Magnesium in PDB 5eul: Structure of the Seca-Secy Complex with A Translocating Polypeptide Substrate

The structure of Structure of the Seca-Secy Complex with A Translocating Polypeptide Substrate, PDB code: 5eul was solved by L.Li, E.Park, J.Ling, J.Ingram, H.Ploegh, T.A.Rapoport, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	53.85 / 3.70
Space group	P 61 2 2
Cell size a, b, c (Å), α, β, γ (°)	127.798, 127.798, 554.772, 90.00, 90.00, 120.00
R / Rfree (%)	29.5 / 31.5

The structure of Structure of the Seca-Secy Complex with A Translocating Polypeptide Substrate also contains other interesting chemical elements:

Fluorine	(F)	3 atoms
Bromine	(Br)	216 atoms
Tantalum	(Ta)	108 atoms

The binding sites of Magnesium atom in the Structure of the Seca-Secy Complex with A Translocating Polypeptide Substrate (pdb code 5eul). 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 Structure of the Seca-Secy Complex with A Translocating Polypeptide Substrate, PDB code: 5eul:

Magnesium binding site 1 out of 1 in the Structure of the Seca-Secy Complex with A Translocating Polypeptide Substrate


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Structure of the Seca-Secy Complex with A Translocating Polypeptide Substrate within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg1001 b:0.9 occ:1.00 O3B A:ADP1003 2.4 0.7 1.0 O3A A:ADP1003 3.5 0.0 1.0 PB A:ADP1003 3.6 0.7 1.0 OD2 A:ASP207 3.9 0.7 1.0 NZ A:LYS106 4.1 0.9 1.0 F3 A:BEF1002 4.1 0.6 1.0 OD1 A:ASP207 4.3 0.7 1.0 CG A:ASP207 4.4 0.7 1.0 CD A:LYS106 4.5 0.4 1.0 O2B A:ADP1003 4.5 0.9 1.0 F1 A:BEF1002 4.6 0.6 1.0 O1B A:ADP1003 4.7 0.2 1.0 CE A:LYS106 4.7 0.1 1.0 OG1 A:THR107 4.8 0.7 1.0 BE A:BEF1002 4.8 0.4 1.0 CB A:LYS106 4.9 0.9 1.0 PA A:ADP1003 4.9 0.8 1.0

L.Li, E.Park, J.Ling, J.Ingram, H.Ploegh, T.A.Rapoport. Crystal Structure of A Substrate-Engaged Secy Protein-Translocation Channel. Nature V. 531 395 2016.
ISSN: ESSN 1476-4687
PubMed: 26950603
DOI: 10.1038/NATURE17163