Chlorine in PDB 4rrm: E129A Mutant of N-Terminal Editing Domain of Threonyl-Trna Synthetase From Aeropyrum Pernix with L-THR3AA

Enzymatic activity of E129A Mutant of N-Terminal Editing Domain of Threonyl-Trna Synthetase From Aeropyrum Pernix with L-THR3AA

All present enzymatic activity of E129A Mutant of N-Terminal Editing Domain of Threonyl-Trna Synthetase From Aeropyrum Pernix with L-THR3AA:
6.1.1.3;

Protein crystallography data

The structure of E129A Mutant of N-Terminal Editing Domain of Threonyl-Trna Synthetase From Aeropyrum Pernix with L-THR3AA, PDB code: 4rrm 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 (°) 47.091, 47.091, 112.729, 90.00, 90.00, 90.00
R / Rfree (%) 18.8 / 25.9

Other elements in 4rrm:

The structure of E129A Mutant of N-Terminal Editing Domain of Threonyl-Trna Synthetase From Aeropyrum Pernix with L-THR3AA also contains other interesting chemical elements:

Magnesium (Mg) 1 atom

Chlorine Binding Sites:

The binding sites of Chlorine atom in the E129A Mutant of N-Terminal Editing Domain of Threonyl-Trna Synthetase From Aeropyrum Pernix with L-THR3AA (pdb code 4rrm). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total only one binding site of Chlorine was determined in the E129A Mutant of N-Terminal Editing Domain of Threonyl-Trna Synthetase From Aeropyrum Pernix with L-THR3AA, PDB code: 4rrm:

Chlorine binding site 1 out of 1 in 4rrm

Go back to Chlorine Binding Sites List in 4rrm
Chlorine binding site 1 out of 1 in the E129A Mutant of N-Terminal Editing Domain of Threonyl-Trna Synthetase From Aeropyrum Pernix with L-THR3AA


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of E129A Mutant of N-Terminal Editing Domain of Threonyl-Trna Synthetase From Aeropyrum Pernix with L-THR3AA within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl503

b:27.3
occ:1.00
 O A:SER133 2.8 12.4 1.0
CE1 A:PHE134 3.4 12.2 1.0
CZ A:PHE134 3.8 11.3 1.0
N A:SER133 3.8 11.3 1.0
CD1 A:PHE134 3.8 11.5 1.0
C A:SER133 3.9 8.9 1.0
CD A:ARG132 4.0 15.0 1.0
CA A:SER133 4.5 9.9 1.0
CE2 A:PHE134 4.5 12.4 1.0
CB A:ARG132 4.5 10.5 1.0
CG A:PHE134 4.6 12.2 1.0
CA A:ARG132 4.7 10.1 1.0
C A:ARG132 4.7 11.2 1.0
CD2 A:PHE134 4.8 9.6 1.0
CG A:ARG132 4.9 11.5 1.0
N A:PHE134 4.9 9.8 1.0
NE A:ARG132 4.9 16.6 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: Sat Dec 12 11:12:04 2020

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