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Magnesium in PDB 2azx: Charged and Uncharged Trnas Adopt Distinct Conformations When Complexed with Human Tryptophanyl-Trna Synthetase

Enzymatic activity of Charged and Uncharged Trnas Adopt Distinct Conformations When Complexed with Human Tryptophanyl-Trna Synthetase

All present enzymatic activity of Charged and Uncharged Trnas Adopt Distinct Conformations When Complexed with Human Tryptophanyl-Trna Synthetase:
6.1.1.2;

Protein crystallography data

The structure of Charged and Uncharged Trnas Adopt Distinct Conformations When Complexed with Human Tryptophanyl-Trna Synthetase, PDB code: 2azx was solved by X.L.Yang, F.J.Otero, K.L.Ewalt, J.Liu, M.A.Swairjo, C.Kohrer, U.L.Rajbhandary, R.J.Skene, D.E.Mcree, P.Schimmel, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 50.00 / 2.80
Space group I 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 114.058, 132.621, 246.633, 90.00, 90.00, 90.00
R / Rfree (%) 20.5 / 25.2

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Charged and Uncharged Trnas Adopt Distinct Conformations When Complexed with Human Tryptophanyl-Trna Synthetase (pdb code 2azx). 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 Charged and Uncharged Trnas Adopt Distinct Conformations When Complexed with Human Tryptophanyl-Trna Synthetase, PDB code: 2azx:

Magnesium binding site 1 out of 1 in 2azx

Go back to Magnesium Binding Sites List in 2azx
Magnesium binding site 1 out of 1 in the Charged and Uncharged Trnas Adopt Distinct Conformations When Complexed with Human Tryptophanyl-Trna Synthetase


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Charged and Uncharged Trnas Adopt Distinct Conformations When Complexed with Human Tryptophanyl-Trna Synthetase within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mg901

b:82.3
occ:1.00
 O B:ASP354 2.5 73.8 1.0
N B:SER358 2.7 54.4 1.0
OG B:SER358 2.7 49.3 1.0
N B:SER357 2.9 62.1 1.0
O B:SER351 3.0 63.0 1.0
CB B:SER357 3.2 59.4 1.0
O3 B:SO4705 3.3 0.1 1.0
CA B:SER357 3.3 59.1 1.0
C B:SER357 3.4 57.6 1.0
O4 B:SO4705 3.5 0.5 1.0
CB B:SER358 3.6 52.1 1.0
CA B:SER358 3.7 52.9 1.0
C B:ASP354 3.8 74.1 1.0
N B:ASN356 3.8 69.2 1.0
C B:ASN356 3.8 65.6 1.0
S B:SO4705 3.9 0.4 1.0
OG B:SER357 3.9 59.5 1.0
O B:ALA352 4.0 67.7 1.0
C B:SER351 4.0 63.7 1.0
C B:ALA352 4.1 67.2 1.0
CA B:ALA352 4.1 65.3 1.0
CA B:ASN356 4.3 67.6 1.0
C B:PRO355 4.3 70.9 1.0
O1 B:SO4705 4.3 0.2 1.0
CZ B:PHE360 4.4 50.2 1.0
CE2 B:PHE360 4.4 49.1 1.0
O B:SER358 4.4 54.4 1.0
N B:ALA352 4.5 64.0 1.0
CA B:PRO355 4.5 72.5 1.0
C B:SER358 4.5 52.5 1.0
N B:PRO355 4.6 73.5 1.0
O B:SER357 4.6 57.3 1.0
O B:SER353 4.6 76.4 1.0
C B:SER353 4.8 74.4 1.0
O B:ASN356 4.8 66.6 1.0
CA B:ASP354 4.8 74.8 1.0
N B:SER353 4.8 69.2 1.0
N B:ASP354 4.8 74.9 1.0
O B:PRO355 4.9 71.0 1.0

Reference:

X.L.Yang, F.J.Otero, K.L.Ewalt, J.Liu, M.A.Swairjo, C.Kohrer, U.L.Rajbhandary, R.J.Skene, D.E.Mcree, P.Schimmel. Two Conformations of A Crystalline Human Trna Synthetase-Trna Complex: Implications For Protein Synthesis. Embo J. V. 25 2919 2006.
ISSN: ISSN 0261-4189
PubMed: 16724112
DOI: 10.1038/SJ.EMBOJ.7601154
Page generated: Tue Aug 13 21:38:37 2024

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