Chlorine in PDB 6bas: Crystal Structure of Thermus Thermophilus Rod Shape Determining Protein Roda D255A Mutant (Q5SIX3_THET8)

Enzymatic activity of Crystal Structure of Thermus Thermophilus Rod Shape Determining Protein Roda D255A Mutant (Q5SIX3_THET8)

All present enzymatic activity of Crystal Structure of Thermus Thermophilus Rod Shape Determining Protein Roda D255A Mutant (Q5SIX3_THET8):
2.4.1.129;

Protein crystallography data

The structure of Crystal Structure of Thermus Thermophilus Rod Shape Determining Protein Roda D255A Mutant (Q5SIX3_THET8), PDB code: 6bas 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 / 3.19
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 (%) 27.7 / 30.2

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Crystal Structure of Thermus Thermophilus Rod Shape Determining Protein Roda D255A Mutant (Q5SIX3_THET8) (pdb code 6bas). 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 Crystal Structure of Thermus Thermophilus Rod Shape Determining Protein Roda D255A Mutant (Q5SIX3_THET8), PDB code: 6bas:

Chlorine binding site 1 out of 1 in 6bas

Go back to Chlorine Binding Sites List in 6bas
Chlorine binding site 1 out of 1 in the Crystal Structure of Thermus Thermophilus Rod Shape Determining Protein Roda D255A Mutant (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 D255A Mutant (Q5SIX3_THET8) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl401

b:0.9
occ:1.00
 NE A:ARG175 3.3 0.7 1.0
CG A:ARG175 3.3 0.3 1.0
N A:TRP174 3.3 1.0 1.0
CD A:ARG175 3.3 0.6 1.0
N A:ARG175 3.5 1.0 1.0
CA A:PRO173 3.5 0.3 1.0
CB A:ARG175 3.8 0.6 1.0
C A:PRO173 3.9 0.9 1.0
CB A:PRO173 4.0 0.3 1.0
CA A:ARG175 4.3 0.8 1.0
CA A:TRP174 4.4 0.7 1.0
CD1 A:TRP174 4.4 0.5 1.0
C A:TRP174 4.4 0.9 1.0
NE1 A:TRP174 4.5 0.8 1.0
CG A:TRP174 4.5 0.2 1.0
CZ A:ARG175 4.5 0.2 1.0
N A:PRO173 4.6 0.2 1.0
O A:LEU172 4.7 0.4 1.0
CE2 A:TRP174 4.7 0.9 1.0
CD2 A:TRP174 4.7 0.6 1.0
NH2 A:ARG175 5.0 0.8 1.0

Reference:

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
Page generated: Sat Dec 12 12:45:58 2020

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