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Chlorine in PDB 6p7q: Structure of E. Coli MS115-1 Nucc, 5'-Papa Bound Form

Protein crystallography data

The structure of Structure of E. Coli MS115-1 Nucc, 5'-Papa Bound Form, PDB code: 6p7q was solved by Q.Ye, R.K.Lau, K.R.Berg, K.D.Corbett, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 55.66 / 1.66
Space group H 3 2
Cell size a, b, c (Å), α, β, γ (°) 131.781, 131.781, 252.836, 90.00, 90.00, 120.00
R / Rfree (%) 15.9 / 18.5

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Structure of E. Coli MS115-1 Nucc, 5'-Papa Bound Form (pdb code 6p7q). 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 E. Coli MS115-1 Nucc, 5'-Papa Bound Form, PDB code: 6p7q:

Chlorine binding site 1 out of 1 in 6p7q

Go back to Chlorine Binding Sites List in 6p7q
Chlorine binding site 1 out of 1 in the Structure of E. Coli MS115-1 Nucc, 5'-Papa Bound Form


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Structure of E. Coli MS115-1 Nucc, 5'-Papa Bound Form within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl301

b:28.4
occ:1.00
HE1 B:TRP160 2.3 27.6 1.0
HH11 A:ARG126 2.7 30.4 1.0
HA A:SER123 2.9 33.5 1.0
O A:HOH552 3.0 28.1 1.0
HB3 B:SER167 3.0 34.3 1.0
HD2 A:ARG126 3.1 28.6 1.0
NE1 B:TRP160 3.2 23.1 1.0
O B:HOH553 3.2 41.0 1.0
NH1 A:ARG126 3.4 25.4 1.0
O B:HOH523 3.4 38.6 1.0
HB3 A:SER123 3.4 33.0 1.0
HH12 A:ARG126 3.7 30.4 1.0
HZ2 B:TRP160 3.7 25.5 1.0
CA A:SER123 3.7 27.9 1.0
HB2 B:ALA111 3.8 28.9 1.0
HB2 A:SER123 3.8 33.0 1.0
HD3 A:ARG126 3.8 28.6 1.0
CB A:SER123 3.8 27.5 1.0
CD A:ARG126 3.8 23.9 1.0
CB B:SER167 3.9 28.6 1.0
HG B:SER167 4.0 35.4 1.0
CE2 B:TRP160 4.1 20.3 1.0
OG B:SER167 4.1 29.5 1.0
O B:HOH415 4.1 32.1 1.0
N A:SER123 4.2 20.0 1.0
CD1 B:TRP160 4.2 21.6 1.0
CZ2 B:TRP160 4.2 21.3 1.0
HD1 B:TRP160 4.3 25.8 1.0
CZ A:ARG126 4.3 24.8 1.0
H A:SER123 4.4 23.9 1.0
NE A:ARG126 4.5 22.9 1.0
HB2 B:SER167 4.5 34.3 1.0
HA B:SER167 4.6 27.0 1.0
O B:SER167 4.6 20.2 1.0
HB2 A:ARG126 4.6 24.0 1.0
C A:ALA122 4.7 21.3 1.0
CB B:ALA111 4.7 24.1 1.0
HB3 A:ALA122 4.7 25.3 1.0
CA B:SER167 4.7 22.5 1.0
O A:ALA122 4.8 23.2 1.0
C B:SER167 4.9 20.5 1.0
O A:ARG119 4.9 26.7 1.0
HB1 B:ALA111 4.9 28.9 1.0
HB1 A:ALA122 4.9 25.3 1.0
HB2 B:ALA171 4.9 25.5 1.0
HB3 B:ALA111 5.0 28.9 1.0
C A:SER123 5.0 30.3 1.0

Reference:

R.K.Lau, Q.Ye, E.A.Birkholz, K.R.Berg, L.Patel, I.T.Mathews, J.D.Watrous, K.Ego, A.T.Whiteley, B.Lowey, J.J.Mekalanos, P.J.Kranzusch, M.Jain, J.Pogliano, K.D.Corbett. Structure and Mechanism of A Cyclic Trinucleotide-Activated Bacterial Endonuclease Mediating Bacteriophage Immunity To Be Published.
Page generated: Mon Jul 29 13:11:03 2024

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