Magnesium in PDB 1duh: Crystal Structure of the Conserved Domain IV of E. Coli 4.5S Rna

The structure of Crystal Structure of the Conserved Domain IV of E. Coli 4.5S Rna, PDB code: 1duh was solved by L.Jovine, T.Hainzl, C.Oubridge, W.G.Scott, J.Li, T.K.Sixma, A.Wonacott, T.Skarzynski, K.Nagai, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	22.50 / 2.70
Space group	P 32 2 1
Cell size a, b, c (Å), α, β, γ (°)	69.697, 69.697, 84.102, 90.00, 90.00, 120.00
R / Rfree (%)	23 / 24.5

The structure of Crystal Structure of the Conserved Domain IV of E. Coli 4.5S Rna also contains other interesting chemical elements:

Lutetium

(Lu)

1 atom

The binding sites of Magnesium atom in the Crystal Structure of the Conserved Domain IV of E. Coli 4.5S Rna (pdb code 1duh). 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 of the Conserved Domain IV of E. Coli 4.5S Rna, PDB code: 1duh:

Magnesium binding site 1 out of 1 in the Crystal Structure of the Conserved Domain IV of E. Coli 4.5S Rna


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 the Conserved Domain IV of E. Coli 4.5S Rna within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg2 b:73.6 occ:1.00 O3' A:A59 1.9 94.3 1.0 OP1 A:A60 2.7 96.3 1.0 P A:A60 2.8 97.4 1.0 C5' A:A60 3.1 80.5 1.0 C3' A:A59 3.1 91.3 1.0 O5' A:A60 3.4 89.8 1.0 O2' A:A59 3.5 89.8 1.0 C4' A:A59 3.5 90.1 1.0 C2' A:A59 3.8 89.8 1.0 OP2 A:A60 4.1 97.0 1.0 C5' A:A59 4.2 92.0 1.0 C4' A:A60 4.4 76.3 1.0 O4' A:A60 4.7 75.2 1.0 O4' A:A59 4.8 88.6 1.0 C1' A:A59 5.0 86.1 1.0

L.Jovine, T.Hainzl, C.Oubridge, W.G.Scott, J.Li, T.K.Sixma, A.Wonacott, T.Skarzynski, K.Nagai. Crystal Structure of the Ffh and Ef-G Binding Sites in the Conserved Domain IV of Escherichia Coli 4.5S Rna. Structure Fold.Des. V. 8 527 2000.
ISSN: ISSN 0969-2126
PubMed: 10801497
DOI: 10.1016/S0969-2126(00)00137-4