Magnesium in PDB 4rrd: N-Terminal Editing Domain of Threonyl-Trna Synthetase From Aeropyrum Pernix with L-THR3AA (Snapshot 4)

Enzymatic activity of N-Terminal Editing Domain of Threonyl-Trna Synthetase From Aeropyrum Pernix with L-THR3AA (Snapshot 4)

All present enzymatic activity of N-Terminal Editing Domain of Threonyl-Trna Synthetase From Aeropyrum Pernix with L-THR3AA (Snapshot 4):
6.1.1.3;

Protein crystallography data

The structure of N-Terminal Editing Domain of Threonyl-Trna Synthetase From Aeropyrum Pernix with L-THR3AA (Snapshot 4), PDB code: 4rrd was solved by S.Ahmad, S.Muthukumar, A.S.K.Yerabham, V.Kamarthapu, R.Sankaranarayanan, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 25.00 / 1.86
Space group P 41 21 2
Cell size a, b, c (Å), α, β, γ (°) 47.532, 47.532, 113.556, 90.00, 90.00, 90.00
R / Rfree (%) 17.8 / 21.5

Magnesium Binding Sites:

The binding sites of Magnesium atom in the N-Terminal Editing Domain of Threonyl-Trna Synthetase From Aeropyrum Pernix with L-THR3AA (Snapshot 4) (pdb code 4rrd). 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 N-Terminal Editing Domain of Threonyl-Trna Synthetase From Aeropyrum Pernix with L-THR3AA (Snapshot 4), PDB code: 4rrd:

Magnesium binding site 1 out of 1 in 4rrd

Go back to Magnesium Binding Sites List in 4rrd
Magnesium binding site 1 out of 1 in the N-Terminal Editing Domain of Threonyl-Trna Synthetase From Aeropyrum Pernix with L-THR3AA (Snapshot 4)


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of N-Terminal Editing Domain of Threonyl-Trna Synthetase From Aeropyrum Pernix with L-THR3AA (Snapshot 4) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg502

b:32.0
occ:1.00
 O A:HOH722 2.2 27.7 1.0
O A:HOH630 2.2 29.7 1.0
O A:HOH621 2.3 26.8 1.0
O A:HOH653 4.2 33.3 1.0
OE2 A:GLU29 4.2 30.5 1.0
O A:THR15 4.3 24.4 1.0
O A:HOH607 4.6 26.2 1.0
O A:GLY28 4.8 30.8 1.0
O A:HOH661 4.8 35.7 1.0
OG1 A:THR15 4.8 27.9 1.0
C A:GLY28 4.9 26.4 1.0
CA A:GLY28 5.0 28.5 1.0

Reference:

S.Ahmad, S.Muthukumar, S.K.Kuncha, S.B.Routh, A.S.Yerabham, T.Hussain, V.Kamarthapu, S.P.Kruparani, R.Sankaranarayanan. Specificity and Catalysis Hardwired at the Rna-Protein Interface in A Translational Proofreading Enzyme. Nat Commun V. 6 7552 2015.
ISSN: ESSN 2041-1723
PubMed: 26113036
DOI: 10.1038/NCOMMS8552
Page generated: Mon Dec 14 19:31:59 2020

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