Magnesium in PDB 4kq5: Crystal Structure of Human Farnesyl Pyrophosphate Synthase Mutant (Y204A) Complexed with Mg and Zoledronate

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

The structure of Crystal Structure of Human Farnesyl Pyrophosphate Synthase Mutant (Y204A) Complexed with Mg and Zoledronate, PDB code: 4kq5 was solved by B.L.Barnett, M.K.Tsoumpra, J.R.C.Muniz, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	32.50 / 2.40
Space group	P 41 21 2
Cell size a, b, c (Å), α, β, γ (°)	111.650, 111.650, 67.940, 90.00, 90.00, 90.00
R / Rfree (%)	18.5 / 24.7

The binding sites of Magnesium atom in the Crystal Structure of Human Farnesyl Pyrophosphate Synthase Mutant (Y204A) Complexed with Mg and Zoledronate (pdb code 4kq5). 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 Mutant (Y204A) Complexed with Mg and Zoledronate, PDB code: 4kq5:
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 Mutant (Y204A) Complexed with Mg and Zoledronate


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 Mutant (Y204A) Complexed with Mg and Zoledronate within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg401 b:33.6 occ:1.00 O A:HOH584 1.9 24.1 1.0 OD2 A:ASP103 1.9 46.6 1.0 O A:HOH585 2.0 27.3 1.0 O17 A:ZOL404 2.0 39.0 1.0 OD2 A:ASP107 2.2 49.4 1.0 O12 A:ZOL404 2.2 36.9 1.0 CG A:ASP103 3.0 43.9 1.0 MG A:MG403 3.2 31.1 1.0 CG A:ASP107 3.2 42.5 1.0 P14 A:ZOL404 3.3 35.4 1.0 P9 A:ZOL404 3.4 35.9 1.0 OD1 A:ASP103 3.5 42.1 1.0 O A:HOH622 3.5 33.8 1.0 CB A:ASP107 3.7 41.2 1.0 C8 A:ZOL404 3.7 36.0 1.0 O16 A:ZOL404 4.0 33.2 1.0 O11 A:ZOL404 4.0 40.6 1.0 NH2 A:ARG112 4.0 37.8 1.0 C7 A:ZOL404 4.1 35.8 1.0 O A:HOH519 4.2 8.4 1.0 CB A:ASP103 4.3 39.6 1.0 O A:ASP103 4.3 41.7 1.0 OD1 A:ASP107 4.4 40.9 1.0 O A:HOH590 4.4 37.9 1.0 O15 A:ZOL404 4.4 32.2 1.0 OG A:SER109 4.5 55.3 1.0 C A:ASP103 4.6 42.4 1.0 O A:HOH591 4.6 32.2 1.0 OD1 A:ASP104 4.6 46.0 1.0 O A:HOH586 4.6 22.8 1.0 O10 A:ZOL404 4.6 32.9 1.0 O A:HOH502 4.7 29.4 1.0 MG A:MG402 4.9 22.4 1.0 O A:HOH503 5.0 38.4 1.0

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


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 Mutant (Y204A) Complexed with Mg and Zoledronate within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg402 b:22.4 occ:1.00 O A:HOH586 2.0 22.8 1.0 O11 A:ZOL404 2.1 40.6 1.0 O16 A:ZOL404 2.2 33.2 1.0 O A:HOH588 2.2 35.4 1.0 O A:HOH587 2.2 25.8 1.0 OD2 A:ASP243 2.2 46.5 1.0 CG A:ASP243 3.3 46.6 1.0 O A:HOH622 3.3 33.8 1.0 P9 A:ZOL404 3.4 35.9 1.0 P14 A:ZOL404 3.4 35.4 1.0 O13 A:ZOL404 3.7 35.9 1.0 OD1 A:ASP247 3.8 50.8 1.0 C8 A:ZOL404 3.8 36.0 1.0 OD1 A:ASP243 3.8 46.3 1.0 O A:HOH506 3.9 28.0 1.0 O A:HOH669 3.9 68.0 1.0 O A:ASP243 4.0 48.7 1.0 O12 A:ZOL404 4.2 36.9 1.0 OD2 A:ASP261 4.2 52.8 1.0 O17 A:ZOL404 4.2 39.0 1.0 OD1 A:ASP261 4.2 52.4 1.0 O A:HOH585 4.2 27.3 1.0 CG A:ASP247 4.4 52.5 1.0 NE2 A:GLN240 4.4 35.9 1.0 C A:ASP243 4.4 48.1 1.0 CB A:ASP247 4.4 44.2 1.0 OD1 A:ASP244 4.5 37.8 1.0 CB A:ASP243 4.5 44.0 1.0 O10 A:ZOL404 4.6 32.9 1.0 O15 A:ZOL404 4.6 32.2 1.0 CG A:ASP261 4.6 50.8 1.0 MG A:MG401 4.9 33.6 1.0 N A:ASP244 4.9 43.2 1.0 CE A:LYS257 5.0 35.0 1.0

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


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 Mutant (Y204A) Complexed with Mg and Zoledronate within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg403 b:31.1 occ:1.00 O A:HOH591 1.9 32.2 1.0 OD2 A:ASP107 2.0 49.4 1.0 OD1 A:ASP103 2.1 42.1 1.0 O A:HOH590 2.2 37.9 1.0 O12 A:ZOL404 2.2 36.9 1.0 O A:HOH589 2.3 29.3 1.0 CG A:ASP107 2.9 42.5 1.0 CG A:ASP103 2.9 43.9 1.0 OD1 A:ASP107 3.0 40.9 1.0 OD2 A:ASP103 3.2 46.6 1.0 MG A:MG401 3.2 33.6 1.0 P9 A:ZOL404 3.4 35.9 1.0 O10 A:ZOL404 3.6 32.9 1.0 OD2 A:ASP174 3.8 47.4 1.0 NZ A:LYS266 3.8 57.0 1.0 O A:HOH585 4.0 27.3 1.0 OE1 A:GLN171 4.1 42.5 1.0 CB A:ASP107 4.3 41.2 1.0 CB A:ASP103 4.3 39.6 1.0 NE2 A:GLN171 4.3 36.9 1.0 C19 A:ZOL404 4.3 38.9 1.0 CG A:ASP174 4.4 50.7 1.0 O11 A:ZOL404 4.5 40.6 1.0 O A:HOH506 4.5 28.0 1.0 OD1 A:ASP174 4.6 51.9 1.0 O A:ASP103 4.6 41.7 1.0 CD A:GLN171 4.7 49.5 1.0 C7 A:ZOL404 4.7 35.8 1.0 C8 A:ZOL404 4.7 36.0 1.0 O A:HOH584 4.7 24.1 1.0 O17 A:ZOL404 4.8 39.0 1.0 N15 A:ZOL404 4.8 37.9 1.0 CA A:ASP103 4.9 37.7 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 Human Farnesyl Pyrophosphate Synthase Mutant (Y204A) Complexed with Mg and Zoledronate To Be Published.