Magnesium in PDB 4rrh: K116M Mutant of N-Terminal Editing Domain of Threonyl-Trna Synthetase From Aeropyrum Pernix with L-SER3AA

Enzymatic activity of K116M Mutant of N-Terminal Editing Domain of Threonyl-Trna Synthetase From Aeropyrum Pernix with L-SER3AA

All present enzymatic activity of K116M Mutant of N-Terminal Editing Domain of Threonyl-Trna Synthetase From Aeropyrum Pernix with L-SER3AA:
6.1.1.3;

Protein crystallography data

The structure of K116M Mutant of N-Terminal Editing Domain of Threonyl-Trna Synthetase From Aeropyrum Pernix with L-SER3AA, PDB code: 4rrh was solved by S.Ahmad, S.Muthukumar, R.Sankaranarayanan, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 25.00 / 1.55
Space group P 41 21 2
Cell size a, b, c (Å), α, β, γ (°) 47.161, 47.161, 113.006, 90.00, 90.00, 90.00
R / Rfree (%) 20.4 / 23.3

Magnesium Binding Sites:

The binding sites of Magnesium atom in the K116M Mutant of N-Terminal Editing Domain of Threonyl-Trna Synthetase From Aeropyrum Pernix with L-SER3AA (pdb code 4rrh). 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 K116M Mutant of N-Terminal Editing Domain of Threonyl-Trna Synthetase From Aeropyrum Pernix with L-SER3AA, PDB code: 4rrh:

Magnesium binding site 1 out of 1 in 4rrh

Go back to Magnesium Binding Sites List in 4rrh
Magnesium binding site 1 out of 1 in the K116M Mutant of N-Terminal Editing Domain of Threonyl-Trna Synthetase From Aeropyrum Pernix with L-SER3AA


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of K116M Mutant of N-Terminal Editing Domain of Threonyl-Trna Synthetase From Aeropyrum Pernix with L-SER3AA within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg202

b:21.8
occ:1.00
 O A:HOH318 2.0 15.8 1.0
O A:HOH368 2.2 23.0 1.0
O A:HOH310 2.2 20.8 1.0
O A:HOH326 2.3 21.8 1.0
O A:HOH341 4.0 27.6 1.0
O A:THR15 4.2 17.9 1.0
OE1 A:GLU29 4.2 24.4 1.0
O A:HOH304 4.2 18.0 1.0
O A:GLY28 4.6 17.2 1.0
OG1 A:THR15 4.6 14.0 1.0
C A:GLY28 4.9 16.6 1.0
O A:HOH382 4.9 41.0 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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