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Magnesium in PDB 1dou: Monovalent Cations Sequester Within the A-Tract Minor Groove of [D(Cgcgaattcgcg)]2

Protein crystallography data

The structure of Monovalent Cations Sequester Within the A-Tract Minor Groove of [D(Cgcgaattcgcg)]2, PDB code: 1dou was solved by K.K.Woods, L.Mcfail-Isom, C.C.Sines, S.B.Howerton, R.K.Stephens, L.D.Williams, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 10.00 / 1.82
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 25.296, 40.243, 65.939, 90.00, 90.00, 90.00
R / Rfree (%) 20.9 / 26.7

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Monovalent Cations Sequester Within the A-Tract Minor Groove of [D(Cgcgaattcgcg)]2 (pdb code 1dou). 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 Monovalent Cations Sequester Within the A-Tract Minor Groove of [D(Cgcgaattcgcg)]2, PDB code: 1dou:

Magnesium binding site 1 out of 1 in 1dou

Go back to Magnesium Binding Sites List in 1dou
Magnesium binding site 1 out of 1 in the Monovalent Cations Sequester Within the A-Tract Minor Groove of [D(Cgcgaattcgcg)]2


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Monovalent Cations Sequester Within the A-Tract Minor Groove of [D(Cgcgaattcgcg)]2 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg25

b:12.7
occ:1.00
O B:HOH305 2.0 12.2 1.0
O B:HOH307 2.2 12.2 1.0
O B:HOH308 2.2 13.1 1.0
O A:HOH306 2.2 12.7 1.0
O A:HOH303 2.3 12.6 1.0
O A:HOH304 2.4 15.1 1.0
O B:HOH106 3.7 10.2 1.0
O B:HOH113 4.0 22.0 1.0
O A:HOH117 4.1 11.9 1.0
O6 B:DG22 4.2 9.3 1.0
O6 A:DG2 4.4 4.7 1.0
N7 A:DG2 4.5 10.6 1.0
C5 A:DC1 4.5 2.5 1.0
C6 A:DC1 5.0 6.5 1.0

Reference:

K.K.Woods, L.Mcfail-Isom, C.C.Sines, S.B.Howerton, R.K.Stephens, L.D.Williams. Monovalent Cations Sequester Within the A-Tract Minor Groove of [D(Cgcgaattcgcg)]2 J.Am.Chem.Soc. V. 122 1546 2000.
ISSN: ISSN 0002-7863
DOI: 10.1021/JA9919579
Page generated: Mon Dec 14 05:50:35 2020

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