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Magnesium in PDB 2x1a: Structure of RNA15 Rrm with Rna Bound (G)

Protein crystallography data

The structure of Structure of RNA15 Rrm with Rna Bound (G), PDB code: 2x1a was solved by C.Pancevac, D.C.Goldstone, A.Ramos, I.A.Taylor, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 37.48 / 2.05
Space group P 21 21 2
Cell size a, b, c (Å), α, β, γ (°) 37.037, 74.967, 31.508, 90.00, 90.00, 90.00
R / Rfree (%) 20.615 / 25.807

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Structure of RNA15 Rrm with Rna Bound (G) (pdb code 2x1a). 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 RNA15 Rrm with Rna Bound (G), PDB code: 2x1a:

Magnesium binding site 1 out of 1 in 2x1a

Go back to Magnesium Binding Sites List in 2x1a
Magnesium binding site 1 out of 1 in the Structure of RNA15 Rrm with Rna Bound (G)


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Structure of RNA15 Rrm with Rna Bound (G) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg1102

b:42.8
occ:1.00
OP1 B:G2 2.7 65.1 1.0
N A:SER24 3.2 19.8 1.0
N2 B:G2 3.3 43.8 1.0
O A:GLY60 3.5 18.9 1.0
CA A:SER24 3.7 19.9 1.0
P B:G2 3.8 64.8 1.0
OH A:TYR21 4.0 26.4 1.0
OP2 B:G2 4.0 64.3 1.0
C5' B:G2 4.1 59.8 1.0
C A:GLY23 4.2 19.9 1.0
C A:GLY60 4.3 19.7 1.0
CB A:TYR61 4.3 19.4 1.0
CA A:GLY23 4.3 19.8 1.0
C2 B:G2 4.3 45.2 1.0
O A:LYS59 4.4 22.1 1.0
O5' B:G2 4.4 62.1 1.0
O B:HOH2001 4.4 44.0 1.0
N3 B:G2 4.5 46.6 1.0
CD2 A:TYR61 4.6 21.0 1.0
CB A:SER24 4.7 20.1 1.0
CG A:TYR61 4.8 19.4 1.0
C A:SER24 4.8 19.7 1.0
N A:ILE25 4.8 19.6 1.0
N A:TYR61 4.9 19.1 1.0
CA A:GLY60 4.9 20.3 1.0

Reference:

C.Pancevac, D.C.Goldstone, A.Ramos, I.A.Taylor. Structure of the RNA15 Rrm-Rna Complex Reveals the Molecular Basis of Gu Specificity in Transcriptional 3-End Processing Factors. Nucleic Acids Res. V. 38 3119 2010.
ISSN: ISSN 0305-1048
PubMed: 20097654
DOI: 10.1093/NAR/GKQ002
Page generated: Sun Aug 10 16:18:17 2025

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