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Magnesium in PDB 2bv3: Crystal Structure of A Mutant Elongation Factor G Trapped with A Gtp Analogue

Protein crystallography data

The structure of Crystal Structure of A Mutant Elongation Factor G Trapped with A Gtp Analogue, PDB code: 2bv3 was solved by S.Hansson, R.Singh, A.T.Gudkov, A.Liljas, D.T.Logan, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 17.43 / 2.50
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 74.990, 103.340, 118.910, 90.00, 90.00, 90.00
R / Rfree (%) 20.2 / 27

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Crystal Structure of A Mutant Elongation Factor G Trapped with A Gtp Analogue (pdb code 2bv3). 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 A Mutant Elongation Factor G Trapped with A Gtp Analogue, PDB code: 2bv3:

Magnesium binding site 1 out of 1 in 2bv3

Go back to Magnesium Binding Sites List in 2bv3
Magnesium binding site 1 out of 1 in the Crystal Structure of A Mutant Elongation Factor G Trapped with A Gtp Analogue


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 A Mutant Elongation Factor G Trapped with A Gtp Analogue within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg1690

b:69.0
occ:1.00
O1G A:GNP1689 1.9 89.0 0.8
OG1 A:THR26 2.4 46.2 1.0
O2B A:GNP1689 2.4 71.3 0.8
PG A:GNP1689 2.9 86.3 0.8
N3B A:GNP1689 3.0 72.4 0.8
CB A:THR26 3.3 43.8 1.0
PB A:GNP1689 3.4 63.0 0.8
O1A A:GNP1689 3.5 53.9 0.8
O3G A:GNP1689 3.5 77.2 0.8
O2G A:GNP1689 4.1 80.7 0.8
CG2 A:THR26 4.2 45.1 1.0
PA A:GNP1689 4.2 53.3 0.8
O3A A:GNP1689 4.3 53.3 0.8
O1B A:GNP1689 4.5 52.7 0.8
CA A:THR26 4.5 48.0 1.0
O2A A:GNP1689 4.5 43.8 0.8
N A:THR26 4.5 41.3 1.0

Reference:

S.Hansson, R.Singh, A.T.Gudkov, A.Liljas, D.T.Logan. Crystal Structure of A Mutant Elongation Factor G Trapped with A Gtp Analogue. Febs Lett. V. 579 4492 2005.
ISSN: ISSN 0014-5793
PubMed: 16083884
DOI: 10.1016/J.FEBSLET.2005.07.016
Page generated: Mon Dec 14 07:17:40 2020

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