Magnesium in PDB 3gqk: Crystal Structure of the Bacteriophage PHI29 Gene Product 12 C- Terminal Fragment in Complex with Atp

The structure of Crystal Structure of the Bacteriophage PHI29 Gene Product 12 C- Terminal Fragment in Complex with Atp, PDB code: 3gqk was solved by Y.Xiang, M.G.Rossmann, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	26.95 / 2.50
Space group	P 21 3
Cell size a, b, c (Å), α, β, γ (°)	85.211, 85.211, 85.211, 90.00, 90.00, 90.00
R / Rfree (%)	26.4 / 33.4

The binding sites of Magnesium atom in the Crystal Structure of the Bacteriophage PHI29 Gene Product 12 C- Terminal Fragment in Complex with Atp (pdb code 3gqk). 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 the Bacteriophage PHI29 Gene Product 12 C- Terminal Fragment in Complex with Atp, PDB code: 3gqk:

Magnesium binding site 1 out of 1 in the Crystal Structure of the Bacteriophage PHI29 Gene Product 12 C- Terminal Fragment in Complex with Atp


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 the Bacteriophage PHI29 Gene Product 12 C- Terminal Fragment in Complex with Atp within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg855 b:74.4 occ:1.00 O1B A:ATP1 2.3 66.4 1.0 O2G A:ATP1 2.3 63.7 1.0 OE1 A:GLU698 3.1 48.5 1.0 O1G A:ATP1 3.2 59.5 1.0 PG A:ATP1 3.2 68.2 1.0 PB A:ATP1 3.5 70.3 1.0 O2A A:ATP1 3.6 80.0 1.0 O3B A:ATP1 3.8 71.0 1.0 CD A:GLU698 4.1 48.9 1.0 O3A A:ATP1 4.2 76.7 1.0 OE2 A:GLU698 4.3 52.5 1.0 PA A:ATP1 4.4 77.7 1.0 O3G A:ATP1 4.6 63.6 1.0 CZ2 A:TRP795 4.7 43.1 1.0 OE2 A:GLU794 4.7 42.4 1.0 NE1 A:TRP795 4.9 41.9 1.0 O2B A:ATP1 4.9 70.9 1.0 O1A A:ATP1 4.9 84.6 1.0

Y.Xiang, P.G.Leiman, L.Li, S.Grimes, D.L.Anderson, M.G.Rossmann. Crystallographic Insights Into the Autocatalytic Assembly Mechanism of A Bacteriophage Tail Spike. Mol.Cell V. 34 375 2009.
ISSN: ISSN 1097-2765
PubMed: 19450535
DOI: 10.1016/J.MOLCEL.2009.04.009