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Magnesium in PDB 2j7k: Crystal Structure of the T84A Mutant Ef-G:Gdpcp Complex

Enzymatic activity of Crystal Structure of the T84A Mutant Ef-G:Gdpcp Complex

All present enzymatic activity of Crystal Structure of the T84A Mutant Ef-G:Gdpcp Complex:
3.6.1.48;

Protein crystallography data

The structure of Crystal Structure of the T84A Mutant Ef-G:Gdpcp Complex, PDB code: 2j7k was solved by S.Hansson, D.T.Logan, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 26.00 / 2.9
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 77.230, 88.680, 114.900, 90.00, 90.00, 90.00
R / Rfree (%) 22.6 / 28.8

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Crystal Structure of the T84A Mutant Ef-G:Gdpcp Complex (pdb code 2j7k). 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 T84A Mutant Ef-G:Gdpcp Complex, PDB code: 2j7k:

Magnesium binding site 1 out of 1 in 2j7k

Go back to Magnesium Binding Sites List in 2j7k
Magnesium binding site 1 out of 1 in the Crystal Structure of the T84A Mutant Ef-G:Gdpcp Complex


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 T84A Mutant Ef-G:Gdpcp Complex within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg950

b:45.7
occ:1.00
OG1 A:THR26 2.2 52.5 1.0
O2G A:GCP900 2.3 61.3 1.0
O2B A:GCP900 2.8 56.0 1.0
CB A:THR26 3.6 52.4 1.0
PG A:GCP900 3.7 61.0 1.0
PB A:GCP900 4.0 57.3 1.0
O2A A:GCP900 4.1 56.6 1.0
CG2 A:THR26 4.2 52.0 1.0
C3B A:GCP900 4.2 59.0 1.0
O3G A:GCP900 4.4 61.4 1.0
CE A:LYS25 4.5 55.6 1.0
CA A:THR26 4.6 52.5 1.0
N A:THR26 4.6 53.1 1.0
O1G A:GCP900 4.8 61.1 1.0

Reference:

S.Hansson, D.T.Logan. New Insights Into the Role of the P-Loop Lysine: Implications From the Crystal Structure of A Mutant Ef-G:Gdpcp Complex To Be Published.
Page generated: Wed Aug 14 00:38:46 2024

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