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Magnesium in PDB 3kd3: Crystal Structure of A Phosphoserine Phosphohydrolase-Like Protein From Francisella Tularensis Subsp. Tularensis Schu S4

Protein crystallography data

The structure of Crystal Structure of A Phosphoserine Phosphohydrolase-Like Protein From Francisella Tularensis Subsp. Tularensis Schu S4, PDB code: 3kd3 was solved by B.Nocek, M.Zhou, S.Peterson, W.Anderson, A.Joachimiak, Csgid, Center Forstructural Genomics Of Infectious Diseases (Csgid), with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 29.34 / 1.70
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 72.574, 78.798, 87.918, 90.00, 90.00, 90.00
R / Rfree (%) 16.3 / 18.6

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Crystal Structure of A Phosphoserine Phosphohydrolase-Like Protein From Francisella Tularensis Subsp. Tularensis Schu S4 (pdb code 3kd3). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Crystal Structure of A Phosphoserine Phosphohydrolase-Like Protein From Francisella Tularensis Subsp. Tularensis Schu S4, PDB code: 3kd3:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in 3kd3

Go back to Magnesium Binding Sites List in 3kd3
Magnesium binding site 1 out of 2 in the Crystal Structure of A Phosphoserine Phosphohydrolase-Like Protein From Francisella Tularensis Subsp. Tularensis Schu S4


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 A Phosphoserine Phosphohydrolase-Like Protein From Francisella Tularensis Subsp. Tularensis Schu S4 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg401

b:16.1
occ:1.00
OD2 A:ASP7 2.1 22.6 1.0
O A:HOH217 2.2 11.0 1.0
OD1 A:ASP169 2.3 10.9 1.0
O A:ASP9 2.3 6.2 1.0
O A:HOH362 2.6 24.1 1.0
CG A:ASP169 3.2 8.7 1.0
CG A:ASP7 3.2 11.1 1.0
C A:ASP9 3.3 7.2 1.0
OD2 A:ASP169 3.4 10.3 1.0
CB A:ASP9 3.8 7.4 1.0
CB A:ASP7 3.9 8.6 1.0
OG1 A:THR11 4.0 7.2 1.0
CA A:ASP9 4.0 5.7 1.0
OD1 A:ASP7 4.1 19.7 1.0
N A:ASP9 4.2 5.9 1.0
O A:HOH356 4.3 14.3 1.0
O A:HOH295 4.3 21.2 1.0
O A:HOH265 4.3 10.6 1.0
N A:SER10 4.4 6.1 1.0
CB A:SER10 4.4 8.1 1.0
OE2 A:GLU16 4.4 16.4 1.0
OD2 A:ASP173 4.5 14.8 1.0
N A:ASP169 4.5 7.1 1.0
CB A:ASP169 4.6 7.5 1.0
SE A:MSE44 4.6 15.4 0.8
CA A:SER10 4.7 6.6 1.0
N A:GLY170 4.8 7.8 1.0
C A:SER10 4.9 6.8 1.0
N A:THR11 4.9 6.6 1.0
C A:PHE8 4.9 7.0 1.0
CB A:THR11 5.0 6.5 1.0

Magnesium binding site 2 out of 2 in 3kd3

Go back to Magnesium Binding Sites List in 3kd3
Magnesium binding site 2 out of 2 in the Crystal Structure of A Phosphoserine Phosphohydrolase-Like Protein From Francisella Tularensis Subsp. Tularensis Schu S4


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 A Phosphoserine Phosphohydrolase-Like Protein From Francisella Tularensis Subsp. Tularensis Schu S4 within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mg401

b:14.6
occ:1.00
OD1 B:ASP169 2.2 10.6 1.0
OD2 B:ASP7 2.2 14.5 1.0
O B:ASP9 2.2 7.9 1.0
O B:HOH284 2.3 11.8 1.0
O B:HOH336 2.6 21.5 1.0
CG B:ASP169 3.1 8.3 1.0
CG B:ASP7 3.2 11.7 1.0
C B:ASP9 3.3 7.2 1.0
OD2 B:ASP169 3.4 9.8 1.0
CB B:ASP9 3.8 6.4 1.0
CB B:ASP7 3.8 8.2 1.0
CA B:ASP9 4.0 6.8 1.0
OG1 B:THR11 4.1 6.6 1.0
O B:HOH247 4.1 7.7 1.0
OD1 B:ASP7 4.1 13.1 1.0
N B:ASP9 4.2 6.6 1.0
O B:HOH324 4.3 14.3 1.0
N B:SER10 4.3 7.2 1.0
OE2 B:GLU16 4.4 13.5 1.0
CB B:SER10 4.4 6.5 1.0
OD2 B:ASP173 4.5 11.3 1.0
CB B:ASP169 4.5 5.7 1.0
N B:ASP169 4.5 6.6 1.0
CA B:SER10 4.7 7.4 1.0
SE B:MSE44 4.7 14.8 0.8
NZ B:LYS149 4.8 21.1 1.0
C B:SER10 4.8 7.0 1.0
N B:GLY170 4.9 6.8 1.0
N B:THR11 4.9 7.4 1.0
C B:PHE8 4.9 5.6 1.0
O B:HOH344 4.9 20.7 1.0
CB B:THR11 5.0 7.4 1.0
CA B:ASP169 5.0 6.1 1.0

Reference:

B.Nocek, M.Zhou, S.Peterson, W.Anderson, A.Joachimiak, Csgid. Crystal Structure of A Phosphoserine Phosphohydrolase-Like Protein From Francisella Tularensis Subsp. Tularensis SCHUS4 To Be Published.
Page generated: Wed Aug 14 18:02:27 2024

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