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Magnesium in PDB 2fii: Crystal Structure Analysis of the B-Dna Dodecamer Cgcgaat-Au-Cgcg, with Incorporated Arabino-Uridin (Au)

Protein crystallography data

The structure of Crystal Structure Analysis of the B-Dna Dodecamer Cgcgaat-Au-Cgcg, with Incorporated Arabino-Uridin (Au), PDB code: 2fii was solved by M.Egli, F.Li, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 30.00 / 1.24
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 25.699, 39.915, 65.564, 90.00, 90.00, 90.00
R / Rfree (%) 15.5 / 21.2

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Crystal Structure Analysis of the B-Dna Dodecamer Cgcgaat-Au-Cgcg, with Incorporated Arabino-Uridin (Au) (pdb code 2fii). 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 Crystal Structure Analysis of the B-Dna Dodecamer Cgcgaat-Au-Cgcg, with Incorporated Arabino-Uridin (Au), PDB code: 2fii:

Magnesium binding site 1 out of 1 in 2fii

Go back to Magnesium Binding Sites List in 2fii
Magnesium binding site 1 out of 1 in the Crystal Structure Analysis of the B-Dna Dodecamer Cgcgaat-Au-Cgcg, with Incorporated Arabino-Uridin (Au)


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Crystal Structure Analysis of the B-Dna Dodecamer Cgcgaat-Au-Cgcg, with Incorporated Arabino-Uridin (Au) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg310

b:20.8
occ:1.00
O A:HOH205 2.1 21.4 1.0
O B:HOH206 2.1 23.2 1.0
O A:HOH204 2.1 23.2 1.0
O B:HOH349 4.1 23.9 1.0
O A:HOH336 4.2 32.0 1.0
O6 B:DG122 4.2 20.5 1.0
N7 A:DG2 4.4 19.5 1.0
C5 A:DC1 4.4 21.5 1.0
O B:HOH330 4.4 26.3 1.0
O6 A:DG2 4.4 20.0 1.0
C6 A:DC1 4.7 21.0 1.0
O B:HOH331 5.0 42.0 1.0

Reference:

F.Li, S.Sarkhel, C.J.Wilds, Z.Wawrzak, T.P.Prakash, M.Manoharan, M.Egli. 2'-Fluoroarabino- and Arabinonucleic Acid Show Different Conformations, Resulting in Deviating Rna Affinities and Processing of Their Heteroduplexes with Rna By Rnase H. Biochemistry V. 45 4141 2006.
ISSN: ISSN 0006-2960
PubMed: 16566588
DOI: 10.1021/BI052322R
Page generated: Tue Aug 13 23:07:35 2024

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