Fluorine in PDB 8ox6: Cryo-Em Structure of ATP8B1-CDC50A in E1P Conformation

All present enzymatic activity of Cryo-Em Structure of ATP8B1-CDC50A in E1P Conformation:
7.6.2.1;

The structure of Cryo-Em Structure of ATP8B1-CDC50A in E1P Conformation also contains other interesting chemical elements:

Aluminium	(Al)	1 atom
Magnesium	(Mg)	1 atom

The binding sites of Fluorine atom in the Cryo-Em Structure of ATP8B1-CDC50A in E1P Conformation (pdb code 8ox6). This binding sites where shown within 5.0 Angstroms radius around Fluorine atom.
In total 4 binding sites of Fluorine where determined in the Cryo-Em Structure of ATP8B1-CDC50A in E1P Conformation, PDB code: 8ox6:
Jump to Fluorine binding site number: 1; 2; 3; 4;

Fluorine binding site 1 out of 4 in the Cryo-Em Structure of ATP8B1-CDC50A in E1P Conformation


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 E1P Conformation within 5.0Å range: probe atom residue distance (Å) B Occ A:F1202 b:90.5 occ:1.00 F1 A:ALF1202 0.0 90.5 1.0 AL A:ALF1202 1.8 90.5 1.0 F4 A:ALF1202 2.5 90.5 1.0 F3 A:ALF1202 2.5 90.5 1.0 OG1 A:THR732 2.7 92.1 1.0 NZ A:LYS873 2.8 86.1 1.0 OD1 A:ASP454 3.0 82.7 1.0 ND2 A:ASN896 3.2 84.0 1.0 CB A:THR732 3.3 92.1 1.0 CE A:LYS873 3.4 86.1 1.0 CA A:THR732 3.5 92.1 1.0 F2 A:ALF1202 3.6 90.5 1.0 CG A:ASP454 3.6 82.7 1.0 O A:LEU731 3.9 86.9 1.0 OD2 A:ASP454 3.9 82.7 1.0 N A:GLY733 4.4 100.3 1.0 C A:THR732 4.5 92.1 1.0 CG A:ASN896 4.5 84.0 1.0 OD2 A:ASP897 4.5 78.8 1.0 N A:THR732 4.6 92.1 1.0 CB A:ASP454 4.7 82.7 1.0 C A:LEU731 4.7 86.9 1.0 CG2 A:THR732 4.8 92.1 1.0 CD A:LYS873 4.9 86.1 1.0

Fluorine binding site 2 out of 4 in the Cryo-Em Structure of ATP8B1-CDC50A in E1P Conformation


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 E1P Conformation within 5.0Å range: probe atom residue distance (Å) B Occ A:F1202 b:90.5 occ:1.00 F2 A:ALF1202 0.0 90.5 1.0 AL A:ALF1202 1.8 90.5 1.0 OD2 A:ASP454 2.1 82.7 1.0 MG A:MG1201 2.2 83.8 1.0 F4 A:ALF1202 2.5 90.5 1.0 F3 A:ALF1202 2.6 90.5 1.0 OE2 A:GLU914 2.6 84.2 1.0 O A:THR456 2.8 85.3 1.0 CG A:ASP454 2.9 82.7 1.0 OD1 A:ASP454 3.0 82.7 1.0 CB A:THR456 3.5 85.3 1.0 ND2 A:ASN896 3.5 84.0 1.0 CD A:GLU914 3.5 84.2 1.0 F1 A:ALF1202 3.6 90.5 1.0 OE1 A:GLU914 3.7 84.2 1.0 C A:THR456 3.7 85.3 1.0 CA A:THR456 3.9 85.3 1.0 N A:THR456 4.0 85.3 1.0 OD1 A:ASP897 4.2 78.8 1.0 CG2 A:THR456 4.2 85.3 1.0 OD1 A:ASN896 4.3 84.0 1.0 OD1 A:ASP893 4.3 77.0 1.0 CG A:ASN896 4.3 84.0 1.0 OG1 A:THR732 4.3 92.1 1.0 CB A:ASP454 4.3 82.7 1.0 OG1 A:THR456 4.4 85.3 1.0 O A:ASP893 4.5 77.0 1.0 CG A:GLU914 4.9 84.2 1.0 CG A:ASP897 5.0 78.8 1.0 N A:GLY457 5.0 79.7 1.0 NZ A:LYS873 5.0 86.1 1.0

Fluorine binding site 3 out of 4 in the Cryo-Em Structure of ATP8B1-CDC50A in E1P Conformation


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 E1P Conformation within 5.0Å range: probe atom residue distance (Å) B Occ A:F1202 b:90.5 occ:1.00 F3 A:ALF1202 0.0 90.5 1.0 AL A:ALF1202 1.8 90.5 1.0 ND2 A:ASN896 2.3 84.0 1.0 OD2 A:ASP454 2.3 82.7 1.0 F1 A:ALF1202 2.5 90.5 1.0 F2 A:ALF1202 2.6 90.5 1.0 NZ A:LYS873 2.6 86.1 1.0 CG A:ASP454 2.6 82.7 1.0 OD2 A:ASP897 2.8 78.8 1.0 OD1 A:ASP897 2.9 78.8 1.0 OD1 A:ASP454 3.0 82.7 1.0 CG A:ASP897 3.1 78.8 1.0 CG A:ASN896 3.1 84.0 1.0 OD1 A:ASN896 3.4 84.0 1.0 MG A:MG1201 3.5 83.8 1.0 CB A:ASP454 3.6 82.7 1.0 F4 A:ALF1202 3.6 90.5 1.0 CE A:LYS873 4.0 86.1 1.0 O A:ASP893 4.2 77.0 1.0 CB A:ASN896 4.3 84.0 1.0 CB A:ASP897 4.3 78.8 1.0 N A:ASP897 4.4 78.8 1.0 OG1 A:THR732 4.4 92.1 1.0 C A:ASN896 4.6 84.0 1.0 CA A:ASP897 4.7 78.8 1.0 OE2 A:GLU914 4.7 84.2 1.0 CA A:ASP454 4.8 82.7 1.0 OE1 A:GLU914 4.8 84.2 1.0 O A:THR456 4.9 85.3 1.0

Fluorine binding site 4 out of 4 in the Cryo-Em Structure of ATP8B1-CDC50A in E1P Conformation


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 4 of Cryo-Em Structure of ATP8B1-CDC50A in E1P Conformation within 5.0Å range: probe atom residue distance (Å) B Occ A:F1202 b:90.5 occ:1.00 F4 A:ALF1202 0.0 90.5 1.0 AL A:ALF1202 1.8 90.5 1.0 F1 A:ALF1202 2.5 90.5 1.0 OG1 A:THR732 2.5 92.1 1.0 F2 A:ALF1202 2.5 90.5 1.0 OD1 A:ASP454 3.0 82.7 1.0 CB A:THR456 3.6 85.3 1.0 F3 A:ALF1202 3.6 90.5 1.0 OG1 A:THR456 3.6 85.3 1.0 CG A:ASP454 3.8 82.7 1.0 OD2 A:ASP454 3.8 82.7 1.0 CB A:THR732 3.9 92.1 1.0 N A:THR456 4.0 85.3 1.0 ND2 A:ASN896 4.2 84.0 1.0 N A:GLY733 4.2 100.3 1.0 CA A:THR456 4.4 85.3 1.0 CA A:THR732 4.6 92.1 1.0 O A:THR456 4.6 85.3 1.0 OE2 A:GLU914 4.7 84.2 1.0 MG A:MG1201 4.7 83.8 1.0 CG2 A:THR456 4.7 85.3 1.0 N A:LYS455 4.9 86.3 1.0 CG2 A:THR732 4.9 92.1 1.0 C A:THR732 4.9 92.1 1.0 C A:THR456 5.0 85.3 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