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Magnesium in PDB 4ogu: The Effects of Lysine 200 and Phenylalanine 239 Farnesyl Pyrophosphate Synthase (Fpps) Mutations on the Catalytic Activity, Crystal Structure and Inhibition By Nitrogen Containing Bisphosphonates

Enzymatic activity of The Effects of Lysine 200 and Phenylalanine 239 Farnesyl Pyrophosphate Synthase (Fpps) Mutations on the Catalytic Activity, Crystal Structure and Inhibition By Nitrogen Containing Bisphosphonates

All present enzymatic activity of The Effects of Lysine 200 and Phenylalanine 239 Farnesyl Pyrophosphate Synthase (Fpps) Mutations on the Catalytic Activity, Crystal Structure and Inhibition By Nitrogen Containing Bisphosphonates:
2.5.1.1; 2.5.1.10;

Protein crystallography data

The structure of The Effects of Lysine 200 and Phenylalanine 239 Farnesyl Pyrophosphate Synthase (Fpps) Mutations on the Catalytic Activity, Crystal Structure and Inhibition By Nitrogen Containing Bisphosphonates, PDB code: 4ogu was solved by M.K.Tsoumpra, B.L.Barnett, J.R.C.Muniz, R.L.Walter, F.H.Ebetino, F.Vondelft, R.G.G.Russell, U.Oppermann, J.E.Dunford, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 24.40 / 2.10
Space group P 41 21 2
Cell size a, b, c (Å), α, β, γ (°) 111.210, 111.210, 67.270, 90.00, 90.00, 90.00
R / Rfree (%) 19.7 / 23.1

Magnesium Binding Sites:

The binding sites of Magnesium atom in the The Effects of Lysine 200 and Phenylalanine 239 Farnesyl Pyrophosphate Synthase (Fpps) Mutations on the Catalytic Activity, Crystal Structure and Inhibition By Nitrogen Containing Bisphosphonates (pdb code 4ogu). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 3 binding sites of Magnesium where determined in the The Effects of Lysine 200 and Phenylalanine 239 Farnesyl Pyrophosphate Synthase (Fpps) Mutations on the Catalytic Activity, Crystal Structure and Inhibition By Nitrogen Containing Bisphosphonates, PDB code: 4ogu:
Jump to Magnesium binding site number: 1; 2; 3;

Magnesium binding site 1 out of 3 in 4ogu

Go back to Magnesium Binding Sites List in 4ogu
Magnesium binding site 1 out of 3 in the The Effects of Lysine 200 and Phenylalanine 239 Farnesyl Pyrophosphate Synthase (Fpps) Mutations on the Catalytic Activity, Crystal Structure and Inhibition By Nitrogen Containing Bisphosphonates


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of The Effects of Lysine 200 and Phenylalanine 239 Farnesyl Pyrophosphate Synthase (Fpps) Mutations on the Catalytic Activity, Crystal Structure and Inhibition By Nitrogen Containing Bisphosphonates within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg401

b:34.1
occ:1.00
 O A:HOH594 1.9 22.2 1.0
O10 A:210405 2.1 44.1 1.0
O2 A:210405 2.1 45.8 1.0
OD2 A:ASP103 2.1 46.2 1.0
OD2 A:ASP107 2.1 57.6 1.0
O A:HOH593 2.2 25.4 1.0
MG A:MG403 2.9 14.9 1.0
O A:HOH504 2.9 47.6 1.0
CG A:ASP103 3.0 47.8 1.0
OD1 A:ASP103 3.3 45.4 1.0
CG A:ASP107 3.3 54.9 1.0
P8 A:210405 3.3 48.1 1.0
P1 A:210405 3.3 44.4 1.0
C7 A:210405 3.6 47.3 1.0
C16 A:210405 3.8 46.3 1.0
CB A:ASP107 3.8 47.3 1.0
O9 A:210405 4.0 48.7 1.0
O A:HOH601 4.0 33.9 1.0
O5 A:210405 4.1 40.1 1.0
O A:HOH592 4.1 43.4 1.0
NH2 A:ARG112 4.2 39.1 1.0
O A:HOH588 4.2 27.1 1.0
OD1 A:ASP107 4.3 53.2 1.0
O A:HOH595 4.4 42.4 1.0
O A:ASP103 4.4 46.2 1.0
O3 A:210405 4.4 40.1 1.0
CB A:ASP103 4.4 43.1 1.0
O A:HOH586 4.5 31.7 1.0
O12 A:210405 4.5 43.9 1.0
O A:HOH587 4.6 40.3 1.0
OG A:SER109 4.7 61.8 1.0
OD1 A:ASP104 4.7 41.6 1.0
C A:ASP103 4.8 45.6 1.0
O A:HOH569 4.9 48.9 1.0
C19 A:210405 5.0 47.9 1.0
O14 A:210405 5.0 48.8 1.0

Magnesium binding site 2 out of 3 in 4ogu

Go back to Magnesium Binding Sites List in 4ogu
Magnesium binding site 2 out of 3 in the The Effects of Lysine 200 and Phenylalanine 239 Farnesyl Pyrophosphate Synthase (Fpps) Mutations on the Catalytic Activity, Crystal Structure and Inhibition By Nitrogen Containing Bisphosphonates


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of The Effects of Lysine 200 and Phenylalanine 239 Farnesyl Pyrophosphate Synthase (Fpps) Mutations on the Catalytic Activity, Crystal Structure and Inhibition By Nitrogen Containing Bisphosphonates within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg402

b:35.7
occ:1.00
 O9 A:210405 2.0 48.7 1.0
OD2 A:ASP243 2.1 53.0 1.0
O A:HOH590 2.1 37.1 1.0
O5 A:210405 2.1 40.1 1.0
O A:HOH591 2.3 39.6 1.0
O A:HOH592 2.4 43.4 1.0
CG A:ASP243 3.1 53.2 1.0
P8 A:210405 3.3 48.1 1.0
P1 A:210405 3.4 44.4 1.0
OD1 A:ASP243 3.6 52.3 1.0
O14 A:210405 3.6 48.8 1.0
C7 A:210405 3.7 47.3 1.0
O A:HOH509 3.9 73.1 1.0
NE2 A:GLN240 4.0 56.2 1.0
O A:HOH504 4.0 47.6 1.0
OD2 A:ASP261 4.2 51.9 1.0
O A:HOH589 4.2 33.2 1.0
OD1 A:ASP261 4.2 62.1 1.0
OD1 A:ASP244 4.2 50.8 1.0
O2 A:210405 4.2 45.8 1.0
OD1 A:ASP247 4.3 57.5 1.0
O A:ASP243 4.3 53.2 1.0
O10 A:210405 4.3 44.1 1.0
O12 A:210405 4.3 43.9 1.0
CB A:ASP243 4.4 49.1 1.0
C A:ASP243 4.5 52.4 1.0
O3 A:210405 4.5 40.1 1.0
O A:HOH594 4.5 22.2 1.0
CG A:ASP261 4.6 59.1 1.0
CB A:ASP247 4.7 47.9 1.0
N A:ASP244 4.8 48.0 1.0
CG A:ASP247 4.8 56.9 1.0
CE A:LYS257 4.9 64.8 1.0
O A:HOH601 4.9 33.9 1.0
NZ A:LYS257 4.9 62.1 1.0
CA A:ASP244 5.0 47.1 1.0

Magnesium binding site 3 out of 3 in 4ogu

Go back to Magnesium Binding Sites List in 4ogu
Magnesium binding site 3 out of 3 in the The Effects of Lysine 200 and Phenylalanine 239 Farnesyl Pyrophosphate Synthase (Fpps) Mutations on the Catalytic Activity, Crystal Structure and Inhibition By Nitrogen Containing Bisphosphonates


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 3 of The Effects of Lysine 200 and Phenylalanine 239 Farnesyl Pyrophosphate Synthase (Fpps) Mutations on the Catalytic Activity, Crystal Structure and Inhibition By Nitrogen Containing Bisphosphonates within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg403

b:14.9
occ:1.00
 OD1 A:ASP103 1.9 45.4 1.0
O A:HOH587 2.0 40.3 1.0
O10 A:210405 2.0 44.1 1.0
O A:HOH586 2.1 31.7 1.0
OD2 A:ASP107 2.1 57.6 1.0
O A:HOH588 2.2 27.1 1.0
MG A:MG401 2.9 34.1 1.0
CG A:ASP103 2.9 47.8 1.0
CG A:ASP107 3.0 54.9 1.0
O A:HOH504 3.1 47.6 1.0
OD2 A:ASP103 3.2 46.2 1.0
OD1 A:ASP107 3.2 53.2 1.0
P8 A:210405 3.4 48.1 1.0
O12 A:210405 3.7 43.9 1.0
OD2 A:ASP174 3.8 58.6 1.0
OE1 A:GLN171 4.1 80.7 1.0
O A:HOH594 4.1 22.2 1.0
CB A:ASP103 4.3 43.1 1.0
O9 A:210405 4.4 48.7 1.0
C16 A:210405 4.4 46.3 1.0
CB A:ASP107 4.4 47.3 1.0
NZ A:LYS266 4.4 58.9 1.0
O A:HOH589 4.5 33.2 1.0
C7 A:210405 4.6 47.3 1.0
CE A:LYS266 4.6 40.2 1.0
O2 A:210405 4.7 45.8 1.0
CG A:ASP174 4.7 54.1 1.0
O A:ASP103 4.7 46.2 1.0
O A:HOH593 4.7 25.4 1.0
NE2 A:GLN171 4.7 82.4 1.0
C19 A:210405 4.8 47.9 1.0
CD A:GLN171 4.8 86.2 1.0
NZ A:LYS200 4.9 51.1 1.0

Reference:

M.K.Tsoumpra, B.L.Barnett, J.R.C.Muniz, R.L.Walter, F.H.Ebetino, F.Von Delft, R.G.G.Russell, U.Oppermann, J.E.Dunford. The Effects of Lysine 200 and Phenylalanine 239 Farnesyl Pyrophosphate Synthase (Fpps) Mutations on the Catalytic Activity, Crystal Structure and Inhibition By Nitrogen Containing Bisphosphonates To Be Published.
Page generated: Mon Aug 11 21:30:26 2025

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