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Magnesium in PDB 4q23: The Role of Threonine 201 and Tyrosine 204 in the Human Farnesyl Pyrophosphate Synthase Catalytic Mechanism and the Mode of Inhibition By the Nitrogen-Containing Bisphosphonates

Enzymatic activity of The Role of Threonine 201 and Tyrosine 204 in the Human Farnesyl Pyrophosphate Synthase Catalytic Mechanism and the Mode of Inhibition By the Nitrogen-Containing Bisphosphonates

All present enzymatic activity of The Role of Threonine 201 and Tyrosine 204 in the Human Farnesyl Pyrophosphate Synthase Catalytic Mechanism and the Mode of Inhibition By the Nitrogen-Containing Bisphosphonates:
2.5.1.1; 2.5.1.10;

Protein crystallography data

The structure of The Role of Threonine 201 and Tyrosine 204 in the Human Farnesyl Pyrophosphate Synthase Catalytic Mechanism and the Mode of Inhibition By the Nitrogen-Containing Bisphosphonates, PDB code: 4q23 was solved by M.K.Tsoumpra, J.R.C.Muniz, B.L.Barnett, A.A.Kwaasi, E.S.Pilka, K.L.Kavanagh, A.Evdokimov, R.L.Walter, F.H.Ebetino, F.Von Delft, U.Oppermann, R.G.G.Russell, J.E.Dunford, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 25.02 / 1.98
Space group P 41 21 2
Cell size a, b, c (Å), α, β, γ (°) 111.360, 111.360, 67.600, 90.00, 90.00, 90.00
R / Rfree (%) 19.2 / 22.3

Magnesium Binding Sites:

The binding sites of Magnesium atom in the The Role of Threonine 201 and Tyrosine 204 in the Human Farnesyl Pyrophosphate Synthase Catalytic Mechanism and the Mode of Inhibition By the Nitrogen-Containing Bisphosphonates (pdb code 4q23). 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 Role of Threonine 201 and Tyrosine 204 in the Human Farnesyl Pyrophosphate Synthase Catalytic Mechanism and the Mode of Inhibition By the Nitrogen-Containing Bisphosphonates, PDB code: 4q23:
Jump to Magnesium binding site number: 1; 2; 3;

Magnesium binding site 1 out of 3 in 4q23

Go back to Magnesium Binding Sites List in 4q23
Magnesium binding site 1 out of 3 in the The Role of Threonine 201 and Tyrosine 204 in the Human Farnesyl Pyrophosphate Synthase Catalytic Mechanism and the Mode of Inhibition By the 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 Role of Threonine 201 and Tyrosine 204 in the Human Farnesyl Pyrophosphate Synthase Catalytic Mechanism and the Mode of Inhibition By the Nitrogen-Containing Bisphosphonates within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg902

b:29.2
occ:1.00
 OD2 A:ASP103 2.0 33.0 1.0
O A:HOH1090 2.1 33.0 1.0
O15 A:RIS901 2.1 33.6 1.0
O A:HOH1092 2.1 27.3 1.0
O12 A:RIS901 2.2 28.3 1.0
OD2 A:ASP107 2.3 31.3 1.0
CG A:ASP103 3.0 34.4 1.0
MG A:MG904 3.2 27.7 1.0
CG A:ASP107 3.3 33.9 1.0
P9 A:RIS901 3.3 32.9 1.0
P14 A:RIS901 3.4 34.2 1.0
OD1 A:ASP103 3.4 32.9 1.0
CB A:ASP107 3.7 31.2 1.0
C8 A:RIS901 3.7 35.1 1.0
O A:HOH1003 3.9 27.3 1.0
O16 A:RIS901 3.9 33.7 1.0
C7 A:RIS901 3.9 38.3 1.0
O11 A:RIS901 4.0 30.4 1.0
O10 A:RIS901 4.2 22.4 1.0
NH2 A:ARG112 4.3 29.8 1.0
O A:HOH1094 4.3 27.5 1.0
O A:ASP103 4.3 30.6 1.0
CB A:ASP103 4.4 30.1 1.0
O A:HOH1002 4.4 32.3 1.0
OG A:SER109 4.4 38.5 1.0
OD1 A:ASP107 4.4 34.1 1.0
O A:HOH1089 4.4 34.8 1.0
O17 A:RIS901 4.5 31.8 1.0
OD1 A:ASP104 4.6 31.5 1.0
C A:ASP103 4.6 31.6 1.0
O A:HOH1096 4.7 32.0 1.0
O A:HOH1005 4.8 37.7 1.0
MG A:MG903 4.8 26.4 1.0
C2 A:RIS901 5.0 42.4 1.0

Magnesium binding site 2 out of 3 in 4q23

Go back to Magnesium Binding Sites List in 4q23
Magnesium binding site 2 out of 3 in the The Role of Threonine 201 and Tyrosine 204 in the Human Farnesyl Pyrophosphate Synthase Catalytic Mechanism and the Mode of Inhibition By the 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 Role of Threonine 201 and Tyrosine 204 in the Human Farnesyl Pyrophosphate Synthase Catalytic Mechanism and the Mode of Inhibition By the Nitrogen-Containing Bisphosphonates within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg903

b:26.4
occ:1.00
 O11 A:RIS901 1.9 30.4 1.0
O16 A:RIS901 2.0 33.7 1.0
O A:HOH1089 2.0 34.8 1.0
OD2 A:ASP243 2.1 38.6 1.0
O A:HOH1088 2.1 32.4 1.0
O A:HOH1093 2.1 23.0 1.0
P9 A:RIS901 2.8 32.9 1.0
CG A:ASP243 3.1 39.3 1.0
P14 A:RIS901 3.3 34.2 1.0
O13 A:RIS901 3.5 35.0 1.0
OD1 A:ASP243 3.5 37.4 1.0
C8 A:RIS901 3.5 35.1 1.0
O12 A:RIS901 3.9 28.3 1.0
OD1 A:ASP247 3.9 44.0 1.0
O A:HOH1001 4.1 31.7 1.0
O A:HOH1070 4.2 46.1 1.0
O A:HOH1090 4.2 33.0 1.0
O10 A:RIS901 4.2 22.4 1.0
O15 A:RIS901 4.2 33.6 1.0
O A:ASP243 4.2 39.8 1.0
O17 A:RIS901 4.2 31.8 1.0
NE2 A:GLN240 4.4 39.2 1.0
OD1 A:ASP261 4.4 41.0 1.0
CB A:ASP243 4.4 37.4 1.0
NZ A:LYS257 4.4 49.0 1.0
OD2 A:ASP261 4.5 41.5 1.0
C A:ASP243 4.5 40.1 1.0
OD1 A:ASP244 4.6 35.7 1.0
CE A:LYS257 4.6 39.0 1.0
O A:HOH1003 4.7 27.3 1.0
CG A:ASP247 4.7 45.7 1.0
MG A:MG902 4.8 29.2 1.0
CB A:ASP247 4.8 38.5 1.0
CG A:ASP261 4.9 40.0 1.0
C7 A:RIS901 4.9 38.3 1.0

Magnesium binding site 3 out of 3 in 4q23

Go back to Magnesium Binding Sites List in 4q23
Magnesium binding site 3 out of 3 in the The Role of Threonine 201 and Tyrosine 204 in the Human Farnesyl Pyrophosphate Synthase Catalytic Mechanism and the Mode of Inhibition By the 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 Role of Threonine 201 and Tyrosine 204 in the Human Farnesyl Pyrophosphate Synthase Catalytic Mechanism and the Mode of Inhibition By the Nitrogen-Containing Bisphosphonates within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg904

b:27.7
occ:1.00
 OD1 A:ASP103 1.9 32.9 1.0
O A:HOH1094 2.0 27.5 1.0
OD2 A:ASP107 2.0 31.3 1.0
O A:HOH1096 2.1 32.0 1.0
O15 A:RIS901 2.1 33.6 1.0
O A:HOH1095 2.2 27.5 1.0
CG A:ASP103 2.9 34.4 1.0
CG A:ASP107 3.0 33.9 1.0
MG A:MG902 3.2 29.2 1.0
OD1 A:ASP107 3.2 34.1 1.0
OD2 A:ASP103 3.2 33.0 1.0
P14 A:RIS901 3.3 34.2 1.0
O17 A:RIS901 3.4 31.8 1.0
OD1 A:ASP174 3.9 40.4 1.0
OD2 A:ASP174 4.1 41.3 1.0
O A:HOH1090 4.2 33.0 1.0
NE2 A:GLN171 4.2 35.9 1.0
OE1 A:GLN171 4.3 39.7 1.0
CB A:ASP103 4.3 30.1 1.0
O16 A:RIS901 4.3 33.7 1.0
CG A:ASP174 4.3 43.3 1.0
CB A:ASP107 4.4 31.2 1.0
O A:HOH1001 4.4 31.7 1.0
NZ A:LYS266 4.5 48.4 1.0
C8 A:RIS901 4.6 35.1 1.0
CD A:GLN171 4.7 53.4 1.0
NZ A:LYS200 4.7 42.5 1.0
C7 A:RIS901 4.7 38.3 1.0
C1 A:RIS901 4.8 42.9 1.0
C2 A:RIS901 4.8 42.4 1.0
O A:ASP103 4.8 30.6 1.0
CE A:LYS266 4.8 35.5 1.0
O A:HOH1092 4.9 27.3 1.0
O12 A:RIS901 4.9 28.3 1.0
O A:HOH1002 5.0 32.3 1.0

Reference:

M.K.Tsoumpra, J.R.C.Muniz, B.L.Barnett, A.A.Kwaasi, E.S.Pilka, K.L.Kavanagh, A.Evdokimov, R.L.Walter, F.H.Ebetino, F.Von Delft, U.Oppermann, R.G.G.Russell, J.E.Dunford. The Role of Threonine 201 and Tyrosine 204 in the Human Farnesyl Pyrophosphate Synthase Catalytic Mechanism and the Mode of Inhibition By the Nitrogen-Containing Bisphosphonates To Be Published.
Page generated: Tue Aug 20 01:43:45 2024

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