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Chlorine in PDB 5i4q: Contact-Dependent Inhibition System From Escherichia Coli NC101 - Ternary Cdia/Cdii/Ef-Tu Complex (Domains 2 and 3)

Protein crystallography data

The structure of Contact-Dependent Inhibition System From Escherichia Coli NC101 - Ternary Cdia/Cdii/Ef-Tu Complex (Domains 2 and 3), PDB code: 5i4q was solved by K.Michalska, L.Stols, W.Eschenfeldt, C.S.Hayes, C.W.Goulding, A.Joachimiak, Midwest Center For Structural Genomics (Mcsg), Structure-Function Analysis Of Polymorphic Cdi Toxin-Immunityprotein Complexes (Uc4Cdi), with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 30.00 / 2.35
Space group P 4 21 2
Cell size a, b, c (Å), α, β, γ (°) 131.155, 131.155, 63.327, 90.00, 90.00, 90.00
R / Rfree (%) 18.1 / 21.8

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Contact-Dependent Inhibition System From Escherichia Coli NC101 - Ternary Cdia/Cdii/Ef-Tu Complex (Domains 2 and 3) (pdb code 5i4q). 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 Contact-Dependent Inhibition System From Escherichia Coli NC101 - Ternary Cdia/Cdii/Ef-Tu Complex (Domains 2 and 3), PDB code: 5i4q:

Chlorine binding site 1 out of 1 in 5i4q

Go back to Chlorine Binding Sites List in 5i4q
Chlorine binding site 1 out of 1 in the Contact-Dependent Inhibition System From Escherichia Coli NC101 - Ternary Cdia/Cdii/Ef-Tu Complex (Domains 2 and 3)


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Contact-Dependent Inhibition System From Escherichia Coli NC101 - Ternary Cdia/Cdii/Ef-Tu Complex (Domains 2 and 3) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl301

b:74.0
occ:1.00
N A:ALA233 3.5 39.6 1.0
CA A:ALA233 4.2 40.9 1.0
CA A:GLY232 4.3 39.2 1.0
O A:SER213 4.4 48.4 1.0
C A:GLY232 4.4 37.7 1.0
O A:HOH416 4.4 59.2 1.0
CB A:SER213 4.6 43.4 1.0
NH1 C:ARG224 4.8 81.3 1.0
OG A:SER213 4.9 41.3 1.0
N A:GLY234 5.0 41.0 1.0

Reference:

K.Michalska, G.C.Gucinski, F.Garza-Sanchez, P.M.Johnson, L.M.Stols, W.H.Eschenfeldt, G.Babnigg, D.A.Low, C.W.Goulding, A.Joachimiak, C.S.Hayes. Structure of A Novel Antibacterial Toxin That Exploits Elongation Factor Tu to Cleave Specific Transfer Rnas. Nucleic Acids Res. V. 45 10306 2017.
ISSN: ESSN 1362-4962
PubMed: 28973472
DOI: 10.1093/NAR/GKX700
Page generated: Fri Jul 26 09:08:40 2024

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