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Magnesium in PDB 4rr9: N-Terminal Editing Domain of Threonyl-Trna Synthetase From Aeropyrum Pernix with L-SER3AA (Snapshot 4)

Enzymatic activity of N-Terminal Editing Domain of Threonyl-Trna Synthetase From Aeropyrum Pernix with L-SER3AA (Snapshot 4)

All present enzymatic activity of N-Terminal Editing Domain of Threonyl-Trna Synthetase From Aeropyrum Pernix with L-SER3AA (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-SER3AA (Snapshot 4), PDB code: 4rr9 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 / 1.67
Space group P 41 21 2
Cell size a, b, c (Å), α, β, γ (°) 47.871, 47.871, 113.740, 90.00, 90.00, 90.00
R / Rfree (%) 19.6 / 22.5

Magnesium Binding Sites:

The binding sites of Magnesium atom in the N-Terminal Editing Domain of Threonyl-Trna Synthetase From Aeropyrum Pernix with L-SER3AA (Snapshot 4) (pdb code 4rr9). 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 4), PDB code: 4rr9:

Magnesium binding site 1 out of 1 in 4rr9

Go back to Magnesium Binding Sites List in 4rr9
Magnesium binding site 1 out of 1 in the N-Terminal Editing Domain of Threonyl-Trna Synthetase From Aeropyrum Pernix with L-SER3AA (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-SER3AA (Snapshot 4) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg202

b:32.5
occ:1.00
 O A:HOH366 2.1 32.3 1.0
O A:HOH323 2.1 29.9 1.0
O A:HOH341 2.1 27.8 1.0
O A:HOH379 2.2 35.4 1.0
O A:HOH370 2.2 29.8 1.0
O A:HOH376 2.3 30.2 1.0
OE2 A:GLU29 4.1 32.7 1.0
O A:HOH347 4.2 28.8 1.0
O A:THR15 4.2 23.9 1.0
O A:HOH465 4.2 39.2 1.0
O A:HOH312 4.5 27.2 1.0
O A:GLY28 4.8 27.5 1.0
OG1 A:THR15 4.9 24.2 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 03:17:41 2024

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