Atomistry » Magnesium » PDB 4mpo-4naa » 4n9u
Atomistry »
  Magnesium »
    PDB 4mpo-4naa »
      4n9u »

Magnesium in PDB 4n9u: The Role of Lysine 200 in the Human Farnesyl Pyrophosphate Synthase Catalytic Mechanism and the Mode of Inhibition By the Nitrogen- Containing Bisphosphonates

Enzymatic activity of The Role of Lysine 200 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 Lysine 200 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 Lysine 200 in the Human Farnesyl Pyrophosphate Synthase Catalytic Mechanism and the Mode of Inhibition By the Nitrogen- Containing Bisphosphonates, PDB code: 4n9u was solved by M.K.Tsoumpra, J.R.C.Muniz, B.L.Barnett, E.Pilka, A.A.Kwaasi, K.L.Kavanagh, A.Evdokimov, R.L.Walter, F.H.Ebetino, 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) 49.69 / 2.11
Space group P 41 21 2
Cell size a, b, c (Å), α, β, γ (°) 111.110, 111.110, 69.580, 90.00, 90.00, 90.00
R / Rfree (%) 19.1 / 24

Magnesium Binding Sites:

The binding sites of Magnesium atom in the The Role of Lysine 200 in the Human Farnesyl Pyrophosphate Synthase Catalytic Mechanism and the Mode of Inhibition By the Nitrogen- Containing Bisphosphonates (pdb code 4n9u). 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 Lysine 200 in the Human Farnesyl Pyrophosphate Synthase Catalytic Mechanism and the Mode of Inhibition By the Nitrogen- Containing Bisphosphonates, PDB code: 4n9u:
Jump to Magnesium binding site number: 1; 2; 3;

Magnesium binding site 1 out of 3 in 4n9u

Go back to Magnesium Binding Sites List in 4n9u
Magnesium binding site 1 out of 3 in the The Role of Lysine 200 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 Lysine 200 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:Mg401

b:32.0
occ:1.00
 O A:HOH554 1.9 31.8 1.0
OD1 A:ASP103 2.0 46.6 1.0
O12 A:RIS404 2.0 48.7 1.0
OD2 A:ASP107 2.2 58.4 1.0
O A:HOH553 2.3 25.6 1.0
O15 A:RIS404 2.3 43.3 1.0
O A:HOH581 2.7 42.1 1.0
CG A:ASP103 3.0 47.0 1.0
MG A:MG403 3.2 34.8 1.0
CG A:ASP107 3.3 54.0 1.0
OD2 A:ASP103 3.4 47.6 1.0
P9 A:RIS404 3.4 46.1 1.0
P14 A:RIS404 3.5 50.9 1.0
O A:HOH582 3.6 31.2 1.0
CB A:ASP107 3.8 51.2 1.0
C8 A:RIS404 3.9 47.3 1.0
O A:HOH549 3.9 21.0 1.0
O A:HOH555 4.0 36.9 1.0
C7 A:RIS404 4.1 44.7 1.0
NH2 A:ARG112 4.1 45.9 1.0
O16 A:RIS404 4.2 48.6 1.0
O A:ASP103 4.3 48.2 1.0
O11 A:RIS404 4.3 45.1 1.0
CB A:ASP103 4.3 44.1 1.0
OD1 A:ASP107 4.4 50.3 1.0
O10 A:RIS404 4.4 41.0 1.0
OG A:SER109 4.4 52.6 1.0
O A:HOH583 4.5 44.7 1.0
C A:ASP103 4.6 46.9 1.0
O A:HOH557 4.6 41.2 1.0
OD1 A:ASP104 4.6 45.1 1.0
MG A:MG402 4.7 27.2 1.0
O A:HOH558 4.7 33.5 1.0
O17 A:RIS404 4.8 48.4 1.0
O A:HOH552 4.8 24.4 1.0

Magnesium binding site 2 out of 3 in 4n9u

Go back to Magnesium Binding Sites List in 4n9u
Magnesium binding site 2 out of 3 in the The Role of Lysine 200 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 Lysine 200 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:Mg402

b:27.2
occ:1.00
 O11 A:RIS404 1.9 45.1 1.0
O16 A:RIS404 2.0 48.6 1.0
O A:HOH550 2.0 37.2 1.0
O A:HOH552 2.1 24.4 1.0
OD2 A:ASP243 2.2 51.0 1.0
O A:HOH551 2.3 21.4 1.0
O A:HOH582 2.8 31.2 1.0
P9 A:RIS404 2.9 46.1 1.0
P14 A:RIS404 3.2 50.9 1.0
CG A:ASP243 3.2 55.5 1.0
O A:HOH581 3.3 42.1 1.0
C8 A:RIS404 3.3 47.3 1.0
O13 A:RIS404 3.4 44.1 1.0
OD1 A:ASP243 3.5 55.5 1.0
O12 A:RIS404 3.6 48.7 1.0
O A:HOH562 3.9 32.1 1.0
OD1 A:ASP247 4.0 59.3 1.0
O15 A:RIS404 4.0 43.3 1.0
O10 A:RIS404 4.2 41.0 1.0
O17 A:RIS404 4.3 48.4 1.0
NZ A:LYS257 4.4 66.0 1.0
OD1 A:ASP261 4.4 54.1 1.0
O A:ASP243 4.4 56.5 1.0
NE2 A:GLN240 4.4 56.3 1.0
CE A:LYS257 4.5 55.0 1.0
CB A:ASP243 4.5 50.8 1.0
O A:HOH554 4.6 31.8 1.0
OD2 A:ASP261 4.6 63.4 1.0
MG A:MG401 4.7 32.0 1.0
C A:ASP243 4.7 54.7 1.0
CG A:ASP247 4.7 58.9 1.0
O A:HOH549 4.8 21.0 1.0
CB A:ASP247 4.9 52.2 1.0
C7 A:RIS404 4.9 44.7 1.0
OD1 A:ASP244 4.9 45.2 1.0
CG A:ASP261 4.9 56.3 1.0

Magnesium binding site 3 out of 3 in 4n9u

Go back to Magnesium Binding Sites List in 4n9u
Magnesium binding site 3 out of 3 in the The Role of Lysine 200 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 Lysine 200 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:Mg403

b:34.8
occ:1.00
 OD2 A:ASP103 1.9 47.6 1.0
O A:HOH558 2.0 33.5 1.0
O15 A:RIS404 2.1 43.3 1.0
OD2 A:ASP107 2.2 58.4 1.0
O A:HOH557 2.2 41.2 1.0
O A:HOH556 2.4 51.1 1.0
CG A:ASP103 2.9 47.0 1.0
CG A:ASP107 3.0 54.0 1.0
OD1 A:ASP103 3.2 46.6 1.0
MG A:MG401 3.2 32.0 1.0
OD1 A:ASP107 3.2 50.3 1.0
P14 A:RIS404 3.4 50.9 1.0
O17 A:RIS404 3.6 48.4 1.0
O A:HOH581 3.7 42.1 1.0
OD2 A:ASP174 3.8 65.5 1.0
OE1 A:GLN171 4.2 58.0 1.0
CB A:ASP103 4.3 44.1 1.0
NE2 A:GLN171 4.3 55.5 1.0
O A:HOH562 4.3 32.1 1.0
O16 A:RIS404 4.4 48.6 1.0
CB A:ASP107 4.5 51.2 1.0
O A:HOH554 4.5 31.8 1.0
NZ A:LYS266 4.5 63.4 1.0
CE A:LYS266 4.6 55.1 1.0
C7 A:RIS404 4.7 44.7 1.0
C8 A:RIS404 4.7 47.3 1.0
O12 A:RIS404 4.7 48.7 1.0
CD A:GLN171 4.7 62.5 1.0
O A:HOH555 4.7 36.9 1.0
C2 A:RIS404 4.7 46.7 1.0
CG A:ASP174 4.7 60.2 1.0
C1 A:RIS404 4.8 46.1 1.0
O A:ASP103 4.8 48.2 1.0
CA A:ASP103 5.0 42.6 1.0

Reference:

M.K.Tsoumpra, J.R.C.Muniz, B.L.Barnett, E.Pilka, A.A.Kwaasi, K.L.Kavanagh, A.Evdokimov, R.L.Walter, F.H.Ebetino, U.Oppermann, R.G.G.Russell, J.E.Dunford. The Role of Lysine 200 in the Human Farnesyl Pyrophosphate Synthase Catalytic Mechanism and the Mode of Inhibition By the Nitrogen-Containing Bisphosphonates To Be Published.
Page generated: Mon Aug 19 23:26:42 2024

Last articles

Zn in 9JPJ
Zn in 9JP7
Zn in 9JPK
Zn in 9JPL
Zn in 9GN6
Zn in 9GN7
Zn in 9GKU
Zn in 9GKW
Zn in 9GKX
Zn in 9GL0
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy