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Magnesium in PDB 1sz3: Crystal Structure of Nudix Hydrolase DR1025 in Complexed with Gnp and Mg+2

Protein crystallography data

The structure of Crystal Structure of Nudix Hydrolase DR1025 in Complexed with Gnp and Mg+2, PDB code: 1sz3 was solved by W.Ranatunga, E.E.Hill, J.L.Mooster, E.L.Holbrook, U.Schulze-Gahmen, W.Xu, M.J.Bessman, S.E.Brenner, S.R.Holbrook, Berkeleystructural Genomics Center (Bsgc), with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 50.00 / 1.60
Space group P 41
Cell size a, b, c (Å), α, β, γ (°) 53.072, 53.072, 122.197, 90.00, 90.00, 90.00
R / Rfree (%) 21.3 / 23.4

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Crystal Structure of Nudix Hydrolase DR1025 in Complexed with Gnp and Mg+2 (pdb code 1sz3). 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 Nudix Hydrolase DR1025 in Complexed with Gnp and Mg+2, PDB code: 1sz3:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in 1sz3

Go back to Magnesium Binding Sites List in 1sz3
Magnesium binding site 1 out of 2 in the Crystal Structure of Nudix Hydrolase DR1025 in Complexed with Gnp and Mg+2


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 Nudix Hydrolase DR1025 in Complexed with Gnp and Mg+2 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg201

b:36.3
occ:1.00
O A:HOH765 2.7 26.7 1.0
O A:HOH846 2.7 37.6 1.0
OE2 A:GLU65 2.7 28.9 1.0
O A:HOH853 3.1 41.1 1.0
CD A:GLU65 3.7 25.4 1.0
OE1 A:GLU65 3.9 28.5 1.0
OE1 A:GLU68 4.2 27.9 1.0
N A:ALA51 4.5 17.7 1.0
O A:HOH810 4.7 50.1 1.0
O A:ALA51 4.8 17.7 1.0
CA A:GLY50 4.9 17.1 1.0
CB A:ALA51 5.0 18.0 1.0

Magnesium binding site 2 out of 2 in 1sz3

Go back to Magnesium Binding Sites List in 1sz3
Magnesium binding site 2 out of 2 in the Crystal Structure of Nudix Hydrolase DR1025 in Complexed with Gnp and Mg+2


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 Nudix Hydrolase DR1025 in Complexed with Gnp and Mg+2 within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mg202

b:35.0
occ:1.00
O B:HOH817 2.6 37.8 1.0
OE2 B:GLU65 2.7 28.8 1.0
O B:HOH878 2.7 34.7 1.0
O B:HOH844 2.7 46.3 1.0
CD B:GLU65 3.5 26.0 1.0
OE1 B:GLU65 3.6 29.0 1.0
N B:ALA51 4.2 17.2 1.0
O B:HOH896 4.2 38.6 1.0
OE1 B:GLU68 4.3 29.2 1.0
CA B:GLY50 4.6 16.4 1.0
NH1 B:ARG64 4.6 26.0 1.0
O B:ALA51 4.8 17.9 1.0
C B:GLY50 4.9 15.8 1.0
CB B:ALA51 4.9 18.6 1.0
CG B:GLU65 4.9 23.4 1.0

Reference:

W.Ranatunga, E.E.Hill, J.L.Mooster, E.L.Holbrook, U.Schulze-Gahmen, W.Xu, M.J.Bessman, S.E.Brenner, S.R.Holbrook. Structural Studies of the Nudix Hydrolase DR1025 From Deinococcus Radiodurans and Its Ligand Complexes. J.Mol.Biol. V. 339 103 2004.
ISSN: ISSN 0022-2836
PubMed: 15123424
DOI: 10.1016/J.JMB.2004.01.065
Page generated: Tue Aug 13 14:23:17 2024

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