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Magnesium in PDB 2b1q: X-Ray Structure of the Sucrose-Phosphatase (Spp) From Synechocystis Sp.PCC6803 in Complex with Trehalose

Enzymatic activity of X-Ray Structure of the Sucrose-Phosphatase (Spp) From Synechocystis Sp.PCC6803 in Complex with Trehalose

All present enzymatic activity of X-Ray Structure of the Sucrose-Phosphatase (Spp) From Synechocystis Sp.PCC6803 in Complex with Trehalose:
3.1.3.24;

Protein crystallography data

The structure of X-Ray Structure of the Sucrose-Phosphatase (Spp) From Synechocystis Sp.PCC6803 in Complex with Trehalose, PDB code: 2b1q was solved by S.Fieulaine, J.E.Lunn, J.-L.Ferrer, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 50.00 / 2.20
Space group P 65 2 2
Cell size a, b, c (Å), α, β, γ (°) 68.910, 68.910, 268.650, 90.00, 90.00, 120.00
R / Rfree (%) 17.8 / 20

Magnesium Binding Sites:

The binding sites of Magnesium atom in the X-Ray Structure of the Sucrose-Phosphatase (Spp) From Synechocystis Sp.PCC6803 in Complex with Trehalose (pdb code 2b1q). 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 X-Ray Structure of the Sucrose-Phosphatase (Spp) From Synechocystis Sp.PCC6803 in Complex with Trehalose, PDB code: 2b1q:

Magnesium binding site 1 out of 1 in 2b1q

Go back to Magnesium Binding Sites List in 2b1q
Magnesium binding site 1 out of 1 in the X-Ray Structure of the Sucrose-Phosphatase (Spp) From Synechocystis Sp.PCC6803 in Complex with Trehalose


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of X-Ray Structure of the Sucrose-Phosphatase (Spp) From Synechocystis Sp.PCC6803 in Complex with Trehalose within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg245

b:23.6
occ:1.00
 OD2 A:ASP9 2.3 18.2 1.0
OD1 A:ASN189 2.5 10.8 1.0
OD2 A:ASP190 2.5 12.7 1.0
OD1 A:ASP186 2.5 17.5 1.0
O A:HOH247 2.6 24.1 1.0
OG A:SER187 2.6 12.2 1.0
O A:HOH405 3.1 44.9 1.0
CG A:ASP190 3.3 12.4 1.0
CG A:ASN189 3.3 12.0 1.0
CG A:ASP9 3.5 17.0 1.0
OD1 A:ASP190 3.6 10.0 1.0
CB A:SER187 3.6 12.9 1.0
ND2 A:ASN189 3.7 10.1 1.0
O A:HOH248 3.7 11.9 1.0
N A:SER187 3.7 14.0 1.0
CG A:ASP186 3.7 18.1 1.0
NZ A:LYS163 4.0 9.6 1.0
CA A:SER187 4.1 13.9 1.0
OD1 A:ASP9 4.3 18.1 1.0
OD2 A:ASP186 4.4 20.0 1.0
CB A:ASP9 4.4 13.7 1.0
N A:ASP186 4.4 10.5 1.0
O A:HOH259 4.5 29.7 1.0
CB A:ASP190 4.5 11.2 1.0
C A:ASP186 4.6 11.7 1.0
C A:SER187 4.6 14.1 1.0
CB A:ASN189 4.6 10.3 1.0
N A:ASP190 4.7 11.6 1.0
O A:SER187 4.7 14.9 1.0
N A:ASN189 4.8 12.3 1.0
C A:ASN189 4.8 13.4 1.0
CA A:ASP186 4.9 11.8 1.0
CB A:ASP186 4.9 14.5 1.0
CA A:ASN189 5.0 13.1 1.0

Reference:

S.Fieulaine, J.E.Lunn, J.-L.Ferrer. Crystal Structure of A Cyanobacterial Sucrose-Phosphatase in Complex with Glucose-Containing Disaccharides Proteins V. 68 796 2007.
ISSN: ISSN 0887-3585
PubMed: 17510968
DOI: 10.1002/PROT.21481
Page generated: Sun Aug 10 09:52:12 2025

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