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Magnesium in PDB 1s0p: Structure of the N-Terminal Domain of the Adenylyl Cyclase- Associated Protein (Cap) From Dictyostelium Discoideum.

Protein crystallography data

The structure of Structure of the N-Terminal Domain of the Adenylyl Cyclase- Associated Protein (Cap) From Dictyostelium Discoideum., PDB code: 1s0p was solved by D.Ksiazek, H.Brandstetter, L.Israel, G.P.Bourenkov, G.Katchalova, K.P.Janssen, H.D.Bartunik, A.A.Noegel, M.Schleicher, T.A.Holak, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 1.80 / 1.40
Space group P 1
Cell size a, b, c (Å), α, β, γ (°) 37.520, 42.130, 53.740, 97.42, 105.09, 97.15
R / Rfree (%) 18 / 21

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Structure of the N-Terminal Domain of the Adenylyl Cyclase- Associated Protein (Cap) From Dictyostelium Discoideum. (pdb code 1s0p). 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 Structure of the N-Terminal Domain of the Adenylyl Cyclase- Associated Protein (Cap) From Dictyostelium Discoideum., PDB code: 1s0p:

Magnesium binding site 1 out of 1 in 1s0p

Go back to Magnesium Binding Sites List in 1s0p
Magnesium binding site 1 out of 1 in the Structure of the N-Terminal Domain of the Adenylyl Cyclase- Associated Protein (Cap) From Dictyostelium Discoideum.


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Structure of the N-Terminal Domain of the Adenylyl Cyclase- Associated Protein (Cap) From Dictyostelium Discoideum. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg400

b:44.0
occ:1.00
O A:HOH402 2.0 9.8 1.0
O A:HOH401 2.0 8.5 1.0
O B:HOH405 2.1 9.1 1.0
O B:HOH404 2.1 8.2 1.0
O B:HOH403 2.2 9.5 1.0
O A:HOH406 2.2 9.0 1.0
O A:HOH518 4.0 14.8 1.0
OE1 A:GLU144 4.0 8.6 1.0
OD1 A:ASP128 4.1 13.6 1.0
O A:HOH537 4.1 13.2 1.0
OE1 B:GLU144 4.1 9.4 1.0
OD1 B:ASP128 4.2 14.3 1.0
OE2 A:GLU144 4.4 10.1 1.0
OD2 A:ASP128 4.4 13.8 1.0
O B:SER143 4.4 7.9 1.0
OE2 B:GLU144 4.5 9.7 1.0
OD2 B:ASP128 4.5 13.8 1.0
O A:SER143 4.6 8.2 1.0
O A:HOH519 4.6 12.8 1.0
CD A:GLU144 4.7 8.8 1.0
CG A:ASP128 4.7 11.7 1.0
CD B:GLU144 4.7 8.9 1.0
O B:HOH521 4.7 11.6 1.0
CA A:GLY124 4.7 10.3 1.0
CG B:ASP128 4.8 14.1 1.0
CA B:GLY124 4.9 11.1 1.0
O A:HOH602 4.9 18.4 1.0

Reference:

D.Ksiazek, H.Brandstetter, L.Israel, G.P.Bourenkov, G.Katchalova, K.P.Janssen, H.D.Bartunik, A.A.Noegel, M.Schleicher, T.A.Holak. Structure of the N-Terminal Domain of the Adenylyl Cyclase-Associated Protein (Cap) From Dictyostelium Discoideum Structure V. 11 1171 2003.
ISSN: ISSN 0969-2126
PubMed: 12962635
DOI: 10.1016/S0969-2126(03)00180-1
Page generated: Mon Dec 14 06:46:28 2020

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