Magnesium in PDB 3t1q: Mgla Bound to Gppnhp in Complex with Mglb

All present enzymatic activity of Mgla Bound to Gppnhp in Complex with Mglb:
3.6.5.2;

The structure of Mgla Bound to Gppnhp in Complex with Mglb, PDB code: 3t1q was solved by M.Miertzschke, I.R.Vetter, C.Koerner, A.Wittinghofer, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	45.18 / 2.70
Space group	C 2 2 21
Cell size a, b, c (Å), α, β, γ (°)	105.500, 175.100, 69.100, 90.00, 90.00, 90.00
R / Rfree (%)	19.7 / 26.8

The binding sites of Magnesium atom in the Mgla Bound to Gppnhp in Complex with Mglb (pdb code 3t1q). 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 Mgla Bound to Gppnhp in Complex with Mglb, PDB code: 3t1q:

Magnesium binding site 1 out of 1 in the Mgla Bound to Gppnhp in Complex with Mglb


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Mgla Bound to Gppnhp in Complex with Mglb within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg198 b:38.3 occ:1.00 O3G A:GNP197 1.9 31.1 1.0 OG1 A:THR54 2.0 31.4 1.0 O2B A:GNP197 2.1 24.7 1.0 OG1 A:THR26 2.1 30.8 1.0 O A:HOH201 2.2 21.3 1.0 O A:HOH247 2.2 48.4 1.0 CB A:THR54 3.1 32.9 1.0 PG A:GNP197 3.2 29.8 1.0 PB A:GNP197 3.3 29.1 1.0 CB A:THR26 3.3 30.5 1.0 N3B A:GNP197 3.6 29.3 1.0 N A:THR54 3.8 35.0 1.0 N A:THR26 3.9 29.9 1.0 CG2 A:THR78 3.9 26.4 1.0 O1G A:GNP197 3.9 29.1 1.0 O A:HOH202 4.0 28.1 1.0 OD2 A:ASP58 4.0 22.0 1.0 CA A:THR54 4.0 32.8 1.0 CA A:THR26 4.1 29.7 1.0 CG2 A:THR54 4.2 32.4 1.0 O1B A:GNP197 4.3 31.0 1.0 O2G A:GNP197 4.3 28.0 1.0 O1A A:GNP197 4.4 26.4 1.0 CG2 A:THR26 4.4 26.8 1.0 O3A A:GNP197 4.4 28.2 1.0 PA A:GNP197 4.7 28.9 1.0 O2A A:GNP197 4.7 29.3 1.0 O A:VAL79 4.8 26.3 1.0 O A:HOH254 4.9 28.4 1.0 C A:ARG53 4.9 37.8 1.0 CB A:LYS25 5.0 30.3 1.0 O A:GLU52 5.0 45.1 1.0 CE A:LYS25 5.0 23.8 1.0 C A:LYS25 5.0 30.4 1.0

M.Miertzschke, C.Koerner, I.R.Vetter, D.Keilberg, E.Hot, S.Leonardy, L.Sogaard-Andersen, A.Wittinghofer. Structural Analysis of the Ras-Like G Protein Mgla and Its Cognate Gap Mglb and Implications For Bacterial Polarity. Embo J. V. 30 4185 2011.
ISSN: ISSN 0261-4189
PubMed: 21847100
DOI: 10.1038/EMBOJ.2011.291