Magnesium in PDB 8dhu: Crystal Structure of Larp-DM15 From Drosophila Melanogaster Bound to M7GPPPC

The structure of Crystal Structure of Larp-DM15 From Drosophila Melanogaster Bound to M7GPPPC, PDB code: 8dhu was solved by E.Nguyen, A.J.Berman, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	44.01 / 2.30
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	46.808, 60.737, 129.199, 90, 90, 90
R / Rfree (%)	22 / 27.5

The binding sites of Magnesium atom in the Crystal Structure of Larp-DM15 From Drosophila Melanogaster Bound to M7GPPPC (pdb code 8dhu). 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 Crystal Structure of Larp-DM15 From Drosophila Melanogaster Bound to M7GPPPC, PDB code: 8dhu:

Magnesium binding site 1 out of 1 in the Crystal Structure of Larp-DM15 From Drosophila Melanogaster Bound to M7GPPPC


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Crystal Structure of Larp-DM15 From Drosophila Melanogaster Bound to M7GPPPC within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg1002 b:77.5 occ:1.00 H311 B:91P1001 2.5 86.3 1.0 H221 B:91P1001 3.0 100.7 1.0 H261 B:91P1001 3.1 84.7 1.0 C31 B:91P1001 3.4 72.1 1.0 O13 B:91P1001 3.7 120.0 1.0 O12 B:91P1001 3.8 135.5 1.0 C22 B:91P1001 3.9 84.0 1.0 C26 B:91P1001 4.0 70.7 1.0 H321 B:91P1001 4.0 88.8 1.0 H222 B:91P1001 4.1 100.7 1.0 C32 B:91P1001 4.2 74.2 1.0 H281 B:91P1001 4.3 88.7 1.0 P10 B:91P1001 4.4 88.7 1.0 O24 B:91P1001 4.4 65.9 1.0 N30 B:91P1001 4.4 72.5 1.0 C23 B:91P1001 4.5 71.8 1.0 C28 B:91P1001 4.5 74.1 1.0 C25 B:91P1001 4.5 69.2 1.0 OH B:TYR883 4.6 59.1 1.0 H401 B:91P1001 4.7 103.5 1.0 P14 B:91P1001 4.9 94.5 1.0 O16 B:91P1001 4.9 80.5 1.0 HH B:TYR883 4.9 70.7 1.0 O21 B:91P1001 4.9 87.3 1.0

E.Nguyen, A.J.Berman. Comparative Analysis of the LARP1 C-Terminal DM15 Region Through Coelomate Evolution To Be Published.