Magnesium in PDB 8sba: Cryoem Structure of P-Glycoprotein in Inward Facing 2 State Under Continuous Turnover Conditions with Vinblastine

All present enzymatic activity of Cryoem Structure of P-Glycoprotein in Inward Facing 2 State Under Continuous Turnover Conditions with Vinblastine:
7.6.2.1; 7.6.2.2;

The binding sites of Magnesium atom in the Cryoem Structure of P-Glycoprotein in Inward Facing 2 State Under Continuous Turnover Conditions with Vinblastine (pdb code 8sba). 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 Inward Facing 2 State Under Continuous Turnover Conditions with Vinblastine, PDB code: 8sba:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the Cryoem Structure of P-Glycoprotein in Inward Facing 2 State Under Continuous Turnover Conditions with Vinblastine


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 Inward Facing 2 State Under Continuous Turnover Conditions with Vinblastine within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg1302 b:85.2 occ:1.00 O2B A:ATP1301 2.2 89.9 1.0 O1G A:ATP1301 2.4 89.9 1.0 O3B A:ATP1301 2.6 89.9 1.0 OG A:SER1077 2.7 82.0 1.0 OE1 A:GLN1118 2.9 86.1 1.0 PG A:ATP1301 3.0 89.9 1.0 PB A:ATP1301 3.0 89.9 1.0 O2A A:ATP1301 3.2 89.9 1.0 NE2 A:GLN1118 3.7 86.1 1.0 CD A:GLN1118 3.7 86.1 1.0 O3A A:ATP1301 3.7 89.9 1.0 HB2 A:SER1077 3.7 82.0 1.0 H A:SER1077 3.8 82.0 1.0 O2G A:ATP1301 3.8 89.9 1.0 CB A:SER1077 3.8 82.0 1.0 PA A:ATP1301 4.1 89.9 1.0 O1B A:ATP1301 4.2 89.9 1.0 O3G A:ATP1301 4.2 89.9 1.0 HB3 A:SER1077 4.5 82.0 1.0 N A:SER1077 4.5 82.0 1.0 CA A:SER1077 4.8 82.0 1.0

Magnesium binding site 2 out of 2 in the Cryoem Structure of P-Glycoprotein in Inward Facing 2 State Under Continuous Turnover Conditions with Vinblastine


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 Inward Facing 2 State Under Continuous Turnover Conditions with Vinblastine within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg1303 b:71.4 occ:1.00 O2B A:ATP1306 2.0 78.1 1.0 O3G A:ATP1306 2.5 78.1 1.0 OG A:SER434 2.6 70.7 1.0 NE2 A:GLN475 2.8 67.5 1.0 OE1 A:GLN475 3.0 67.5 1.0 CD A:GLN475 3.3 67.5 1.0 PB A:ATP1306 3.4 78.1 1.0 PG A:ATP1306 3.7 78.1 1.0 O3B A:ATP1306 3.7 78.1 1.0 CB A:SER434 3.8 70.7 1.0 HB2 A:SER434 3.9 70.7 1.0 HB3 A:SER434 4.0 70.7 1.0 O1A A:ATP1306 4.2 78.1 1.0 O1B A:ATP1306 4.3 78.1 1.0 O3A A:ATP1306 4.3 78.1 1.0 O1G A:ATP1306 4.5 78.1 1.0 CG A:GLN475 4.7 67.5 1.0 H A:SER434 4.8 70.7 1.0 O2G A:ATP1306 4.8 78.1 1.0 PA A:ATP1306 4.8 78.1 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