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Magnesium in PDB 3shs: Three N-Terminal Domains of the Bacteriophage RB49 Highly Immunogenic Outer Capsid Protein (Hoc)

Protein crystallography data

The structure of Three N-Terminal Domains of the Bacteriophage RB49 Highly Immunogenic Outer Capsid Protein (Hoc), PDB code: 3shs was solved by A.Fokine, M.Z.Islam, Z.Zhang, V.D.Bowman, V.B.Rao, M.G.Rossmann, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 27.69 / 1.95
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 213.540, 36.731, 62.693, 90.00, 99.28, 90.00
R / Rfree (%) 21.8 / 26.7

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Three N-Terminal Domains of the Bacteriophage RB49 Highly Immunogenic Outer Capsid Protein (Hoc) (pdb code 3shs). 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 Three N-Terminal Domains of the Bacteriophage RB49 Highly Immunogenic Outer Capsid Protein (Hoc), PDB code: 3shs:

Magnesium binding site 1 out of 1 in 3shs

Go back to Magnesium Binding Sites List in 3shs
Magnesium binding site 1 out of 1 in the Three N-Terminal Domains of the Bacteriophage RB49 Highly Immunogenic Outer Capsid Protein (Hoc)


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Three N-Terminal Domains of the Bacteriophage RB49 Highly Immunogenic Outer Capsid Protein (Hoc) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg305

b:68.8
occ:1.00
CE1 A:HIS113 2.6 73.5 1.0
NE2 A:HIS113 2.9 69.7 1.0
OE1 A:GLU111 3.5 80.8 1.0
ND1 A:HIS113 3.9 72.2 1.0
CD2 A:HIS113 4.3 60.7 1.0
CD A:GLU111 4.4 72.7 1.0
CG A:HIS113 4.7 60.2 1.0
OE2 A:GLU111 4.8 74.5 1.0
OD2 A:ASP146 4.9 71.0 1.0

Reference:

A.Fokine, M.Z.Islam, Z.Zhang, V.D.Bowman, V.B.Rao, M.G.Rossmann. Structure of the Three N-Terminal Immunoglobulin Domains of the Highly Immunogenic Outer Capsid Protein From A T4-Like Bacteriophage. J.Virol. V. 85 8141 2011.
ISSN: ISSN 0022-538X
PubMed: 21632759
DOI: 10.1128/JVI.00847-11
Page generated: Thu Aug 15 10:58:44 2024

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