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Magnesium in PDB 8tfw: Fphe, Staphylococcus Aureus Fluorophosphonate-Binding Serine Hydrolases E, Boronic Acid-Based Compound N34 Bound

Protein crystallography data

The structure of Fphe, Staphylococcus Aureus Fluorophosphonate-Binding Serine Hydrolases E, Boronic Acid-Based Compound N34 Bound, PDB code: 8tfw was solved by M.Fellner, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 40.01 / 1.93
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 46.972, 76.419, 73.38, 90, 90.86, 90
R / Rfree (%) 21.3 / 26

Other elements in 8tfw:

The structure of Fphe, Staphylococcus Aureus Fluorophosphonate-Binding Serine Hydrolases E, Boronic Acid-Based Compound N34 Bound also contains other interesting chemical elements:

Fluorine (F) 6 atoms

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Fphe, Staphylococcus Aureus Fluorophosphonate-Binding Serine Hydrolases E, Boronic Acid-Based Compound N34 Bound (pdb code 8tfw). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total only one binding site of Magnesium was determined in the Fphe, Staphylococcus Aureus Fluorophosphonate-Binding Serine Hydrolases E, Boronic Acid-Based Compound N34 Bound, PDB code: 8tfw:

Magnesium binding site 1 out of 1 in 8tfw

Go back to Magnesium Binding Sites List in 8tfw
Magnesium binding site 1 out of 1 in the Fphe, Staphylococcus Aureus Fluorophosphonate-Binding Serine Hydrolases E, Boronic Acid-Based Compound N34 Bound


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Fphe, Staphylococcus Aureus Fluorophosphonate-Binding Serine Hydrolases E, Boronic Acid-Based Compound N34 Bound within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg302

b:34.9
occ:0.93
OE1 A:GLN83 2.1 29.9 1.0
O A:HOH467 2.1 26.1 0.9
O A:HOH454 2.4 28.3 0.9
CD A:GLN83 3.3 27.1 1.0
OH A:TYR116 3.4 33.5 1.0
O A:HOH442 3.9 29.2 1.0
O A:HOH446 3.9 22.3 1.0
NE2 A:GLN83 4.1 22.9 1.0
CG A:GLN83 4.2 24.9 1.0
CZ A:TYR116 4.4 29.6 1.0
CB A:GLN83 4.4 24.3 1.0
CE2 A:TYR116 4.6 27.3 1.0
O A:HOH472 4.6 30.8 1.0

Reference:

M.Fellner, M.Fellner. N/A N/A.
Page generated: Fri Aug 15 16:21:17 2025

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