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Chlorine in PDB 5mi8: Structure of the Phosphomimetic Mutant of Ef-Tu T383E

Protein crystallography data

The structure of Structure of the Phosphomimetic Mutant of Ef-Tu T383E, PDB code: 5mi8 was solved by A.Talavera, J.Hendrix, W.Versees, S.De Gieter, D.Castro-Roa, D.Jurenas, K.Van Nerom, N.Vandenberk, A.Barth, H.De Greve, J.Hofkens, N.Zenkin, R.Loris, A.Garcia-Pino, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 52.75 / 2.18
Space group P 1
Cell size a, b, c (Å), α, β, γ (°) 55.870, 61.510, 65.040, 71.53, 71.17, 87.76
R / Rfree (%) 18.7 / 22.5

Other elements in 5mi8:

The structure of Structure of the Phosphomimetic Mutant of Ef-Tu T383E also contains other interesting chemical elements:

Magnesium (Mg) 4 atoms

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Structure of the Phosphomimetic Mutant of Ef-Tu T383E (pdb code 5mi8). 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 Structure of the Phosphomimetic Mutant of Ef-Tu T383E, PDB code: 5mi8:

Chlorine binding site 1 out of 1 in 5mi8

Go back to Chlorine Binding Sites List in 5mi8
Chlorine binding site 1 out of 1 in the Structure of the Phosphomimetic Mutant of Ef-Tu T383E


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Structure of the Phosphomimetic Mutant of Ef-Tu T383E within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cl406

b:89.8
occ:1.00
OG1 B:THR74 2.9 53.5 1.0
N B:THR74 3.0 52.5 1.0
OD2 B:ASP197 3.1 69.2 1.0
CD B:PRO73 3.4 51.3 1.0
OG1 B:THR72 3.4 40.9 1.0
N B:PRO73 3.5 50.6 1.0
CG B:ASP197 3.5 58.7 1.0
CB B:THR74 3.6 61.2 1.0
CB B:THR72 3.6 43.6 1.0
CA B:THR74 3.8 53.1 1.0
OD1 B:ASP197 3.9 56.5 1.0
CG2 B:THR74 3.9 61.5 1.0
C B:PRO73 3.9 57.2 1.0
CB B:PRO73 4.0 53.7 1.0
CA B:PRO73 4.0 52.2 1.0
C B:THR72 4.0 52.4 1.0
O B:HOH520 4.1 70.4 1.0
CG B:PRO73 4.1 57.3 1.0
CB B:ASP197 4.3 46.9 1.0
CA B:THR72 4.4 46.0 1.0
N B:ARG75 4.4 54.0 1.0
C B:THR74 4.6 56.0 1.0
O B:THR72 4.7 51.0 1.0
CG2 B:THR72 4.8 38.7 1.0

Reference:

A.Talavera, J.Hendrix, W.Versees, D.Jurenas, K.Van Nerom, N.Vandenberk, R.K.Singh, A.Konijnenberg, S.De Gieter, D.Castro-Roa, A.Barth, H.De Greve, F.Sobott, J.Hofkens, N.Zenkin, R.Loris, A.Garcia-Pino. Phosphorylation Decelerates Conformational Dynamics in Bacterial Translation Elongation Factors. Sci Adv V. 4 P9714 2018.
ISSN: ESSN 2375-2548
PubMed: 29546243
DOI: 10.1126/SCIADV.AAP9714
Page generated: Sat Dec 12 12:06:20 2020

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