Magnesium in PDB 6c0v: Molecular Structure of Human P-Glycoprotein in the Atp-Bound, Outward- Facing Conformation

All present enzymatic activity of Molecular Structure of Human P-Glycoprotein in the Atp-Bound, Outward- Facing Conformation:
3.6.3.44;

The binding sites of Magnesium atom in the Molecular Structure of Human P-Glycoprotein in the Atp-Bound, Outward- Facing Conformation (pdb code 6c0v). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Molecular Structure of Human P-Glycoprotein in the Atp-Bound, Outward- Facing Conformation, PDB code: 6c0v:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the Molecular Structure of Human P-Glycoprotein in the Atp-Bound, Outward- Facing Conformation


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Molecular Structure of Human P-Glycoprotein in the Atp-Bound, Outward- Facing Conformation within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg1303 b:0.0 occ:1.00 O2B A:ATP1302 2.0 0.8 1.0 OE1 A:GLN1118 2.1 0.5 1.0 O2G A:ATP1302 2.2 0.1 1.0 OG A:SER1077 2.2 0.5 1.0 CD A:GLN1118 2.9 0.7 1.0 NE2 A:GLN1118 3.1 0.3 1.0 PB A:ATP1302 3.2 0.5 1.0 PG A:ATP1302 3.3 0.5 1.0 CB A:SER1077 3.4 0.8 1.0 O3B A:ATP1302 3.5 0.7 1.0 O1G A:ATP1302 3.8 0.2 1.0 O2A A:ATP1302 4.0 0.7 1.0 OD2 A:ASP1200 4.1 0.9 1.0 O1B A:ATP1302 4.2 0.2 1.0 OD1 A:ASP1200 4.2 0.9 1.0 CG A:GLN1118 4.4 0.3 1.0 N A:SER1077 4.4 0.1 1.0 O3A A:ATP1302 4.4 0.6 1.0 CA A:SER1077 4.5 0.8 1.0 N A:GLY533 4.6 0.5 1.0 PA A:ATP1302 4.6 0.4 1.0 CG A:ASP1200 4.6 0.9 1.0 O3G A:ATP1302 4.6 0.8 1.0 NE2 A:GLN1201 4.7 0.7 1.0 O1A A:ATP1302 4.7 0.4 1.0 CB A:GLN1118 4.9 0.2 1.0

Magnesium binding site 2 out of 2 in the Molecular Structure of Human P-Glycoprotein in the Atp-Bound, Outward- Facing Conformation


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Molecular Structure of Human P-Glycoprotein in the Atp-Bound, Outward- Facing Conformation within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg1304 b:0.7 occ:1.00 OG A:SER434 2.0 0.3 1.0 O3G A:ATP1301 2.0 1.0 1.0 O2B A:ATP1301 2.1 0.4 1.0 OE1 A:GLN475 2.1 0.4 1.0 CB A:SER434 3.1 0.5 1.0 CD A:GLN475 3.1 0.0 1.0 O3B A:ATP1301 3.2 0.7 1.0 PG A:ATP1301 3.2 0.3 1.0 PB A:ATP1301 3.2 0.3 1.0 O1A A:ATP1301 3.5 0.7 1.0 NE2 A:GLN475 3.5 0.4 1.0 N A:SER434 4.0 0.5 1.0 O1G A:ATP1301 4.1 1.0 1.0 CA A:SER434 4.1 0.5 1.0 O3A A:ATP1301 4.2 0.1 1.0 O2G A:ATP1301 4.3 0.0 1.0 PA A:ATP1301 4.3 0.9 1.0 OD1 A:ASP555 4.3 0.6 1.0 O1B A:ATP1301 4.3 0.7 1.0 CG A:GLN475 4.5 0.8 1.0 OD2 A:ASP555 4.5 0.8 1.0 O2A A:ATP1301 4.8 0.3 1.0 CG A:ASP555 4.9 0.3 1.0 CB A:SER1177 5.0 0.2 1.0

Y.Kim, J.Chen. Molecular Structure of Human P-Glycoprotein in the Atp-Bound, Outward-Facing Conformation. Science V. 359 915 2018.
ISSN: ESSN 1095-9203
PubMed: 29371429
DOI: 10.1126/SCIENCE.AAR7389