Magnesium in PDB 2px3: Crystal Structure of Flhf Complexed with Gtp/Mg(2+)

The structure of Crystal Structure of Flhf Complexed with Gtp/Mg(2+), PDB code: 2px3 was solved by G.Bange, K.Wild, I.Sinning, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	49.76 / 3.20
Space group	P 41 21 2
Cell size a, b, c (Å), α, β, γ (°)	80.965, 80.965, 126.137, 90.00, 90.00, 90.00
R / Rfree (%)	25 / 31

The binding sites of Magnesium atom in the Crystal Structure of Flhf Complexed with Gtp/Mg(2+) (pdb code 2px3). 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 Flhf Complexed with Gtp/Mg(2+), PDB code: 2px3:

Magnesium binding site 1 out of 1 in the Crystal Structure of Flhf Complexed with Gtp/Mg(2+)


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 Flhf Complexed with Gtp/Mg(2+) within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg1000 b:28.3 occ:1.00 O A:HOH4 2.1 31.6 1.0 O A:HOH3 2.1 28.7 1.0 O A:HOH2 2.1 28.4 1.0 O2B A:GTP1 2.1 27.7 1.0 O2G A:GTP1 2.1 30.9 1.0 OG1 A:THR189 2.4 32.1 1.0 PG A:GTP1 3.4 33.8 1.0 PB A:GTP1 3.4 28.8 1.0 CB A:THR189 3.4 32.1 1.0 O3B A:GTP1 3.5 31.2 1.0 N A:THR189 3.8 22.4 1.0 OD2 A:ASP259 3.8 27.8 1.0 OD2 A:ASP213 4.1 24.3 1.0 CA A:THR189 4.2 22.4 1.0 O3G A:GTP1 4.3 33.1 1.0 OD1 A:ASP259 4.3 27.8 1.0 O1B A:GTP1 4.3 26.3 1.0 NZ A:LYS188 4.3 24.6 1.0 O1G A:GTP1 4.4 32.6 1.0 O2A A:GTP1 4.4 24.1 1.0 CG A:ASP259 4.5 27.8 1.0 O3A A:GTP1 4.5 26.4 1.0 CG2 A:THR189 4.6 32.1 1.0 CB A:LYS188 4.7 24.6 1.0 CE A:LYS188 4.7 24.6 1.0 O A:THR260 4.8 17.6 1.0 PA A:GTP1 4.8 25.7 1.0 O1A A:GTP1 4.9 27.3 1.0 C A:LYS188 4.9 20.7 1.0

G.Bange, G.Petzold, K.Wild, R.O.Parlitz, I.Sinning. The Crystal Structure of the Third Signal-Recognition Particle Gtpase Flhf Reveals A Homodimer with Bound Gtp. Proc.Natl.Acad.Sci.Usa V. 104 13621 2007.
ISSN: ISSN 0027-8424
PubMed: 17699634
DOI: 10.1073/PNAS.0702570104