Magnesium in PDB 4zgn: Structure CDC123 Complexed with the C-Terminal Domain of EIF2GAMMA

The structure of Structure CDC123 Complexed with the C-Terminal Domain of EIF2GAMMA, PDB code: 4zgn was solved by M.Panvert, E.Dubiez, L.Arnold, J.Perez, W.Seufert, Y.Mechulam, E.Schmitt, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	45.00 / 2.90
Space group	C 2 2 21
Cell size a, b, c (Å), α, β, γ (°)	74.260, 116.640, 132.580, 90.00, 90.00, 90.00
R / Rfree (%)	19.5 / 26.2

The binding sites of Magnesium atom in the Structure CDC123 Complexed with the C-Terminal Domain of EIF2GAMMA (pdb code 4zgn). 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 CDC123 Complexed with the C-Terminal Domain of EIF2GAMMA, PDB code: 4zgn:

Magnesium binding site 1 out of 1 in the Structure CDC123 Complexed with the C-Terminal Domain of EIF2GAMMA


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Structure CDC123 Complexed with the C-Terminal Domain of EIF2GAMMA within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg402 b:72.6 occ:1.00 OD2 A:ASP239 2.1 81.0 1.0 O1B A:ATP401 2.1 85.4 1.0 OD1 A:ASN241 2.2 90.0 1.0 O A:HOH501 2.5 59.4 1.0 O3G A:ATP401 2.6 96.5 1.0 O A:HOH505 2.7 71.0 1.0 O3B A:ATP401 3.0 85.7 1.0 PB A:ATP401 3.1 80.7 1.0 PG A:ATP401 3.3 94.4 1.0 CG A:ASP239 3.3 78.5 1.0 CG A:ASN241 3.4 93.8 1.0 O A:TRP99 3.6 76.3 1.0 CB A:ASP239 4.0 70.5 1.0 O2G A:ATP401 4.0 99.8 1.0 O2B A:ATP401 4.0 79.5 1.0 ND2 A:ASN241 4.0 83.2 1.0 OD1 A:ASP239 4.3 79.0 1.0 O3A A:ATP401 4.3 76.0 1.0 NZ A:LYS96 4.5 81.7 1.0 CB A:ASN241 4.5 76.7 1.0 OD2 A:ASP227 4.5 85.8 1.0 O1G A:ATP401 4.6 94.9 1.0 CE A:LYS96 4.6 71.4 1.0 C A:TRP99 4.7 77.2 1.0 O1A A:ATP401 4.8 75.5 1.0

M.Panvert, E.Dubiez, L.Arnold, J.Perez, Y.Mechulam, W.Seufert, E.Schmitt. CDC123, A Cell Cycle Regulator Needed For EIF2 Assembly, Is An Atp-Grasp Protein with Unique Features. Structure V. 23 1596 2015.
ISSN: ISSN 0969-2126
PubMed: 26211610
DOI: 10.1016/J.STR.2015.06.014