Magnesium in PDB 7oh5: Cryo-Em Structure of DRS2P-CDC50P in the E1-Alfx-Adp State

All present enzymatic activity of Cryo-Em Structure of DRS2P-CDC50P in the E1-Alfx-Adp State:
7.6.2.1;

The structure of Cryo-Em Structure of DRS2P-CDC50P in the E1-Alfx-Adp State also contains other interesting chemical elements:

Aluminium	(Al)	1 atom
Fluorine	(F)	4 atoms

The binding sites of Magnesium atom in the Cryo-Em Structure of DRS2P-CDC50P in the E1-Alfx-Adp State (pdb code 7oh5). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Cryo-Em Structure of DRS2P-CDC50P in the E1-Alfx-Adp State, PDB code: 7oh5:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the Cryo-Em Structure of DRS2P-CDC50P in the E1-Alfx-Adp State


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 DRS2P-CDC50P in the E1-Alfx-Adp State within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg1501 b:76.7 occ:1.00 O2A A:ADP1504 2.1 74.1 1.0 O3B A:ADP1504 3.3 74.1 1.0 PA A:ADP1504 3.3 74.1 1.0 O1A A:ADP1504 3.6 74.1 1.0 CE2 A:PHE698 4.1 77.9 1.0 CZ A:PHE698 4.2 77.9 1.0 O3A A:ADP1504 4.3 74.1 1.0 PB A:ADP1504 4.3 74.1 1.0 NH2 A:ARG755 4.4 77.0 1.0 ND2 A:ASN957 4.5 68.1 1.0 O5' A:ADP1504 4.5 74.1 1.0 C5' A:ADP1504 4.6 74.1 1.0 O1B A:ADP1504 4.9 74.1 1.0 OE2 A:GLU975 4.9 80.8 1.0 C8 A:ADP1504 5.0 74.1 1.0 OE1 A:GLU975 5.0 80.8 1.0

Magnesium binding site 2 out of 2 in the Cryo-Em Structure of DRS2P-CDC50P in the E1-Alfx-Adp State


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Cryo-Em Structure of DRS2P-CDC50P in the E1-Alfx-Adp State within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg1503 b:66.1 occ:1.00 F4 A:ALF1502 1.7 68.8 1.0 O A:THR562 2.0 65.7 1.0 O A:HOH1601 2.0 65.3 1.0 OD2 A:ASP560 2.0 63.0 1.0 O A:HOH1602 2.1 65.7 1.0 OD1 A:ASP954 2.2 65.2 1.0 CG A:ASP560 3.0 63.0 1.0 CG A:ASP954 3.2 65.2 1.0 C A:THR562 3.2 65.7 1.0 OD1 A:ASP560 3.3 63.0 1.0 AL A:ALF1502 3.3 68.8 1.0 O A:ASP954 3.4 65.2 1.0 F2 A:ALF1502 3.7 68.8 1.0 OD2 A:ASP954 3.7 65.2 1.0 F1 A:ALF1502 3.8 68.8 1.0 CA A:THR562 4.0 65.7 1.0 OD2 A:ASP958 4.1 64.1 1.0 CB A:THR562 4.1 65.7 1.0 N A:THR562 4.2 65.7 1.0 OG1 A:THR564 4.2 61.9 1.0 O1B A:ADP1504 4.2 74.1 1.0 N A:ASP954 4.2 65.2 1.0 N A:GLY563 4.2 64.1 1.0 C A:ASP954 4.2 65.2 1.0 CB A:ASP560 4.3 63.0 1.0 N A:THR564 4.3 61.9 1.0 CA A:GLY563 4.4 64.1 1.0 CB A:ASP954 4.5 65.2 1.0 CA A:ASP954 4.5 65.2 1.0 CG2 A:THR562 4.7 65.7 1.0 ND2 A:ASN957 4.8 68.1 1.0 C A:GLY563 4.9 64.1 1.0 C A:LYS561 4.9 64.8 1.0 OD1 A:ASN957 4.9 68.1 1.0 O3B A:ADP1504 4.9 74.1 1.0 F3 A:ALF1502 5.0 68.8 1.0

M.Timcenko, T.Dieudonne, C.Montigny, T.Boesen, J.A.Lyons, G.Lenoir, P.Nissen. Structural Basis of Substrate-Independent Phosphorylation in A P4-Atpase Lipid Flippase J.Mol.Biol. 67062 2021.
ISSN: ESSN 1089-8638
PubMed: 34023399
DOI: 10.1016/J.JMB.2021.167062