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Magnesium in PDB 3omy: Crystal Structure of the PED208 Tram N-Terminal Domain

Protein crystallography data

The structure of Crystal Structure of the PED208 Tram N-Terminal Domain, PDB code: 3omy was solved by J.J.W.Wong, J.Lu, R.A.Edwards, L.S.Frost, J.N.Mark Glover, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 42.14 / 1.30
Space group P 41 21 2
Cell size a, b, c (Å), α, β, γ (°) 54.069, 54.069, 67.268, 90.00, 90.00, 90.00
R / Rfree (%) 15 / 17.3

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Crystal Structure of the PED208 Tram N-Terminal Domain (pdb code 3omy). 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 PED208 Tram N-Terminal Domain, PDB code: 3omy:

Magnesium binding site 1 out of 1 in 3omy

Go back to Magnesium Binding Sites List in 3omy
Magnesium binding site 1 out of 1 in the Crystal Structure of the PED208 Tram N-Terminal Domain


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 PED208 Tram N-Terminal Domain within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mg53

b:24.4
occ:1.00
O B:HOH61 2.6 30.0 1.0
O B:HOH78 2.8 16.7 1.0
OD1 B:ASN35 2.8 2.8 1.0
CA B:ALA31 3.6 2.5 1.0
CG B:ASN35 3.7 3.1 1.0
CB B:ALA31 3.7 3.3 1.0
CG2 B:VAL36 3.8 3.9 1.0
CG2 B:ILE28 3.9 5.0 1.0
ND2 B:ASN35 4.3 4.1 1.0
O B:HOH164 4.3 42.9 1.0
N B:ALA31 4.3 2.4 1.0
N B:VAL36 4.4 2.2 1.0
C B:ASN35 4.5 2.6 1.0
CB B:ASN35 4.6 3.4 1.0
N B:SER32 4.6 2.5 1.0
CA B:VAL36 4.6 2.6 1.0
O B:ASN35 4.7 3.4 1.0
C B:ALA31 4.7 2.4 1.0
CB B:VAL36 4.9 2.6 1.0
C B:GLU30 4.9 2.6 1.0
O B:GLU30 4.9 3.3 1.0
OE1 B:GLU30 5.0 10.2 0.5

Reference:

J.J.Wong, J.Lu, R.A.Edwards, L.S.Frost, J.N.Glover. Structural Basis of Cooperative Dna Recognition By the Plasmid Conjugation Factor, Tram. Nucleic Acids Res. V. 39 6775 2011.
ISSN: ISSN 0305-1048
PubMed: 21565799
DOI: 10.1093/NAR/GKR296
Page generated: Mon Aug 11 01:15:13 2025

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