Magnesium in PDB 7vgh: Cryo-Em Structure of the Human P4-Type Flippase ATP8B1-CDC50B in the Auto-Inhibited E2P State

All present enzymatic activity of Cryo-Em Structure of the Human P4-Type Flippase ATP8B1-CDC50B in the Auto-Inhibited E2P State:
7.6.2.1;

The binding sites of Magnesium atom in the Cryo-Em Structure of the Human P4-Type Flippase ATP8B1-CDC50B in the Auto-Inhibited E2P State (pdb code 7vgh). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total only one binding site of Magnesium was determined in the Cryo-Em Structure of the Human P4-Type Flippase ATP8B1-CDC50B in the Auto-Inhibited E2P State, PDB code: 7vgh:

Magnesium binding site 1 out of 1 in the Cryo-Em Structure of the Human P4-Type Flippase ATP8B1-CDC50B in the Auto-Inhibited E2P State


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Cryo-Em Structure of the Human P4-Type Flippase ATP8B1-CDC50B in the Auto-Inhibited E2P State within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg1401 b:51.7 occ:1.00 OD2 B:PHD454 2.0 65.0 1.0 O B:THR456 2.1 54.8 1.0 OP2 B:PHD454 2.7 65.0 1.0 OD1 B:ASP893 2.8 50.1 1.0 CG B:PHD454 3.2 65.0 1.0 C B:THR456 3.3 54.8 1.0 O B:ASP893 3.4 50.1 1.0 OD1 B:PHD454 3.7 65.0 1.0 P B:PHD454 3.8 65.0 1.0 CG B:ASP893 3.9 50.1 1.0 C B:ASP893 4.1 50.1 1.0 CA B:THR456 4.2 54.8 1.0 CB B:THR456 4.2 54.8 1.0 OP1 B:PHD454 4.3 65.0 1.0 N B:GLY457 4.3 52.0 1.0 O B:ALA229 4.3 69.5 1.0 OD2 B:ASP893 4.3 50.1 1.0 CG2 B:THR456 4.4 54.8 1.0 OD1 B:ASN896 4.4 55.9 1.0 N B:THR456 4.4 54.8 1.0 CA B:GLY457 4.4 52.0 1.0 CB B:PHD454 4.4 65.0 1.0 OD2 B:ASP897 4.4 52.2 1.0 OG1 B:THR458 4.5 49.8 1.0 N B:ASP893 4.8 50.1 1.0 N B:GLY894 4.8 53.7 1.0 CA B:ASP893 4.9 50.1 1.0 N B:THR458 4.9 49.8 1.0 CA B:GLY894 4.9 53.7 1.0 C B:GLY457 4.9 52.0 1.0 CB B:ASP893 5.0 50.1 1.0

M.T.Cheng, Y.Chen, Z.P.Chen, X.Liu, Z.Zhang, Y.Chen, W.T.Hou, C.Z.Zhou. Structural Insights Into the Activation of Autoinhibited Human Lipid Flippase ATP8B1 Upon Substrate Binding. Proc.Natl.Acad.Sci.Usa V. 119 56119 2022.
ISSN: ESSN 1091-6490
PubMed: 35349344
DOI: 10.1073/PNAS.2118656119