Europium in PDB 3py9: X-Ray Structural Studies of the Entire Extra-Cellular Region of the Ser/Thr Kinase Prkc From Staphylococcus Aureus

The structure of X-Ray Structural Studies of the Entire Extra-Cellular Region of the Ser/Thr Kinase Prkc From Staphylococcus Aureus, PDB code: 3py9 was solved by A.Ruggiero, F.Squeglia, D.Marasco, R.Marchetti, A.Molinaro, R.Berisio, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	9.97 / 2.20
Space group	P 21 21 2
Cell size a, b, c (Å), α, β, γ (°)	55.681, 69.103, 88.430, 90.00, 90.00, 90.00
R / Rfree (%)	24.4 / 29.3

The binding sites of Europium atom in the X-Ray Structural Studies of the Entire Extra-Cellular Region of the Ser/Thr Kinase Prkc From Staphylococcus Aureus (pdb code 3py9). This binding sites where shown within 5.0 Angstroms radius around Europium atom.
In total 4 binding sites of Europium where determined in the X-Ray Structural Studies of the Entire Extra-Cellular Region of the Ser/Thr Kinase Prkc From Staphylococcus Aureus, PDB code: 3py9:
Jump to Europium binding site number: 1; 2; 3; 4;

Europium binding site 1 out of 4 in the X-Ray Structural Studies of the Entire Extra-Cellular Region of the Ser/Thr Kinase Prkc From Staphylococcus Aureus


Mono view


Stereo pair view

A full contact list of Europium with other atoms in the Eu binding site number 1 of X-Ray Structural Studies of the Entire Extra-Cellular Region of the Ser/Thr Kinase Prkc From Staphylococcus Aureus within 5.0Å range: probe atom residue distance (Å) B Occ A:Eu301 b:62.3 occ:0.50 OE1 A:GLU8 2.8 42.0 1.0 OE2 A:GLU8 2.9 42.1 1.0 CD A:GLU8 3.2 41.4 1.0 O A:GLY55 4.5 40.3 1.0 CG A:GLU8 4.7 39.6 1.0

Europium binding site 2 out of 4 in the X-Ray Structural Studies of the Entire Extra-Cellular Region of the Ser/Thr Kinase Prkc From Staphylococcus Aureus


Mono view


Stereo pair view

A full contact list of Europium with other atoms in the Eu binding site number 2 of X-Ray Structural Studies of the Entire Extra-Cellular Region of the Ser/Thr Kinase Prkc From Staphylococcus Aureus within 5.0Å range: probe atom residue distance (Å) B Occ A:Eu302 b:73.8 occ:0.50 OE1 A:GLU44 2.5 46.0 1.0 OE2 A:GLU44 2.6 45.7 1.0 CD A:GLU44 2.9 44.7 1.0 CG A:GLU44 4.4 44.3 1.0 O A:HOH410 4.6 58.2 1.0 O A:LYS70 4.8 42.7 1.0 O A:HOH393 4.9 45.9 1.0

Europium binding site 3 out of 4 in the X-Ray Structural Studies of the Entire Extra-Cellular Region of the Ser/Thr Kinase Prkc From Staphylococcus Aureus


Mono view


Stereo pair view

A full contact list of Europium with other atoms in the Eu binding site number 3 of X-Ray Structural Studies of the Entire Extra-Cellular Region of the Ser/Thr Kinase Prkc From Staphylococcus Aureus within 5.0Å range: probe atom residue distance (Å) B Occ A:Eu303 b:97.0 occ:0.50 OD1 A:ASP230 2.5 41.1 1.0 OD2 A:ASP230 2.6 42.1 1.0 CG A:ASP230 2.9 38.6 1.0 O A:HOH400 3.7 54.2 1.0 CB A:ASP230 4.4 36.5 1.0 O A:HOH327 4.5 32.7 1.0

Europium binding site 4 out of 4 in the X-Ray Structural Studies of the Entire Extra-Cellular Region of the Ser/Thr Kinase Prkc From Staphylococcus Aureus


Mono view


Stereo pair view

A full contact list of Europium with other atoms in the Eu binding site number 4 of X-Ray Structural Studies of the Entire Extra-Cellular Region of the Ser/Thr Kinase Prkc From Staphylococcus Aureus within 5.0Å range: probe atom residue distance (Å) B Occ A:Eu305 b:78.3 occ:0.50 OD2 A:ASP99 2.4 52.0 1.0 OD1 A:ASP130 2.4 55.2 1.0 OD1 A:ASN132 2.6 49.5 1.0 CG A:ASP99 3.2 51.7 1.0 OD1 A:ASP99 3.4 55.5 1.0 CG A:ASP130 3.6 54.6 1.0 CG A:ASN132 3.8 49.1 1.0 CA A:ASP130 4.1 53.1 1.0 CB A:ASP99 4.4 50.2 1.0 CB A:ASP130 4.4 53.4 1.0 C A:ASP130 4.5 52.2 1.0 N A:ASN132 4.5 49.0 1.0 OD2 A:ASP130 4.5 56.0 1.0 CA A:ASN132 4.6 48.0 1.0 CB A:ASN132 4.7 48.2 1.0 ND2 A:ASN132 4.7 50.1 1.0 O A:ASP130 4.7 52.2 1.0 O A:HOH334 5.0 54.5 1.0

A.Ruggiero, F.Squeglia, D.Marasco, R.Marchetti, A.Molinaro, R.Berisio. X-Ray Structural Studies of the Entire Extracellular Region of the Serine/Threonine Kinase Prkc From Staphylococcus Aureus. Biochem.J. V. 435 33 2011.
ISSN: ISSN 0264-6021
PubMed: 21208192
DOI: 10.1042/BJ20101643