Magnesium in PDB 2qis: Crystal Structure of Human Farnesyl Pyrophosphate Synthase T210S Mutant Bound to Risedronate

All present enzymatic activity of Crystal Structure of Human Farnesyl Pyrophosphate Synthase T210S Mutant Bound to Risedronate:
2.5.1.10;

The structure of Crystal Structure of Human Farnesyl Pyrophosphate Synthase T210S Mutant Bound to Risedronate, PDB code: 2qis was solved by K.L.Kavanagh, J.E.Dunford, V.Hozjan, A.Evdokimov, O.Gileadi, F.Von Delft, J.Weigelt, C.H.Arrowsmith, M.Sundstrom, A.Edwards, U.Oppermann, Structural Genomics Consortium (Sgc), with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	30.92 / 1.80
Space group	P 41 21 2
Cell size a, b, c (Å), α, β, γ (°)	111.470, 111.470, 67.603, 90.00, 90.00, 90.00
R / Rfree (%)	17.8 / 20.6

The binding sites of Magnesium atom in the Crystal Structure of Human Farnesyl Pyrophosphate Synthase T210S Mutant Bound to Risedronate (pdb code 2qis). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 3 binding sites of Magnesium where determined in the Crystal Structure of Human Farnesyl Pyrophosphate Synthase T210S Mutant Bound to Risedronate, PDB code: 2qis:
Jump to Magnesium binding site number: 1; 2; 3;

Magnesium binding site 1 out of 3 in the Crystal Structure of Human Farnesyl Pyrophosphate Synthase T210S Mutant Bound to Risedronate


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 Human Farnesyl Pyrophosphate Synthase T210S Mutant Bound to Risedronate within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg907 b:24.4 occ:1.00 O12 A:RIS901 2.0 23.2 1.0 O A:HOH1011 2.1 21.8 1.0 OD2 A:ASP117 2.1 40.2 1.0 O A:HOH1003 2.1 21.2 1.0 O15 A:RIS901 2.1 23.3 1.0 OD2 A:ASP121 2.3 39.7 1.0 CG A:ASP117 3.1 41.7 1.0 MG A:MG909 3.2 20.9 1.0 P9 A:RIS901 3.3 24.1 1.0 P14 A:RIS901 3.3 25.8 1.0 CG A:ASP121 3.3 35.9 1.0 OD1 A:ASP117 3.4 37.2 1.0 C8 A:RIS901 3.6 24.8 1.0 CB A:ASP121 3.8 36.1 1.0 O A:HOH1038 3.9 27.1 1.0 C7 A:RIS901 3.9 23.3 1.0 O16 A:RIS901 3.9 25.9 1.0 O11 A:RIS901 4.1 25.7 1.0 NH2 A:ARG126 4.2 37.9 1.0 O A:HOH1006 4.3 25.9 1.0 O A:ASP117 4.4 37.9 1.0 O A:HOH1067 4.4 23.6 1.0 CB A:ASP117 4.4 36.8 1.0 OG A:SER123 4.4 41.0 1.0 OD1 A:ASP121 4.4 39.1 1.0 O10 A:RIS901 4.5 24.7 1.0 O A:HOH998 4.5 26.2 1.0 OD1 A:ASP118 4.5 39.8 1.0 O17 A:RIS901 4.6 24.7 1.0 C A:ASP117 4.6 36.6 1.0 O A:HOH1043 4.8 23.0 1.0 O A:HOH1061 4.8 30.6 1.0 MG A:MG908 4.9 27.4 1.0 O A:HOH1028 4.9 25.1 1.0 C2 A:RIS901 4.9 24.7 1.0

Magnesium binding site 2 out of 3 in the Crystal Structure of Human Farnesyl Pyrophosphate Synthase T210S Mutant Bound to Risedronate


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Crystal Structure of Human Farnesyl Pyrophosphate Synthase T210S Mutant Bound to Risedronate within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg908 b:27.4 occ:1.00 O11 A:RIS901 2.0 25.7 1.0 O16 A:RIS901 2.0 25.9 1.0 O A:HOH1039 2.1 22.8 1.0 OD2 A:ASP257 2.1 40.1 1.0 O A:HOH1040 2.2 26.6 1.0 O A:HOH1067 2.2 23.6 1.0 CG A:ASP257 3.1 40.5 1.0 P9 A:RIS901 3.3 24.1 1.0 P14 A:RIS901 3.3 25.8 1.0 C8 A:RIS901 3.6 24.8 1.0 O13 A:RIS901 3.6 23.9 1.0 OD1 A:ASP257 3.6 42.7 1.0 O A:HOH1004 4.0 25.3 1.0 O12 A:RIS901 4.1 23.2 1.0 OD1 A:ASP261 4.1 45.8 1.0 O A:HOH919 4.1 39.0 1.0 O A:ASP257 4.2 37.5 1.0 O A:HOH1003 4.2 21.2 1.0 O15 A:RIS901 4.2 23.3 1.0 OD1 A:ASP275 4.3 42.0 1.0 NE2 A:GLN254 4.3 40.6 1.0 O10 A:RIS901 4.3 24.7 1.0 CB A:ASP257 4.4 40.8 1.0 OD2 A:ASP275 4.4 40.5 1.0 O17 A:RIS901 4.4 24.7 1.0 C A:ASP257 4.5 38.4 1.0 OD1 A:ASP258 4.5 37.1 1.0 NZ A:LYS271 4.6 50.0 1.0 CB A:ASP261 4.7 40.7 1.0 CG A:ASP261 4.7 44.3 1.0 O A:HOH1038 4.7 27.1 1.0 CG A:ASP275 4.8 40.1 1.0 CE A:LYS271 4.9 49.8 1.0 N A:ASP258 4.9 37.3 1.0 MG A:MG907 4.9 24.4 1.0

Magnesium binding site 3 out of 3 in the Crystal Structure of Human Farnesyl Pyrophosphate Synthase T210S Mutant Bound to Risedronate


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 3 of Crystal Structure of Human Farnesyl Pyrophosphate Synthase T210S Mutant Bound to Risedronate within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg909 b:20.9 occ:1.00 O A:HOH1028 2.1 25.1 1.0 OD1 A:ASP117 2.1 37.2 1.0 O A:HOH1043 2.1 23.0 1.0 O15 A:RIS901 2.1 23.3 1.0 OD2 A:ASP121 2.2 39.7 1.0 O A:HOH1006 2.2 25.9 1.0 CG A:ASP117 3.1 41.7 1.0 CG A:ASP121 3.1 35.9 1.0 MG A:MG907 3.2 24.4 1.0 OD1 A:ASP121 3.3 39.1 1.0 P14 A:RIS901 3.4 25.8 1.0 OD2 A:ASP117 3.4 40.2 1.0 O17 A:RIS901 3.4 24.7 1.0 OD1 A:ASP188 4.0 49.4 1.0 NE2 A:GLN185 4.2 40.0 1.0 OE1 A:GLN185 4.2 46.4 1.0 O A:HOH1003 4.3 21.2 1.0 OD2 A:ASP188 4.3 46.0 1.0 O16 A:RIS901 4.4 25.9 1.0 O A:HOH1004 4.4 25.3 1.0 CB A:ASP117 4.4 36.8 1.0 CG A:ASP188 4.4 45.9 1.0 CB A:ASP121 4.5 36.1 1.0 NZ A:LYS280 4.5 55.2 1.0 C1 A:RIS901 4.6 29.7 1.0 C8 A:RIS901 4.6 24.8 1.0 CD A:GLN185 4.6 45.2 1.0 C7 A:RIS901 4.7 23.3 1.0 CE A:LYS280 4.7 45.0 1.0 NZ A:LYS214 4.7 39.6 1.0 C2 A:RIS901 4.7 24.7 1.0 O A:ASP117 4.8 37.9 1.0 O12 A:RIS901 4.8 23.2 1.0 O A:HOH1011 4.9 21.8 1.0

K.L.Kavanagh, J.E.Dunford, V.Hozjan, A.Evdokimov, O.Gileadi, F.Von Delft, J.Weigelt, C.H.Arrowsmith, M.Sundstrom, A.Edwards, U.Oppermann. Crystal Structure of Human Farnesyl Pyrophosphate Synthase T210S Mutant Bound to Risedronate. To Be Published.