Chlorine in PDB 6bar: Crystal Structure of Thermus Thermophilus Rod Shape Determining Protein Roda (Q5SIX3_THET8)

The structure of Crystal Structure of Thermus Thermophilus Rod Shape Determining Protein Roda (Q5SIX3_THET8), PDB code: 6bar was solved by M.Sjodt, K.Brock, G.Dobihal, P.D.A.Rohs, A.G.Green, T.A.Hopf, A.J.Meeske, D.S.Marks, T.G.Bernhardt, D.Z.Rudner, A.C.Kruse, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	40.01 / 2.91
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	122.405, 80.012, 47.827, 90.00, 91.06, 90.00
R / Rfree (%)	22.9 / 27.4

The binding sites of Chlorine atom in the Crystal Structure of Thermus Thermophilus Rod Shape Determining Protein Roda (Q5SIX3_THET8) (pdb code 6bar). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 2 binding sites of Chlorine where determined in the Crystal Structure of Thermus Thermophilus Rod Shape Determining Protein Roda (Q5SIX3_THET8), PDB code: 6bar:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in the Crystal Structure of Thermus Thermophilus Rod Shape Determining Protein Roda (Q5SIX3_THET8)


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Crystal Structure of Thermus Thermophilus Rod Shape Determining Protein Roda (Q5SIX3_THET8) within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl403 b:0.7 occ:1.00 NH1 A:ARG283 3.5 0.8 1.0 CA A:GLY14 3.8 0.8 1.0 N A:GLY14 4.0 0.8 1.0 NH2 A:ARG283 4.1 0.6 1.0 CZ A:ARG283 4.2 0.5 1.0

Chlorine binding site 2 out of 2 in the Crystal Structure of Thermus Thermophilus Rod Shape Determining Protein Roda (Q5SIX3_THET8)


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Crystal Structure of Thermus Thermophilus Rod Shape Determining Protein Roda (Q5SIX3_THET8) within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl404 b:0.2 occ:1.00 NE A:ARG175 3.1 0.7 1.0 CD A:ARG175 3.2 0.4 1.0 CG A:ARG175 3.2 0.1 1.0 N A:TRP174 3.4 0.6 1.0 N A:ARG175 3.4 0.3 1.0 CA A:PRO173 3.6 0.1 1.0 CB A:ARG175 3.7 0.1 1.0 C A:PRO173 4.0 0.7 1.0 CB A:PRO173 4.2 0.3 1.0 CA A:ARG175 4.2 0.5 1.0 CZ A:ARG175 4.4 0.2 1.0 C A:TRP174 4.4 0.3 1.0 CA A:TRP174 4.4 0.6 1.0 CD1 A:TRP174 4.4 1.0 1.0 CG A:TRP174 4.5 0.3 1.0 NE1 A:TRP174 4.5 0.9 1.0 CD2 A:TRP174 4.7 0.0 1.0 CE2 A:TRP174 4.7 0.6 1.0 O A:LEU172 4.7 0.8 1.0 N A:PRO173 4.8 0.4 1.0 NH2 A:ARG175 4.9 0.8 1.0

M.Sjodt, K.Brock, G.Dobihal, P.D.A.Rohs, A.G.Green, T.A.Hopf, A.J.Meeske, V.Srisuknimit, D.Kahne, S.Walker, D.S.Marks, T.G.Bernhardt, D.Z.Rudner, A.C.Kruse. Structure of the Peptidoglycan Polymerase Roda Resolved By Evolutionary Coupling Analysis. Nature V. 556 118 2018.
ISSN: ESSN 1476-4687
PubMed: 29590088
DOI: 10.1038/NATURE25985