Fluorine in PDB 8ox9: Cryo-Em Structure of ATP8B1-CDC50A in E2P Active Conformation with Bound Pc

All present enzymatic activity of Cryo-Em Structure of ATP8B1-CDC50A in E2P Active Conformation with Bound Pc:
7.6.2.1;

The structure of Cryo-Em Structure of ATP8B1-CDC50A in E2P Active Conformation with Bound Pc also contains other interesting chemical elements:

Magnesium

(Mg)

1 atom

The binding sites of Fluorine atom in the Cryo-Em Structure of ATP8B1-CDC50A in E2P Active Conformation with Bound Pc (pdb code 8ox9). This binding sites where shown within 5.0 Angstroms radius around Fluorine atom.
In total 3 binding sites of Fluorine where determined in the Cryo-Em Structure of ATP8B1-CDC50A in E2P Active Conformation with Bound Pc, PDB code: 8ox9:
Jump to Fluorine binding site number: 1; 2; 3;

Fluorine binding site 1 out of 3 in the Cryo-Em Structure of ATP8B1-CDC50A in E2P Active Conformation with Bound Pc


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 1 of Cryo-Em Structure of ATP8B1-CDC50A in E2P Active Conformation with Bound Pc within 5.0Å range: probe atom residue distance (Å) B Occ A:F1301 b:40.5 occ:1.00 F1 A:BEF1301 0.0 40.5 1.0 BE A:BEF1301 1.5 40.5 1.0 OD1 A:ASP454 2.3 38.1 1.0 ND2 A:ASN896 2.4 39.8 1.0 F3 A:BEF1301 2.5 40.5 1.0 F2 A:BEF1301 2.6 40.5 1.0 NZ A:LYS873 2.9 36.9 1.0 CG A:ASP454 3.2 38.1 1.0 N A:GLY733 3.2 42.5 1.0 OD2 A:ASP454 3.5 38.1 1.0 CA A:GLY233 3.6 46.9 1.0 N A:GLY233 3.6 46.9 1.0 CG A:ASN896 3.6 39.8 1.0 CE A:LYS873 3.8 36.9 1.0 CA A:THR732 3.9 42.2 1.0 OG1 A:THR732 3.9 42.2 1.0 C A:THR732 4.0 42.2 1.0 CA A:GLY733 4.1 42.5 1.0 OD1 A:ASN896 4.2 39.8 1.0 C A:ASP232 4.2 49.3 1.0 MG A:MG1302 4.2 35.5 1.0 OD1 A:ASP897 4.3 36.6 1.0 CB A:THR732 4.5 42.2 1.0 O A:LEU731 4.5 39.9 1.0 CB A:ASP454 4.5 38.1 1.0 O A:ASP232 4.7 49.3 1.0 CB A:ASN896 4.8 39.8 1.0 OD2 A:ASP897 4.8 36.6 1.0 CA A:ASP232 4.9 49.3 1.0 C A:GLY733 4.9 42.5 1.0 N A:LYS455 4.9 42.1 1.0 CG A:ASP897 5.0 36.6 1.0 N A:ASP734 5.0 47.6 1.0 N A:THR732 5.0 42.2 1.0

Fluorine binding site 2 out of 3 in the Cryo-Em Structure of ATP8B1-CDC50A in E2P Active Conformation with Bound Pc


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 2 of Cryo-Em Structure of ATP8B1-CDC50A in E2P Active Conformation with Bound Pc within 5.0Å range: probe atom residue distance (Å) B Occ A:F1301 b:40.5 occ:1.00 F2 A:BEF1301 0.0 40.5 1.0 BE A:BEF1301 1.6 40.5 1.0 OD2 A:ASP454 1.8 38.1 1.0 MG A:MG1302 2.1 35.5 1.0 CG A:ASP454 2.3 38.1 1.0 OD1 A:ASP454 2.4 38.1 1.0 F3 A:BEF1301 2.5 40.5 1.0 F1 A:BEF1301 2.6 40.5 1.0 O A:THR456 2.8 43.2 1.0 N A:THR456 3.2 43.2 1.0 CB A:THR456 3.4 43.2 1.0 CA A:THR456 3.5 43.2 1.0 C A:THR456 3.6 43.2 1.0 CB A:ASP454 3.8 38.1 1.0 OD1 A:ASP893 3.9 39.9 1.0 CA A:GLY233 3.9 46.9 1.0 OG1 A:THR456 3.9 43.2 1.0 N A:LYS455 4.0 42.1 1.0 ND2 A:ASN896 4.1 39.8 1.0 C A:LYS455 4.2 42.1 1.0 OD2 A:ASP897 4.4 36.6 1.0 O A:ASP893 4.5 39.9 1.0 CG2 A:THR456 4.6 43.2 1.0 CA A:ASP454 4.6 38.1 1.0 CA A:LYS455 4.6 42.1 1.0 NZ A:LYS873 4.6 36.9 1.0 N A:GLY233 4.6 46.9 1.0 C A:ASP454 4.7 38.1 1.0 OG1 A:THR732 4.7 42.2 1.0 OD1 A:ASN896 4.7 39.8 1.0 CG A:ASN896 4.9 39.8 1.0 N A:GLY457 4.9 39.6 1.0 O A:ALA229 4.9 49.7 1.0

Fluorine binding site 3 out of 3 in the Cryo-Em Structure of ATP8B1-CDC50A in E2P Active Conformation with Bound Pc


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 3 of Cryo-Em Structure of ATP8B1-CDC50A in E2P Active Conformation with Bound Pc within 5.0Å range: probe atom residue distance (Å) B Occ A:F1301 b:40.5 occ:1.00 F3 A:BEF1301 0.0 40.5 1.0 BE A:BEF1301 1.5 40.5 1.0 OG1 A:THR732 2.2 42.2 1.0 F2 A:BEF1301 2.5 40.5 1.0 F1 A:BEF1301 2.5 40.5 1.0 OD1 A:ASP454 2.7 38.1 1.0 N A:THR456 3.1 43.2 1.0 OG1 A:THR456 3.1 43.2 1.0 CB A:THR732 3.2 42.2 1.0 CA A:GLY233 3.3 46.9 1.0 CB A:THR456 3.6 43.2 1.0 N A:LYS455 3.6 42.1 1.0 CG A:ASP454 3.6 38.1 1.0 CA A:THR732 3.6 42.2 1.0 N A:GLY733 3.7 42.5 1.0 CB A:LYS455 3.7 42.1 1.0 OD2 A:ASP454 3.9 38.1 1.0 CA A:THR456 3.9 43.2 1.0 CA A:LYS455 4.0 42.1 1.0 C A:LYS455 4.0 42.1 1.0 C A:THR732 4.1 42.2 1.0 N A:GLY233 4.1 46.9 1.0 N A:ASP734 4.3 47.6 1.0 C A:GLY233 4.3 46.9 1.0 O A:GLY233 4.3 46.9 1.0 CE A:LYS455 4.5 42.1 1.0 MG A:MG1302 4.5 35.5 1.0 CB A:ASP734 4.5 47.6 1.0 CG2 A:THR732 4.5 42.2 1.0 O A:THR456 4.6 43.2 1.0 CA A:GLY733 4.7 42.5 1.0 C A:ASP454 4.7 38.1 1.0 C A:THR456 4.8 43.2 1.0 NZ A:LYS873 4.8 36.9 1.0 CG A:LYS455 4.8 42.1 1.0 CB A:ASP454 4.8 38.1 1.0 ND2 A:ASN896 4.8 39.8 1.0 C A:GLY733 4.9 42.5 1.0 N A:THR732 4.9 42.2 1.0 O A:LEU731 4.9 39.9 1.0 CA A:ASP454 4.9 38.1 1.0 CG2 A:THR456 5.0 43.2 1.0

T.Dieudonne, F.Kummerer, M.J.Laursen, C.Stock, R.K.Flygaard, S.Khalid, G.Lenoir, J.A.Lyons, K.Lindorff-Larsen, P.Nissen. Activation and Substrate Specificity of the Human P4-Atpase ATP8B1. Nat Commun V. 14 7492 2023.
ISSN: ESSN 2041-1723
PubMed: 37980352
DOI: 10.1038/S41467-023-42828-9