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Magnesium in PDB 4rr7: N-Terminal Editing Domain of Threonyl-Trna Synthetase From Aeropyrum Pernix with L-SER3AA (Snapshot 2)

Enzymatic activity of N-Terminal Editing Domain of Threonyl-Trna Synthetase From Aeropyrum Pernix with L-SER3AA (Snapshot 2)

All present enzymatic activity of N-Terminal Editing Domain of Threonyl-Trna Synthetase From Aeropyrum Pernix with L-SER3AA (Snapshot 2):
6.1.1.3;

Protein crystallography data

The structure of N-Terminal Editing Domain of Threonyl-Trna Synthetase From Aeropyrum Pernix with L-SER3AA (Snapshot 2), PDB code: 4rr7 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 (°) 47.846, 47.846, 114.709, 90.00, 90.00, 90.00
R / Rfree (%) 19 / 23.7

Magnesium Binding Sites:

The binding sites of Magnesium atom in the N-Terminal Editing Domain of Threonyl-Trna Synthetase From Aeropyrum Pernix with L-SER3AA (Snapshot 2) (pdb code 4rr7). 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-SER3AA (Snapshot 2), PDB code: 4rr7:

Magnesium binding site 1 out of 1 in 4rr7

Go back to Magnesium Binding Sites List in 4rr7
Magnesium binding site 1 out of 1 in the N-Terminal Editing Domain of Threonyl-Trna Synthetase From Aeropyrum Pernix with L-SER3AA (Snapshot 2)


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-SER3AA (Snapshot 2) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg202

b:67.1
occ:1.00
 O A:HOH409 2.1 33.5 1.0
O A:HOH381 2.5 46.0 1.0
O A:HOH435 2.9 38.4 1.0
O A:HOH415 3.6 39.0 1.0
OE2 A:GLU29 4.4 38.0 1.0
O A:THR15 4.4 27.4 1.0
O A:HOH322 4.5 32.5 1.0
OG1 A:THR15 4.6 31.0 1.0
O A:HOH383 4.7 38.4 1.0
O A:GLY28 4.8 33.5 1.0
C A:GLY28 4.9 32.2 1.0
N A:GLY28 4.9 34.4 1.0
CA A:GLY28 4.9 31.2 1.0
O A:HOH382 4.9 46.3 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: Tue Aug 20 03:17:28 2024

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