Magnesium in PDB 4kpj: Crystal Structure of Farnesyl Pyrophosphate Synthase (Y204A) Mutant Complexed with Mg, Pamidronate

All present enzymatic activity of Crystal Structure of Farnesyl Pyrophosphate Synthase (Y204A) Mutant Complexed with Mg, Pamidronate:
2.5.1.1; 2.5.1.10;

The structure of Crystal Structure of Farnesyl Pyrophosphate Synthase (Y204A) Mutant Complexed with Mg, Pamidronate, PDB code: 4kpj was solved by B.L.Barnett, M.K.Tsoumpra, J.R.C.Muniz, R.L.Walter, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	50.84 / 1.95
Space group	P 41 21 2
Cell size a, b, c (Å), α, β, γ (°)	111.310, 111.310, 66.600, 90.00, 90.00, 90.00
R / Rfree (%)	17.2 / 21.5

The binding sites of Magnesium atom in the Crystal Structure of Farnesyl Pyrophosphate Synthase (Y204A) Mutant Complexed with Mg, Pamidronate (pdb code 4kpj). 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 Farnesyl Pyrophosphate Synthase (Y204A) Mutant Complexed with Mg, Pamidronate, PDB code: 4kpj:
Jump to Magnesium binding site number: 1; 2; 3;

Magnesium binding site 1 out of 3 in the Crystal Structure of Farnesyl Pyrophosphate Synthase (Y204A) Mutant Complexed with Mg, Pamidronate


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 Farnesyl Pyrophosphate Synthase (Y204A) Mutant Complexed with Mg, Pamidronate within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg902 b:19.5 occ:1.00 O A:HOH1005 2.0 16.8 1.0 O A:HOH1004 2.1 18.9 1.0 O2 A:210901 2.1 19.6 1.0 OD2 A:ASP103 2.1 17.3 1.0 O10 A:210901 2.1 19.0 1.0 OD2 A:ASP107 2.2 24.6 1.0 CG A:ASP103 3.1 20.1 1.0 MG A:MG904 3.2 8.4 1.0 CG A:ASP107 3.3 20.7 1.0 P1 A:210901 3.3 20.2 1.0 P8 A:210901 3.3 18.6 1.0 OD1 A:ASP103 3.4 17.2 1.0 C7 A:210901 3.7 20.4 1.0 CB A:ASP107 3.7 16.6 1.0 O A:HOH1015 3.9 15.1 1.0 C16 A:210901 3.9 22.5 1.0 O9 A:210901 4.0 22.4 1.0 O5 A:210901 4.1 20.9 1.0 NH2 A:ARG112 4.2 20.3 1.0 O A:HOH1002 4.2 17.2 1.0 O A:HOH1008 4.3 17.1 1.0 O A:ASP103 4.3 18.9 1.0 OD1 A:ASP107 4.4 19.0 1.0 CB A:ASP103 4.4 15.4 1.0 O A:HOH1013 4.4 23.4 1.0 O3 A:210901 4.4 19.5 1.0 OG A:SER109 4.5 23.7 1.0 O12 A:210901 4.6 19.0 1.0 OD1 A:ASP104 4.6 18.9 1.0 C A:ASP103 4.6 19.6 1.0 O A:HOH1001 4.8 18.2 1.0 O A:HOH1014 4.8 23.1 1.0 MG A:MG903 4.8 19.0 1.0 O A:HOH1003 5.0 17.5 1.0

Magnesium binding site 2 out of 3 in the Crystal Structure of Farnesyl Pyrophosphate Synthase (Y204A) Mutant Complexed with Mg, Pamidronate


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 Farnesyl Pyrophosphate Synthase (Y204A) Mutant Complexed with Mg, Pamidronate within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg903 b:19.0 occ:1.00 O5 A:210901 1.9 20.9 1.0 O9 A:210901 2.0 22.4 1.0 O A:HOH1006 2.1 17.9 1.0 O A:HOH1008 2.1 17.1 1.0 OD2 A:ASP243 2.1 19.3 1.0 O A:HOH1007 2.2 21.5 1.0 CG A:ASP243 3.2 22.0 1.0 P1 A:210901 3.2 20.2 1.0 P8 A:210901 3.3 18.6 1.0 O14 A:210901 3.5 19.4 1.0 C7 A:210901 3.5 20.4 1.0 OD1 A:ASP243 3.6 21.8 1.0 O A:HOH1009 3.9 23.6 1.0 OD1 A:ASP247 4.0 27.4 1.0 O2 A:210901 4.0 19.6 1.0 O A:ASP243 4.2 21.0 1.0 O10 A:210901 4.2 19.0 1.0 NE2 A:GLN240 4.2 22.3 1.0 O A:HOH1170 4.2 43.1 1.0 O A:HOH1005 4.2 16.8 1.0 OD1 A:ASP261 4.3 26.1 1.0 OD2 A:ASP261 4.3 23.1 1.0 O12 A:210901 4.3 19.0 1.0 O3 A:210901 4.4 19.5 1.0 CB A:ASP243 4.4 21.4 1.0 OD1 A:ASP244 4.4 22.1 1.0 C A:ASP243 4.5 22.6 1.0 CG A:ASP247 4.6 26.5 1.0 CB A:ASP247 4.7 21.4 1.0 CG A:ASP261 4.7 25.6 1.0 O A:HOH1015 4.8 15.1 1.0 NZ A:LYS257 4.8 42.1 1.0 MG A:MG902 4.8 19.5 1.0 N A:ASP244 4.9 19.8 1.0 CE A:LYS257 4.9 26.4 1.0

Magnesium binding site 3 out of 3 in the Crystal Structure of Farnesyl Pyrophosphate Synthase (Y204A) Mutant Complexed with Mg, Pamidronate


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 Farnesyl Pyrophosphate Synthase (Y204A) Mutant Complexed with Mg, Pamidronate within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg904 b:8.4 occ:1.00 OD1 A:ASP103 2.0 17.2 1.0 O A:HOH1002 2.0 17.2 1.0 O A:HOH1001 2.0 18.2 1.0 O10 A:210901 2.0 19.0 1.0 O A:HOH1003 2.1 17.5 1.0 OD2 A:ASP107 2.2 24.6 1.0 CG A:ASP103 3.0 20.1 1.0 CG A:ASP107 3.0 20.7 1.0 MG A:MG902 3.2 19.5 1.0 OD1 A:ASP107 3.2 19.0 1.0 P8 A:210901 3.3 18.6 1.0 OD2 A:ASP103 3.3 17.3 1.0 O12 A:210901 3.4 19.0 1.0 OD1 A:ASP174 4.0 30.7 1.0 NE2 A:GLN171 4.1 24.4 1.0 NZ A:LYS266 4.2 28.0 1.0 O A:HOH1005 4.2 16.8 1.0 OE1 A:GLN171 4.2 27.3 1.0 O9 A:210901 4.3 22.4 1.0 CB A:ASP103 4.3 15.4 1.0 O A:HOH1009 4.4 23.6 1.0 CB A:ASP107 4.5 16.6 1.0 CG A:ASP174 4.5 28.2 1.0 OD2 A:ASP174 4.5 28.4 1.0 C16 A:210901 4.5 22.5 1.0 C7 A:210901 4.6 20.4 1.0 CD A:GLN171 4.6 36.1 1.0 C19 A:210901 4.7 23.4 1.0 O A:ASP103 4.7 18.9 1.0 NZ A:LYS200 4.8 19.7 1.0 O2 A:210901 4.8 19.6 1.0 O A:HOH1004 4.8 18.9 1.0 CA A:ASP103 5.0 14.7 1.0

M.K.Tsoumpra, J.R.C.Muniz, B.L.Barnett, E.Pilka, A.Kwaasi, K.L.Kavanagh, A.G.Evdokimov, R.L.Walter, F.H.Ebetino, U.Oppermann, R.G.G.Russell, J.E.Dunford. Crystal Structure of Farnesyl Pyrophosphate Synthase (Y204A) Mutant Complexed with Mg, Pamidronate To Be Published.