Magnesium in PDB 1g7t: X-Ray Structure of Translation Initiation Factor IF2/EIF5B Complexed with Gdpnp

The structure of X-Ray Structure of Translation Initiation Factor IF2/EIF5B Complexed with Gdpnp, PDB code: 1g7t was solved by A.Roll-Mecak, C.Cao, T.E.Dever, S.K.Burley, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	22.00 / 2.00
Space group	P 1
Cell size a, b, c (Å), α, β, γ (°)	48.799, 53.680, 94.926, 105.17, 94.76, 100.17
R / Rfree (%)	23.1 / 26.7

The binding sites of Magnesium atom in the X-Ray Structure of Translation Initiation Factor IF2/EIF5B Complexed with Gdpnp (pdb code 1g7t). 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 X-Ray Structure of Translation Initiation Factor IF2/EIF5B Complexed with Gdpnp, PDB code: 1g7t:

Magnesium binding site 1 out of 1 in the X-Ray Structure of Translation Initiation Factor IF2/EIF5B Complexed with Gdpnp


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of X-Ray Structure of Translation Initiation Factor IF2/EIF5B Complexed with Gdpnp within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg602 b:35.4 occ:1.00 O A:HOH844 2.4 25.6 1.0 O1A A:GNP601 2.6 27.6 1.0 O2B A:GNP601 2.8 25.2 1.0 OG1 A:THR19 2.9 20.8 1.0 O3G A:GNP601 3.0 29.3 1.0 N3B A:GNP601 3.2 27.9 1.0 O A:HOH934 3.2 26.8 1.0 CB A:THR19 3.3 23.4 1.0 O A:HOH895 3.4 57.1 1.0 PB A:GNP601 3.5 25.6 1.0 PA A:GNP601 3.6 27.3 1.0 PG A:GNP601 3.8 29.6 1.0 O3A A:GNP601 3.8 26.1 1.0 O2A A:GNP601 4.0 28.2 1.0 CG2 A:THR19 4.0 24.1 1.0 O A:HOH968 4.1 43.7 1.0 O1G A:GNP601 4.1 31.1 1.0 CA A:THR19 4.5 22.7 1.0 N A:THR19 4.5 22.5 1.0 O1B A:GNP601 4.9 26.1 1.0

A.Roll-Mecak, C.Cao, T.E.Dever, S.K.Burley. X-Ray Structures of the Universal Translation Initiation Factor IF2/EIF5B: Conformational Changes on Gdp and Gtp Binding. Cell(Cambridge,Mass.) V. 103 781 2000.
ISSN: ISSN 0092-8674
PubMed: 11114334
DOI: 10.1016/S0092-8674(00)00181-1