Fluorine in PDB 6h90: K145A Variant of Beta-Phosphoglucomutase From Lactococcus Lactis Inhibited By Beryllium Trifluoride to 1.3 A.

Enzymatic activity of K145A Variant of Beta-Phosphoglucomutase From Lactococcus Lactis Inhibited By Beryllium Trifluoride to 1.3 A.

All present enzymatic activity of K145A Variant of Beta-Phosphoglucomutase From Lactococcus Lactis Inhibited By Beryllium Trifluoride to 1.3 A.:
5.4.2.6;

Protein crystallography data

The structure of K145A Variant of Beta-Phosphoglucomutase From Lactococcus Lactis Inhibited By Beryllium Trifluoride to 1.3 A., PDB code: 6h90 was solved by A.J.Robertson, C.Bisson, J.P.Waltho, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 40.75 / 1.31
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 52.320, 53.630, 81.500, 90.00, 90.00, 90.00
R / Rfree (%) 13.5 / 16.3

Other elements in 6h90:

The structure of K145A Variant of Beta-Phosphoglucomutase From Lactococcus Lactis Inhibited By Beryllium Trifluoride to 1.3 A. also contains other interesting chemical elements:

Magnesium (Mg) 1 atom
Sodium (Na) 1 atom

Fluorine Binding Sites:

The binding sites of Fluorine atom in the K145A Variant of Beta-Phosphoglucomutase From Lactococcus Lactis Inhibited By Beryllium Trifluoride to 1.3 A. (pdb code 6h90). This binding sites where shown within 5.0 Angstroms radius around Fluorine atom.
In total 3 binding sites of Fluorine where determined in the K145A Variant of Beta-Phosphoglucomutase From Lactococcus Lactis Inhibited By Beryllium Trifluoride to 1.3 A., PDB code: 6h90:
Jump to Fluorine binding site number: 1; 2; 3;

Fluorine binding site 1 out of 3 in 6h90

Go back to Fluorine Binding Sites List in 6h90
Fluorine binding site 1 out of 3 in the K145A Variant of Beta-Phosphoglucomutase From Lactococcus Lactis Inhibited By Beryllium Trifluoride to 1.3 A.


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 1 of K145A Variant of Beta-Phosphoglucomutase From Lactococcus Lactis Inhibited By Beryllium Trifluoride to 1.3 A. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:F303

b:12.8
occ:1.00
F1 A:BEF303 0.0 12.8 1.0
BE A:BEF303 1.6 10.6 1.0
F3 A:BEF303 2.5 11.0 1.0
O A:HOH632 2.6 20.5 1.0
OD1 A:ASP8 2.6 10.0 1.0
F2 A:BEF303 2.6 10.3 1.0
N A:ALA115 2.9 9.4 1.0
O A:HOH613 3.3 28.5 1.0
CB A:ALA115 3.4 13.5 1.0
O A:HOH459 3.5 13.0 1.0
OG A:SER114 3.7 9.8 1.0
CA A:ALA115 3.7 10.7 1.0
CG A:ASP8 3.7 9.9 1.0
CA A:SER114 3.8 9.4 1.0
C A:SER114 3.8 8.9 1.0
O A:HOH481 4.1 11.5 1.0
OD2 A:ASP8 4.2 10.2 1.0
CB A:SER114 4.2 8.9 1.0
MG A:MG301 4.3 10.8 1.0
N A:SER116 4.3 10.0 1.0
O A:HOH687 4.4 29.2 1.0
C A:ALA115 4.4 11.7 1.0
O A:HOH462 4.5 17.7 1.0
OE2 A:GLU169 4.5 12.7 1.0
N A:LEU9 4.9 8.9 1.0
CB A:ASP8 4.9 9.9 1.0

Fluorine binding site 2 out of 3 in 6h90

Go back to Fluorine Binding Sites List in 6h90
Fluorine binding site 2 out of 3 in the K145A Variant of Beta-Phosphoglucomutase From Lactococcus Lactis Inhibited By Beryllium Trifluoride to 1.3 A.


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 2 of K145A Variant of Beta-Phosphoglucomutase From Lactococcus Lactis Inhibited By Beryllium Trifluoride to 1.3 A. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:F303

b:10.3
occ:1.00
F2 A:BEF303 0.0 10.3 1.0
BE A:BEF303 1.6 10.6 1.0
MG A:MG301 2.0 10.8 1.0
F3 A:BEF303 2.5 11.0 1.0
F1 A:BEF303 2.6 12.8 1.0
OD1 A:ASP8 2.6 10.0 1.0
OD2 A:ASP8 2.8 10.2 1.0
O A:HOH481 2.9 11.5 1.0
O A:HOH433 3.0 12.6 1.0
O A:ASP10 3.0 10.8 1.0
CG A:ASP8 3.1 9.9 1.0
CB A:ASP10 3.3 12.3 1.0
O A:HOH632 3.4 20.5 1.0
N A:ASP10 3.5 9.5 1.0
O A:HOH613 3.6 28.5 1.0
CA A:ASP10 3.7 10.5 1.0
C A:ASP10 3.7 10.1 1.0
OD1 A:ASP170 4.1 11.2 1.0
OD2 A:ASP10 4.2 22.8 1.0
CG A:ASP10 4.3 17.5 1.0
N A:LEU9 4.5 8.9 1.0
C A:LEU9 4.5 8.9 1.0
CB A:ASP8 4.6 9.9 1.0
OE2 A:GLU169 4.8 12.7 1.0

Fluorine binding site 3 out of 3 in 6h90

Go back to Fluorine Binding Sites List in 6h90
Fluorine binding site 3 out of 3 in the K145A Variant of Beta-Phosphoglucomutase From Lactococcus Lactis Inhibited By Beryllium Trifluoride to 1.3 A.


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 3 of K145A Variant of Beta-Phosphoglucomutase From Lactococcus Lactis Inhibited By Beryllium Trifluoride to 1.3 A. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:F303

b:11.0
occ:1.00
F3 A:BEF303 0.0 11.0 1.0
BE A:BEF303 1.6 10.6 1.0
OD1 A:ASP8 2.5 10.0 1.0
F1 A:BEF303 2.5 12.8 1.0
F2 A:BEF303 2.5 10.3 1.0
OG A:SER114 2.6 9.8 1.0
N A:ASP10 2.8 9.5 1.0
N A:LEU9 3.0 8.9 1.0
O A:HOH613 3.2 28.5 1.0
CB A:LEU9 3.3 11.8 0.7
CB A:LEU9 3.3 6.1 0.3
CA A:LEU9 3.4 9.9 0.7
CB A:SER114 3.4 8.9 1.0
CA A:LEU9 3.4 8.3 0.3
CG A:ASP8 3.5 9.9 1.0
C A:LEU9 3.5 8.9 1.0
CA A:ASP10 3.8 10.5 1.0
CB A:ASP10 3.8 12.3 1.0
CA A:SER114 4.0 9.4 1.0
OD2 A:ASP8 4.0 10.2 1.0
N A:ALA115 4.2 9.4 1.0
C A:ASP8 4.2 8.9 1.0
MG A:MG301 4.2 10.8 1.0
O A:ASP10 4.3 10.8 1.0
CG A:LEU9 4.4 15.5 0.7
N A:SER116 4.5 10.0 1.0
CA A:ASP8 4.5 8.8 1.0
C A:SER114 4.5 8.9 1.0
CB A:SER116 4.6 11.7 1.0
C A:ASP10 4.6 10.1 1.0
CB A:ASP8 4.6 9.9 1.0
CD2 A:LEU9 4.6 18.3 0.7
CG A:LEU9 4.7 5.1 0.3
O A:LEU9 4.7 10.1 1.0
O A:HOH632 4.8 20.5 1.0
CD2 A:LEU9 4.8 5.4 0.3

Reference:

A.J.Robertson, C.Bisson, J.P.Waltho. Transition State of Phospho-Enzyme Hydrolysis in Beta-Phosphoglucomutase. To Be Published.
Page generated: Sun Dec 13 12:52:29 2020

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