Magnesium in PDB 1qpg: 3-Phosphoglycerate Kinase, Mutation R65Q

All present enzymatic activity of 3-Phosphoglycerate Kinase, Mutation R65Q:
2.7.2.3;

The structure of 3-Phosphoglycerate Kinase, Mutation R65Q, PDB code: 1qpg was solved by T.M.Mcphillips, B.T.Hsu, M.A.Sherman, M.T.Mas, D.C.Rees, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	8.00 / 2.40
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	96.000, 70.100, 82.300, 90.00, 122.20, 90.00
R / Rfree (%)	18.5 / n/a

The binding sites of Magnesium atom in the 3-Phosphoglycerate Kinase, Mutation R65Q (pdb code 1qpg). 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 3-Phosphoglycerate Kinase, Mutation R65Q, PDB code: 1qpg:

Magnesium binding site 1 out of 1 in the 3-Phosphoglycerate Kinase, Mutation R65Q


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of 3-Phosphoglycerate Kinase, Mutation R65Q within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg450 b:40.5 occ:1.00 MG A:MAP450 0.0 40.5 1.0 O2A A:MAP450 2.2 46.8 1.0 O1G A:MAP450 2.4 44.5 1.0 O1B A:MAP450 2.5 43.6 1.0 PA A:MAP450 3.2 41.1 1.0 PG A:MAP450 3.3 46.8 1.0 PB A:MAP450 3.4 42.0 1.0 O3A A:MAP450 3.5 36.5 1.0 O2G A:MAP450 3.6 53.2 1.0 OD2 A:ASP372 3.7 46.0 1.0 N3B A:MAP450 3.7 44.8 1.0 O1A A:MAP450 4.2 35.5 1.0 O5' A:MAP450 4.3 42.7 1.0 O3G A:MAP450 4.7 53.1 1.0 N A:ASP372 4.7 37.4 1.0 CG A:ASP372 4.7 45.8 1.0 O2B A:MAP450 4.7 31.5 1.0 N A:GLY371 4.8 38.7 1.0 CA A:GLY371 4.8 35.5 1.0 C5' A:MAP450 5.0 39.0 1.0

T.M.Mcphillips, B.T.Hsu, M.A.Sherman, M.T.Mas, D.C.Rees. Structure of the R65Q Mutant of Yeast 3-Phosphoglycerate Kinase Complexed with Mg-Amp-Pnp and 3-Phospho-D-Glycerate. Biochemistry V. 35 4118 1996.
ISSN: ISSN 0006-2960
PubMed: 8672447
DOI: 10.1021/BI952500O