Magnesium in PDB 6roh: Cryo-Em Structure of the Autoinhibited DRS2P-CDC50P

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

The structure of Cryo-Em Structure of the Autoinhibited 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 Autoinhibited DRS2P-CDC50P (pdb code 6roh). 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 Autoinhibited DRS2P-CDC50P, PDB code: 6roh:

Magnesium binding site 1 out of 1 in the Cryo-Em Structure of the Autoinhibited 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 Autoinhibited DRS2P-CDC50P within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg2102 b:56.3 occ:1.00 F2 A:BFD560 1.7 55.8 1.0 O A:HOH2201 1.7 55.5 1.0 O A:HOH2202 1.9 55.7 1.0 O A:THR562 2.0 55.1 1.0 OD2 A:BFD560 2.1 55.8 1.0 OD1 A:ASP954 2.1 55.4 1.0 BE A:BFD560 2.9 55.8 1.0 CG A:BFD560 2.9 55.8 1.0 OD1 A:BFD560 3.1 55.8 1.0 C A:THR562 3.2 55.1 1.0 CG A:ASP954 3.3 55.4 1.0 O A:ASP954 3.5 55.4 1.0 OD2 A:ASP954 3.8 55.4 1.0 F3 A:BFD560 3.8 55.8 1.0 OG1 A:THR564 3.9 52.6 1.0 F1 A:BFD560 3.9 55.8 1.0 OD2 A:ASP958 3.9 59.4 1.0 CA A:THR562 4.0 55.1 1.0 N A:THR562 4.1 55.1 1.0 OD1 A:ASN957 4.2 61.6 1.0 N A:GLY563 4.2 53.9 1.0 N A:ASP954 4.2 55.4 1.0 CB A:THR562 4.3 55.1 1.0 C A:ASP954 4.3 55.4 1.0 CB A:BFD560 4.3 55.8 1.0 N A:THR564 4.4 52.6 1.0 CA A:GLY563 4.4 53.9 1.0 O A:ALA337 4.4 63.6 1.0 CB A:ASP954 4.5 55.4 1.0 CA A:ASP954 4.6 55.4 1.0 C A:LYS561 4.7 55.0 1.0 C A:GLY563 4.8 53.9 1.0 N A:LYS561 5.0 55.0 1.0 CB A:THR564 5.0 52.6 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