Magnesium in PDB 6roi: Cryo-Em Structure of the Partially Activated DRS2P-CDC50P

All present enzymatic activity of Cryo-Em Structure of the Partially Activated DRS2P-CDC50P:
7.6.2.1;

The structure of Cryo-Em Structure of the Partially Activated DRS2P-CDC50P also contains other interesting chemical elements:

Fluorine

(F)

3 atoms

The binding sites of Magnesium atom in the Cryo-Em Structure of the Partially Activated DRS2P-CDC50P (pdb code 6roi). 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 Partially Activated DRS2P-CDC50P, PDB code: 6roi:

Magnesium binding site 1 out of 1 in the Cryo-Em Structure of the Partially Activated DRS2P-CDC50P


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 Partially Activated DRS2P-CDC50P within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg1501 b:82.6 occ:1.00 F2 A:BFD560 1.7 71.9 1.0 O A:HOH1601 1.7 77.6 1.0 O A:HOH1602 1.8 80.1 1.0 O A:THR562 2.0 71.2 1.0 OD2 A:BFD560 2.1 71.9 1.0 OD1 A:ASP954 2.3 74.3 1.0 BE A:BFD560 2.8 71.9 1.0 CG A:BFD560 3.0 71.9 1.0 C A:THR562 3.2 71.2 1.0 OD1 A:BFD560 3.2 71.9 1.0 F1 A:BFD560 3.4 71.9 1.0 CG A:ASP954 3.4 74.3 1.0 O A:ASP954 3.5 74.3 1.0 OD2 A:ASP954 4.0 74.3 1.0 OG1 A:THR562 4.0 71.2 1.0 N A:GLY563 4.1 67.3 1.0 CA A:GLY563 4.1 67.3 1.0 F3 A:BFD560 4.1 71.9 1.0 OG1 A:THR564 4.2 66.9 1.0 CA A:THR562 4.2 71.2 1.0 C A:ASP954 4.3 74.3 1.0 N A:ASP954 4.3 74.3 1.0 N A:THR562 4.3 71.2 1.0 N A:THR564 4.3 66.9 1.0 CB A:BFD560 4.3 71.9 1.0 O A:ALA337 4.3 86.5 1.0 C A:GLY563 4.6 67.3 1.0 CB A:ASP954 4.6 74.3 1.0 CB A:THR562 4.6 71.2 1.0 CA A:ASP954 4.7 74.3 1.0 OD1 A:ASN957 4.8 83.3 1.0 ND2 A:ASN957 5.0 83.3 1.0

M.Timcenko, J.A.Lyons, D.Januliene, J.J.Ulstrup, T.Dieudonne, C.Montigny, M.R.Ash, J.L.Karlsen, T.Boesen, W.Kuhlbrandt, G.Lenoir, A.Moeller, P.Nissen. Structure and Autoregulation of A P4-Atpase Lipid Flippase. Nature V. 571 366 2019.
ISSN: ESSN 1476-4687
PubMed: 31243363
DOI: 10.1038/S41586-019-1344-7