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Chlorine in PDB 3op1: Crystal Structure of Macrolide-Efflux Protein SP_1110 From Streptococcus Pneumoniae

Protein crystallography data

The structure of Crystal Structure of Macrolide-Efflux Protein SP_1110 From Streptococcus Pneumoniae, PDB code: 3op1 was solved by Y.Kim, H.Li, G.Cobb, A.Joachimiak, Midwest Center For Structural Genomics(Mcsg), with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 35.76 / 2.49
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 180.153, 73.247, 87.518, 90.00, 112.48, 90.00
R / Rfree (%) 19.8 / 26.5

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Crystal Structure of Macrolide-Efflux Protein SP_1110 From Streptococcus Pneumoniae (pdb code 3op1). 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 Macrolide-Efflux Protein SP_1110 From Streptococcus Pneumoniae, PDB code: 3op1:

Chlorine binding site 1 out of 1 in 3op1

Go back to Chlorine Binding Sites List in 3op1
Chlorine binding site 1 out of 1 in the Crystal Structure of Macrolide-Efflux Protein SP_1110 From Streptococcus Pneumoniae


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 Macrolide-Efflux Protein SP_1110 From Streptococcus Pneumoniae within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cl306

b:85.4
occ:1.00
O1 B:PEG314 3.0 50.6 1.0
O4 A:PEG319 3.1 43.6 1.0
CG A:ARG215 3.8 39.8 1.0
O A:HOH375 3.9 46.8 1.0
O B:HOH398 4.1 48.7 1.0
NE A:ARG215 4.1 50.5 1.0
C4 A:PEG319 4.3 46.1 1.0
CD A:ARG215 4.4 51.2 1.0
NE B:ARG215 4.4 48.2 1.0
C1 B:PEG314 4.4 45.7 1.0
CG B:ARG215 4.5 33.7 1.0
O1 A:GOL317 4.5 74.8 1.0
O A:LEU213 4.7 31.1 1.0
CD B:ARG215 4.8 44.5 1.0
N A:ARG215 4.9 41.5 1.0

Reference:

Y.Kim, H.Li, G.Cobb, A.Joachimiak. Crystal Structure of Macrolide-Efflux Protein SP_1110 From Streptococcus Pneumoniae To Be Published.
Page generated: Sat Dec 12 10:00:30 2020

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