Atomistry » Magnesium » PDB 3l9b-3lop » 3lee
Atomistry »
  Magnesium »
    PDB 3l9b-3lop »
      3lee »

Magnesium in PDB 3lee: Crystal Structure of the Human Squalene Synthase Complexed with Bph- 652

Enzymatic activity of Crystal Structure of the Human Squalene Synthase Complexed with Bph- 652

All present enzymatic activity of Crystal Structure of the Human Squalene Synthase Complexed with Bph- 652:
2.5.1.21;

Protein crystallography data

The structure of Crystal Structure of the Human Squalene Synthase Complexed with Bph- 652, PDB code: 3lee was solved by Y.-L.Liu, F.-Y.Lin, E.Oldfield, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 29.58 / 3.20
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 85.662, 153.422, 92.904, 90.00, 90.50, 90.00
R / Rfree (%) 19.1 / 27.6

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Crystal Structure of the Human Squalene Synthase Complexed with Bph- 652 (pdb code 3lee). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 6 binding sites of Magnesium where determined in the Crystal Structure of the Human Squalene Synthase Complexed with Bph- 652, PDB code: 3lee:
Jump to Magnesium binding site number: 1; 2; 3; 4; 5; 6;

Magnesium binding site 1 out of 6 in 3lee

Go back to Magnesium Binding Sites List in 3lee
Magnesium binding site 1 out of 6 in the Crystal Structure of the Human Squalene Synthase Complexed with Bph- 652


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 the Human Squalene Synthase Complexed with Bph- 652 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg452

b:40.2
occ:1.00
 OD2 A:ASP84 2.3 60.8 1.0
OE2 A:GLU83 2.3 50.1 1.0
OAC A:B65451 2.6 78.2 1.0
OD2 A:ASP80 2.7 47.0 1.0
OD1 A:ASP84 2.9 61.6 1.0
CG A:ASP84 2.9 58.5 1.0
OAA A:B65451 3.0 78.2 1.0
CD A:GLU83 3.0 51.8 1.0
PAX A:B65451 3.3 78.5 1.0
CG A:GLU83 3.4 49.4 1.0
CG A:ASP80 3.5 43.6 1.0
OD1 A:ASP80 3.6 49.4 1.0
OH A:TYR171 3.7 54.0 1.0
OE1 A:GLU83 3.9 54.8 1.0
OAB A:B65451 4.2 77.7 1.0
CB A:ASP84 4.4 53.7 1.0
OAE A:B65451 4.6 75.6 1.0
CAW A:B65451 4.8 77.4 1.0
NH1 A:ARG228 4.8 69.8 1.0
CB A:ASP80 4.9 39.0 1.0
CB A:GLU83 4.9 46.9 1.0
CA A:ASP84 4.9 52.6 1.0

Magnesium binding site 2 out of 6 in 3lee

Go back to Magnesium Binding Sites List in 3lee
Magnesium binding site 2 out of 6 in the Crystal Structure of the Human Squalene Synthase Complexed with Bph- 652


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 the Human Squalene Synthase Complexed with Bph- 652 within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mg452

b:37.5
occ:1.00
 OD1 B:ASP84 2.2 51.3 1.0
OD1 B:ASP80 2.3 46.2 1.0
OAA B:B65451 2.6 80.8 1.0
OAC B:B65451 2.8 79.3 1.0
OE1 B:GLU83 2.9 58.2 1.0
CG B:ASP84 3.0 50.9 1.0
PAX B:B65451 3.0 81.3 1.0
OD2 B:ASP84 3.1 51.4 1.0
CG B:ASP80 3.4 42.8 1.0
CD B:GLU83 3.6 55.5 1.0
OAB B:B65451 3.6 79.5 1.0
OD2 B:ASP80 3.7 42.3 1.0
OE2 B:GLU83 4.0 58.0 1.0
O B:ASP80 4.4 43.2 1.0
CB B:ASP84 4.4 50.2 1.0
CB B:GLU83 4.6 47.1 1.0
CB B:ASP80 4.7 40.1 1.0
CG B:GLU83 4.7 51.3 1.0
CAW B:B65451 4.7 82.8 1.0
N B:ASP84 4.8 51.3 1.0
CA B:ASP84 4.9 50.3 1.0
OH B:TYR171 4.9 53.9 1.0
O B:HOH5 4.9 37.8 1.0

Magnesium binding site 3 out of 6 in 3lee

Go back to Magnesium Binding Sites List in 3lee
Magnesium binding site 3 out of 6 in the Crystal Structure of the Human Squalene Synthase Complexed with Bph- 652


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 the Human Squalene Synthase Complexed with Bph- 652 within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Mg452

b:52.6
occ:1.00
 OAC C:B65451 2.2 91.1 1.0
OD2 C:ASP80 2.3 40.8 1.0
OD1 C:ASP84 2.6 53.7 1.0
OE1 C:GLU83 2.7 57.7 1.0
OAA C:B65451 2.8 90.9 1.0
PAX C:B65451 3.0 92.4 1.0
OD2 C:ASP84 3.3 53.9 1.0
CG C:ASP84 3.3 51.6 1.0
CG C:ASP80 3.5 38.5 1.0
CD C:GLU83 3.9 55.0 1.0
OH C:TYR171 3.9 55.8 1.0
OAB C:B65451 4.0 92.0 1.0
OD1 C:ASP80 4.1 37.7 1.0
CAW C:B65451 4.4 91.2 1.0
CAR C:B65451 4.5 88.1 1.0
OE2 C:GLU83 4.6 56.3 1.0
CB C:ASP80 4.6 35.0 1.0
O C:ASP80 4.7 35.6 1.0
OAE C:B65451 4.7 92.1 1.0
CG C:GLU83 4.8 50.7 1.0
CB C:ASP84 4.8 48.0 1.0
CB C:GLU83 4.9 46.9 1.0
CG1 C:VAL175 5.0 39.8 1.0

Magnesium binding site 4 out of 6 in 3lee

Go back to Magnesium Binding Sites List in 3lee
Magnesium binding site 4 out of 6 in the Crystal Structure of the Human Squalene Synthase Complexed with Bph- 652


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 4 of Crystal Structure of the Human Squalene Synthase Complexed with Bph- 652 within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Mg452

b:34.4
occ:1.00
 OD2 D:ASP84 2.3 62.9 1.0
OAC D:B65451 2.5 88.7 1.0
OD2 D:ASP80 2.7 53.9 1.0
OAE D:B65451 2.8 89.7 1.0
O D:HOH395 2.9 30.9 1.0
CG D:ASP84 3.2 64.1 1.0
OD1 D:ASP80 3.4 53.7 1.0
CG D:ASP80 3.5 50.4 1.0
OAF D:B65451 3.5 91.7 1.0
SAY D:B65451 3.7 91.1 1.0
PAX D:B65451 3.9 89.9 1.0
OD1 D:ASP84 3.9 65.4 1.0
CB D:ASP84 4.1 64.5 1.0
CAW D:B65451 4.3 89.2 1.0
O D:ASP80 4.5 51.1 1.0
OE2 D:GLU83 4.6 56.2 1.0
NH1 D:ARG77 4.6 52.5 1.0
CAR D:B65451 4.7 87.5 1.0
OAA D:B65451 4.8 88.5 1.0
OAB D:B65451 4.8 89.4 1.0
NH1 D:ARG228 4.9 0.4 1.0
CB D:ASP80 4.9 46.8 1.0
OAD D:B65451 5.0 91.1 1.0

Magnesium binding site 5 out of 6 in 3lee

Go back to Magnesium Binding Sites List in 3lee
Magnesium binding site 5 out of 6 in the Crystal Structure of the Human Squalene Synthase Complexed with Bph- 652


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 5 of Crystal Structure of the Human Squalene Synthase Complexed with Bph- 652 within 5.0Å range:
probe atom residue distance (Å) B Occ
E:Mg452

b:81.3
occ:1.00
 OH E:TYR171 2.2 71.4 1.0
OAA E:B65451 2.5 87.2 1.0
OE1 E:GLU83 2.7 80.1 1.0
OE2 E:GLU83 2.8 81.6 1.0
CD E:GLU83 3.1 81.3 1.0
CZ E:TYR171 3.2 71.4 1.0
CG1 E:VAL175 3.5 65.3 1.0
PAX E:B65451 3.6 87.8 1.0
OAB E:B65451 3.7 86.5 1.0
CE1 E:TYR171 3.9 71.8 1.0
CB E:VAL175 3.9 63.8 1.0
CE2 E:TYR171 4.2 70.9 1.0
OAC E:B65451 4.2 87.1 1.0
OD2 E:ASP80 4.4 66.6 1.0
CG2 E:VAL175 4.4 63.6 1.0
OD1 E:ASP84 4.4 92.6 1.0
CG E:GLU83 4.6 81.7 1.0
CE E:MET154 4.7 80.2 1.0

Magnesium binding site 6 out of 6 in 3lee

Go back to Magnesium Binding Sites List in 3lee
Magnesium binding site 6 out of 6 in the Crystal Structure of the Human Squalene Synthase Complexed with Bph- 652


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 6 of Crystal Structure of the Human Squalene Synthase Complexed with Bph- 652 within 5.0Å range:
probe atom residue distance (Å) B Occ
F:Mg452

b:81.3
occ:1.00
 OAC F:B65451 2.5 0.2 1.0
OAB F:B65451 2.5 0.7 1.0
OD1 F:ASP84 2.6 0.6 1.0
PAX F:B65451 2.8 0.6 1.0
OD1 F:ASP80 2.8 76.6 1.0
OE1 F:GLU83 3.1 0.1 1.0
OAA F:B65451 3.4 0.3 1.0
CG F:ASP84 3.5 0.1 1.0
OD2 F:ASP84 3.6 0.5 1.0
O F:HOH377 3.7 53.8 1.0
CG F:ASP80 3.7 74.2 1.0
OD2 F:ASP80 4.0 75.2 1.0
CD F:GLU83 4.0 0.4 1.0
CAW F:B65451 4.5 0.9 1.0
OAE F:B65451 4.6 0.3 1.0
OE2 F:GLU83 4.7 0.9 1.0
OH F:TYR171 4.8 88.8 1.0
CB F:ASP84 4.8 0.4 1.0
CG F:GLU83 4.9 0.3 1.0
SAY F:B65451 5.0 0.6 1.0

Reference:

F.-Y.Lin, C.-I.Liu, Y.-L.Liu, Y.Zhang, K.Wang, R.Cao, A.H.J.Wang, E.Oldfield. Mechanism of Action (and Inhibition) of Head-to-Head Terpene Synthases: A Structural Investigation To Be Published.
Page generated: Wed Aug 14 18:31:17 2024

Last articles

Cl in 5W6O
Cl in 5W6S
Cl in 5W5S
Cl in 5W6L
Cl in 5W6H
Cl in 5W5U
Cl in 5W6F
Cl in 5W4V
Cl in 5W5J
Cl in 5W5B
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy