Magnesium in PDB 1ubx: Structure of Farnesyl Pyrophosphate Synthetase

All present enzymatic activity of Structure of Farnesyl Pyrophosphate Synthetase:
2.5.1.1;

The structure of Structure of Farnesyl Pyrophosphate Synthetase, PDB code: 1ubx was solved by L.C.Tarshis, P.Proteau, C.D.Poulter, J.C.Sacchettini, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	N/A / 2.50
Space group	I 41 2 2
Cell size a, b, c (Å), α, β, γ (°)	88.700, 88.700, 276.300, 90.00, 90.00, 90.00
R / Rfree (%)	20.1 / n/a

The binding sites of Magnesium atom in the Structure of Farnesyl Pyrophosphate Synthetase (pdb code 1ubx). 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 Structure of Farnesyl Pyrophosphate Synthetase, PDB code: 1ubx:

Magnesium binding site 1 out of 1 in the Structure of Farnesyl Pyrophosphate Synthetase


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Structure of Farnesyl Pyrophosphate Synthetase within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg402 b:63.6 occ:1.00 OD2 A:ASP117 2.7 41.1 1.0 OD2 A:ASP121 3.0 55.0 1.0 CB A:ASP121 3.2 34.5 1.0 OG A:SER123 3.3 39.8 1.0 O2B A:FPP401 3.3 87.5 1.0 O3A A:FPP401 3.4 74.7 1.0 CG A:ASP117 3.4 27.1 1.0 CG A:ASP121 3.6 49.3 1.0 OD1 A:ASP118 3.7 34.0 1.0 OD1 A:ASP117 3.9 31.6 1.0 PB A:FPP401 4.1 77.5 1.0 O A:ASP117 4.1 17.4 1.0 C A:ASP117 4.3 18.6 1.0 O1A A:FPP401 4.4 78.7 1.0 CB A:ASP117 4.4 25.6 1.0 N A:ASP118 4.5 28.8 1.0 CA A:ASP118 4.5 28.9 1.0 CB A:SER123 4.6 33.3 1.0 CA A:ASP121 4.7 25.5 1.0 PA A:FPP401 4.7 75.5 1.0 NH1 A:ARG126 4.7 35.4 1.0 OD1 A:ASP121 4.8 61.1 1.0 CG A:ASP118 4.9 30.4 1.0 CA A:ASP117 5.0 17.1 1.0

L.C.Tarshis, P.J.Proteau, B.A.Kellogg, J.C.Sacchettini, C.D.Poulter. Regulation of Product Chain Length By Isoprenyl Diphosphate Synthases. Proc.Natl.Acad.Sci.Usa V. 93 15018 1996.
ISSN: ISSN 0027-8424
PubMed: 8986756
DOI: 10.1073/PNAS.93.26.15018