Magnesium in PDB 8sa0: Cryoem Structure of P-Glycoprotein in Occluded Closed State Under Continuous Turnover Conditions with Verapamil

All present enzymatic activity of Cryoem Structure of P-Glycoprotein in Occluded Closed State Under Continuous Turnover Conditions with Verapamil:
7.6.2.1; 7.6.2.2;

The binding sites of Magnesium atom in the Cryoem Structure of P-Glycoprotein in Occluded Closed State Under Continuous Turnover Conditions with Verapamil (pdb code 8sa0). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Cryoem Structure of P-Glycoprotein in Occluded Closed State Under Continuous Turnover Conditions with Verapamil, PDB code: 8sa0:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the Cryoem Structure of P-Glycoprotein in Occluded Closed State Under Continuous Turnover Conditions with Verapamil


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Cryoem Structure of P-Glycoprotein in Occluded Closed State Under Continuous Turnover Conditions with Verapamil within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg1302 b:33.3 occ:1.00 O2B A:ATP1301 2.3 32.1 1.0 CB A:SER1077 2.5 35.3 1.0 O1G A:ATP1301 2.8 32.1 1.0 O3B A:ATP1301 2.9 32.1 1.0 PB A:ATP1301 3.0 32.1 1.0 PG A:ATP1301 3.3 32.1 1.0 O3A A:ATP1301 3.3 32.1 1.0 H A:SER1077 3.4 35.3 1.0 CA A:SER1077 3.5 35.3 1.0 HA A:SER1077 3.5 35.3 1.0 N A:SER1077 3.7 35.3 1.0 O2G A:ATP1301 3.9 32.1 1.0 O1B A:ATP1301 4.4 32.1 1.0 CB A:ASP1200 4.5 97.3 1.0 PA A:ATP1301 4.5 32.1 1.0 O3G A:ATP1301 4.7 32.1 1.0 O2A A:ATP1301 4.7 32.1 1.0 C A:SER1077 4.8 35.3 1.0 C A:LYS1076 4.9 41.7 1.0 CB A:LEU561 4.9 167.5 1.0 O1A A:ATP1301 4.9 32.1 1.0

Magnesium binding site 2 out of 2 in the Cryoem Structure of P-Glycoprotein in Occluded Closed State Under Continuous Turnover Conditions with Verapamil


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Cryoem Structure of P-Glycoprotein in Occluded Closed State Under Continuous Turnover Conditions with Verapamil within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg1303 b:54.7 occ:1.00 O2B A:ATP1305 2.4 65.7 1.0 O2G A:ATP1305 2.6 65.7 1.0 CB A:SER434 3.1 60.6 1.0 H A:SER434 3.3 60.6 1.0 O3B A:ATP1305 3.3 65.7 1.0 PB A:ATP1305 3.5 65.7 1.0 PG A:ATP1305 3.5 65.7 1.0 N A:SER434 3.7 60.6 1.0 CA A:SER434 3.8 60.6 1.0 HA A:SER434 3.8 60.6 1.0 O2A A:ATP1305 3.9 65.7 1.0 O1G A:ATP1305 4.1 65.7 1.0 O3A A:ATP1305 4.3 65.7 1.0 O1B A:ATP1305 4.6 65.7 1.0 H A:GLY1178 4.6 67.2 1.0 PA A:ATP1305 4.7 65.7 1.0 C A:LYS433 4.7 66.5 1.0 CB A:LYS433 4.7 66.5 1.0 O3G A:ATP1305 4.8 65.7 1.0 CB A:SER1177 4.9 64.9 1.0

A.T.Culbertson, M.Liao. Cryo-Em of Human P-Glycoprotein Reveals An Intermediate Occluded Conformation During Active Drug Transport. Nat Commun V. 16 3619 2025.
ISSN: ESSN 2041-1723
PubMed: 40240353
DOI: 10.1038/S41467-025-58561-4