Magnesium in PDB 7ks4: Thermus Phage P74-26 Large Terminase Atpase Domain with Partially Bound Adp

The structure of Thermus Phage P74-26 Large Terminase Atpase Domain with Partially Bound Adp, PDB code: 7ks4 was solved by B.J.Hilbert, B.A.Kelch, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	45.79 / 1.89
Space group	I 2 3
Cell size a, b, c (Å), α, β, γ (°)	129.515, 129.515, 129.515, 90, 90, 90
R / Rfree (%)	19.9 / 22.1

The binding sites of Magnesium atom in the Thermus Phage P74-26 Large Terminase Atpase Domain with Partially Bound Adp (pdb code 7ks4). 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 Thermus Phage P74-26 Large Terminase Atpase Domain with Partially Bound Adp, PDB code: 7ks4:

Magnesium binding site 1 out of 1 in the Thermus Phage P74-26 Large Terminase Atpase Domain with Partially Bound Adp


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Thermus Phage P74-26 Large Terminase Atpase Domain with Partially Bound Adp within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg309 b:26.2 occ:0.40 NZ B:LYS43 0.7 66.1 0.5 CE B:LYS43 0.9 61.5 0.5 CD B:LYS43 2.0 51.5 0.5 O3B B:ADP308 2.8 35.7 0.5 OG B:SER44 3.0 59.6 1.0 CG B:LYS43 3.1 47.7 0.5 OD1 B:ASP149 3.2 40.2 1.0 O B:HOH466 3.7 44.7 1.0 OD2 B:ASP149 3.8 44.2 1.0 CG B:ASP149 3.9 40.7 1.0 O B:HOH401 4.0 45.2 1.0 O1A B:ADP308 4.1 38.8 0.5 N B:SER44 4.1 46.5 1.0 CB B:SER44 4.1 56.1 1.0 CE B:LYS43 4.1 62.5 0.5 PB B:ADP308 4.1 34.2 0.5 CB B:LYS43 4.1 44.9 0.5 NE2 B:GLN72 4.3 51.9 1.0 CB B:LYS43 4.3 44.5 0.5 O1B B:ADP308 4.3 42.2 0.5 CA B:SER44 4.4 49.9 1.0 O B:HOH427 4.4 23.3 0.3 NZ B:LYS43 4.8 65.8 0.5 C B:LYS43 4.8 43.1 0.5 C B:LYS43 4.8 43.0 0.5 O2B B:ADP308 4.9 25.8 0.5 CD B:LYS43 5.0 51.0 0.5

J.Pajak, R.Atz, B.J.Hilbert, M.C.Morais, B.A.Kelch, P.J.Jardine, G.Arya. Viral Packaging Atpases Utilize A Glutamate Switch to Couple Atpase Activity and Dna Translocation. Proc.Natl.Acad.Sci.Usa V. 118 2021.
ISSN: ESSN 1091-6490
PubMed: 33888587
DOI: 10.1073/PNAS.2024928118