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Chlorine in PDB 6y2q: Escherichia Coli Rnla Endoribonuclease

Protein crystallography data

The structure of Escherichia Coli Rnla Endoribonuclease, PDB code: 6y2q was solved by G.Garcia-Rodriguez, R.Loris, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 47.90 / 2.99
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 64.32, 100.8, 154.09, 90, 90, 90
R / Rfree (%) 20 / 25

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Escherichia Coli Rnla Endoribonuclease (pdb code 6y2q). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 2 binding sites of Chlorine where determined in the Escherichia Coli Rnla Endoribonuclease, PDB code: 6y2q:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in 6y2q

Go back to Chlorine Binding Sites List in 6y2q
Chlorine binding site 1 out of 2 in the Escherichia Coli Rnla Endoribonuclease


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Escherichia Coli Rnla Endoribonuclease within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl401

b:54.8
occ:1.00
NZ A:LYS189 3.3 76.4 1.0
N A:GLN105 3.9 71.6 1.0
CD A:LYS189 4.1 62.3 1.0
N A:GLY186 4.1 63.2 1.0
CA A:GLY186 4.2 58.2 1.0
CA A:LEU104 4.2 59.4 1.0
CE A:LYS189 4.3 66.4 1.0
O A:VAL103 4.5 77.3 1.0
CB A:GLN105 4.5 47.2 1.0
C A:LEU104 4.6 69.9 1.0
CD2 A:LEU104 4.6 44.6 1.0
C A:GLN185 4.6 66.4 1.0
CB A:GLN185 4.7 85.5 1.0
OE1 A:GLN105 4.7 79.0 1.0
CA A:GLN105 4.8 55.2 1.0
CB A:LEU104 4.8 45.3 1.0
CG A:GLN105 4.9 50.5 1.0

Chlorine binding site 2 out of 2 in 6y2q

Go back to Chlorine Binding Sites List in 6y2q
Chlorine binding site 2 out of 2 in the Escherichia Coli Rnla Endoribonuclease


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Escherichia Coli Rnla Endoribonuclease within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cl401

b:96.0
occ:1.00
NZ B:LYS189 3.7 69.1 1.0
N B:GLN105 3.9 65.1 1.0
OE1 B:GLN105 4.3 107.6 1.0
CA B:LEU104 4.4 51.8 1.0
CD B:LYS189 4.4 63.2 1.0
CB B:GLN105 4.4 67.1 1.0
N B:GLY186 4.5 51.8 1.0
CA B:GLY186 4.5 64.5 1.0
CG B:GLN105 4.6 87.9 1.0
CE B:LYS189 4.6 63.2 1.0
C B:LEU104 4.6 62.7 1.0
O B:VAL103 4.6 69.0 1.0
OD1 B:ASP183 4.7 123.9 1.0
CA B:GLN105 4.8 51.7 1.0
CD B:GLN105 4.8 99.8 1.0
CB B:GLN185 4.8 80.2 1.0
C B:GLN185 4.9 76.9 1.0
CD2 B:LEU104 5.0 48.6 1.0

Reference:

G.Garcia-Rodriguez, A.Talavera Perez, D.Wilmaerts, J.Michiels, D.Charlier, R.Loris. Quaternary Structure Changes Control Ribonuclease Activity of Rnla Toxin. To Be Published.
Page generated: Mon Jul 29 17:29:15 2024

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