Atomistry » Magnesium » PDB 4rkq-4rri » 4rr8
Atomistry »
  Magnesium »
    PDB 4rkq-4rri »
      4rr8 »

Magnesium in PDB 4rr8: N-Terminal Editing Domain of Threonyl-Trna Synthetase From Aeropyrum Pernix with L-SER3AA (Snapshot 3)

Enzymatic activity of N-Terminal Editing Domain of Threonyl-Trna Synthetase From Aeropyrum Pernix with L-SER3AA (Snapshot 3)

All present enzymatic activity of N-Terminal Editing Domain of Threonyl-Trna Synthetase From Aeropyrum Pernix with L-SER3AA (Snapshot 3):
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 3), PDB code: 4rr8 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 (°) 47.824, 47.824, 114.346, 90.00, 90.00, 90.00
R / Rfree (%) 18.2 / 22.6

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 3) (pdb code 4rr8). 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 3), PDB code: 4rr8:

Magnesium binding site 1 out of 1 in 4rr8

Go back to Magnesium Binding Sites List in 4rr8
Magnesium binding site 1 out of 1 in the N-Terminal Editing Domain of Threonyl-Trna Synthetase From Aeropyrum Pernix with L-SER3AA (Snapshot 3)


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 3) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg202

b:46.8
occ:1.00
 O A:HOH324 2.1 30.7 1.0
O A:HOH351 2.2 32.1 1.0
O A:HOH401 2.3 43.3 1.0
O A:HOH380 2.3 41.0 1.0
O A:HOH366 2.3 44.0 1.0
O A:HOH374 2.4 36.4 1.0
O A:HOH457 4.0 48.1 1.0
OE2 A:GLU29 4.0 37.1 1.0
O A:HOH348 4.1 38.2 1.0
O A:THR15 4.3 26.8 1.0
O A:HOH391 4.6 44.7 1.0
O A:GLY28 4.7 31.6 1.0
O A:HOH304 4.8 29.7 1.0
OG1 A:THR15 4.9 27.1 1.0
CD A:GLU29 5.0 33.9 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 Aug 11 23:27:51 2025

Last articles

Mg in 5NLM
Mg in 5NMX
Mg in 5NMW
Mg in 5NH7
Mg in 5NKL
Mg in 5NM5
Mg in 5NKK
Mg in 5NIF
Mg in 5NJU
Mg in 5NJH
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy