene Monooxygenase) Structure with Fad and Cmpd-4":
1.14.14.17;

The structure of Human Squalene Epoxidase (Sqle, Squalene Monooxygenase) Structure with Fad and Cmpd-4", PDB code: 6c6n was solved by A.K.Padyana, L.Jin, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	37.17 / 2.30
Space group	P 32 2 1
Cell size a, b, c (Å), α, β, γ (°)	126.960, 126.960, 166.120, 90.00, 90.00, 120.00
R / Rfree (%)	18.9 / 22

The binding sites of Silicon atom in the Human Squalene Epoxidase (Sqle, Squalene Monooxygenase) Structure with Fad and Cmpd-4" (pdb code 6c6n). This binding sites where shown within 5.0 Angstroms radius around Silicon atom.
In total 2 binding sites of Silicon where determined in the Human Squalene Epoxidase (Sqle, Squalene Monooxygenase) Structure with Fad and Cmpd-4", PDB code: 6c6n:
Jump to Silicon binding site number: 1; 2;

Silicon binding site 1 out of 2 in the Human Squalene Epoxidase (Sqle, Squalene Monooxygenase) Structure with Fad and Cmpd-4"


Mono view


Stereo pair view

A full contact list of Silicon with other atoms in the Si binding site number 1 of Human Squalene Epoxidase (Sqle, Squalene Monooxygenase) Structure with Fad and Cmpd-4" within 5.0Å range: probe atom residue distance (Å) B Occ A:Si610 b:45.8 occ:1.00 SI1 A:EKV610 0.0 45.8 1.0 C31 A:EKV610 1.9 40.2 1.0 C32 A:EKV610 1.9 31.5 1.0 C22 A:EKV610 1.9 41.8 1.0 C24 A:EKV610 1.9 61.4 1.0 O21 A:EKV610 2.7 58.2 1.0 C29 A:EKV610 2.9 44.3 1.0 C25 A:EKV610 2.9 45.6 1.0 C30 A:EKV610 3.2 36.1 1.0 C19 A:EKV610 4.1 48.4 1.0 C28 A:EKV610 4.2 41.5 1.0 C26 A:EKV610 4.2 46.8 1.0 CD2 A:LEU333 4.3 45.0 1.0 C18 A:EKV610 4.6 40.8 1.0 C27 A:EKV610 4.7 49.4 1.0 CE2 A:PHE166 4.8 38.5 1.0 O A:LEU416 4.9 39.7 1.0 NE2 A:GLN168 4.9 33.5 1.0 CD2 A:PHE166 5.0 36.2 1.0

Silicon binding site 2 out of 2 in the Human Squalene Epoxidase (Sqle, Squalene Monooxygenase) Structure with Fad and Cmpd-4"


Mono view


Stereo pair view

A full contact list of Silicon with other atoms in the Si binding site number 2 of Human Squalene Epoxidase (Sqle, Squalene Monooxygenase) Structure with Fad and Cmpd-4" within 5.0Å range: probe atom residue distance (Å) B Occ B:Si605 b:44.9 occ:1.00 SI1 B:EKV605 0.0 44.9 1.0 C31 B:EKV605 1.9 42.2 1.0 C32 B:EKV605 1.9 33.6 1.0 C22 B:EKV605 1.9 39.2 1.0 C24 B:EKV605 1.9 43.2 1.0 O21 B:EKV605 2.7 38.0 1.0 C29 B:EKV605 2.9 39.0 1.0 C25 B:EKV605 2.9 55.1 1.0 C30 B:EKV605 3.2 27.8 1.0 C19 B:EKV605 4.1 37.9 1.0 C28 B:EKV605 4.2 35.6 1.0 C26 B:EKV605 4.2 40.2 1.0 CD2 B:LEU333 4.4 43.3 1.0 C18 B:EKV605 4.6 43.3 1.0 CB B:ALA322 4.7 29.6 1.0 C27 B:EKV605 4.7 41.9 1.0 CE2 B:PHE166 4.8 36.5 1.0 NE2 B:GLN168 4.9 30.6 1.0 O B:LEU416 4.9 36.9 1.0 CG B:TYR195 4.9 29.6 1.0

A.K.Padyana, S.Gross, L.Jin, G.Cianchetta, R.Narayanaswamy, F.Wang, R.Wang, C.Fang, X.Lv, S.A.Biller, L.Dang, C.E.Mahoney, N.Nagaraja, D.Pirman, Z.Sui, J.Popovici-Muller, G.A.Smolen. Structure and Inhibition Mechanism of the Catalytic Domain of Human Squalene Epoxidase. Nat Commun V. 10 97 2019.
ISSN: ESSN 2041-1723
PubMed: 30626872
DOI: 10.1038/S41467-018-07928-X