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Magnesium in PDB 3g10: Structure of S. Pombe POP2P - MG2+ and MN2+ Bound Form

Protein crystallography data

The structure of Structure of S. Pombe POP2P - MG2+ and MN2+ Bound Form, PDB code: 3g10 was solved by K.R.Andersen, A.T.Jonstrup, L.B.Van, D.E.Brodersen, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 47.82 / 2.60
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 53.124, 53.991, 95.646, 90.00, 90.00, 90.00
R / Rfree (%) 18.7 / 23

Other elements in 3g10:

The structure of Structure of S. Pombe POP2P - MG2+ and MN2+ Bound Form also contains other interesting chemical elements:

Manganese (Mn) 1 atom

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Structure of S. Pombe POP2P - MG2+ and MN2+ Bound Form (pdb code 3g10). 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 S. Pombe POP2P - MG2+ and MN2+ Bound Form, PDB code: 3g10:

Magnesium binding site 1 out of 1 in 3g10

Go back to Magnesium Binding Sites List in 3g10
Magnesium binding site 1 out of 1 in the Structure of S. Pombe POP2P - MG2+ and MN2+ Bound Form


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Structure of S. Pombe POP2P - MG2+ and MN2+ Bound Form within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg333

b:58.5
occ:1.00
OE2 A:GLU52 2.6 73.7 1.0
OD2 A:ASP50 2.7 57.4 1.0
O A:THR51 3.2 51.4 1.0
CD A:GLU52 3.4 66.9 1.0
CG A:ASP50 3.5 53.0 1.0
O A:HOH349 3.5 66.2 1.0
OD1 A:ASP50 3.5 64.7 1.0
OD2 A:ASP240 3.5 57.3 1.0
MN A:MN334 3.6 88.2 1.0
OE1 A:GLU52 3.8 58.5 1.0
O A:HOH351 4.1 65.0 1.0
C A:THR51 4.4 48.5 1.0
CG A:ASP240 4.4 62.1 1.0
CG A:GLU52 4.6 51.2 1.0
CB A:ASP240 4.7 49.3 1.0
N A:THR51 4.9 50.1 1.0
CB A:ASP50 4.9 48.9 1.0

Reference:

K.R.Andersen, A.T.Jonstrup, L.B.Van, D.E.Brodersen. The Activity and Selectivity of Fission Yeast POP2P Are Affected By A High Affinity For ZN2+ and MN2+ in the Active Site Rna V. 15 850 2009.
ISSN: ISSN 1355-8382
PubMed: 19307292
DOI: 10.1261/RNA.1489409
Page generated: Sun Aug 10 21:08:31 2025

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