Chlorine in PDB 3efp: Crystal Structure of the Escherichia Coli Twin Arginine Leader Peptide Binding Protein Dmsd in A Monomeric Form

The structure of Crystal Structure of the Escherichia Coli Twin Arginine Leader Peptide Binding Protein Dmsd in A Monomeric Form, PDB code: 3efp was solved by C.M.Stevens, M.Paetzel, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	30.75 / 2.01
Space group	P 31 2 1
Cell size a, b, c (Å), α, β, γ (°)	128.020, 128.020, 78.723, 90.00, 90.00, 120.00
R / Rfree (%)	17.8 / 21.3

The structure of Crystal Structure of the Escherichia Coli Twin Arginine Leader Peptide Binding Protein Dmsd in A Monomeric Form also contains other interesting chemical elements:

Sodium

(Na)

1 atom

The binding sites of Chlorine atom in the Crystal Structure of the Escherichia Coli Twin Arginine Leader Peptide Binding Protein Dmsd in A Monomeric Form (pdb code 3efp). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 6 binding sites of Chlorine where determined in the Crystal Structure of the Escherichia Coli Twin Arginine Leader Peptide Binding Protein Dmsd in A Monomeric Form, PDB code: 3efp:
Jump to Chlorine binding site number: 1; 2; 3; 4; 5; 6;

Chlorine binding site 1 out of 6 in the Crystal Structure of the Escherichia Coli Twin Arginine Leader Peptide Binding Protein Dmsd in A Monomeric Form


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 the Escherichia Coli Twin Arginine Leader Peptide Binding Protein Dmsd in A Monomeric Form within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl211 b:61.2 occ:1.00 O A:HOH872 3.0 37.5 1.0 O A:GLY100 3.6 17.9 1.0 C A:GLY100 3.8 18.8 1.0 O A:PHE99 3.9 18.0 1.0 N A:ASP101 4.0 18.9 1.0 CA A:ASP101 4.0 19.1 1.0 O A:HOH739 4.1 22.7 1.0 CD2 A:LEU104 4.4 18.6 1.0 CB A:LEU104 4.5 18.4 1.0 O A:HOH884 4.5 36.2 1.0 CA A:GLY100 4.5 18.5 1.0 CB A:ASP101 4.6 18.9 1.0 C A:PHE99 4.9 17.9 1.0

Chlorine binding site 2 out of 6 in the Crystal Structure of the Escherichia Coli Twin Arginine Leader Peptide Binding Protein Dmsd in A Monomeric Form


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 the Escherichia Coli Twin Arginine Leader Peptide Binding Protein Dmsd in A Monomeric Form within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl212 b:73.7 occ:1.00 O A:HOH696 3.4 48.4 1.0 OG1 A:THR38 3.7 21.3 1.0 CE1 A:HIS68 3.7 20.0 1.0 CB A:THR38 4.1 22.1 1.0 CG2 A:THR38 4.1 21.9 1.0 ND1 A:HIS68 4.4 20.8 1.0 CG1 A:VAL34 4.6 20.0 1.0 NE2 A:HIS68 4.8 19.0 1.0 O A:HOH730 4.9 32.3 1.0 O A:HOH725 5.0 28.5 1.0

Chlorine binding site 3 out of 6 in the Crystal Structure of the Escherichia Coli Twin Arginine Leader Peptide Binding Protein Dmsd in A Monomeric Form


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 3 of Crystal Structure of the Escherichia Coli Twin Arginine Leader Peptide Binding Protein Dmsd in A Monomeric Form within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl213 b:68.5 occ:1.00 OG1 A:THR145 3.4 20.1 1.0 N A:THR145 3.7 19.4 1.0 CB A:THR145 3.7 19.1 1.0 OE1 A:GLU146 3.8 26.8 1.0 N A:GLN144 3.9 20.3 1.0 CG A:GLN144 3.9 21.0 1.0 O A:GLY142 4.2 19.6 1.0 C A:ARG143 4.2 20.1 1.0 CA A:ARG143 4.2 20.4 1.0 CA A:THR145 4.3 19.6 1.0 C A:GLN144 4.6 19.5 1.0 CA A:GLN144 4.6 19.9 1.0 CB A:GLN144 4.9 20.4 1.0 CD A:GLN144 4.9 22.8 1.0

Chlorine binding site 4 out of 6 in the Crystal Structure of the Escherichia Coli Twin Arginine Leader Peptide Binding Protein Dmsd in A Monomeric Form


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 4 of Crystal Structure of the Escherichia Coli Twin Arginine Leader Peptide Binding Protein Dmsd in A Monomeric Form within 5.0Å range: probe atom residue distance (Å) B Occ B:Cl209 b:58.1 occ:1.00 O B:HOH683 2.6 20.5 1.0 O B:HOH720 2.7 34.6 1.0 CD B:ARG143 3.7 20.1 1.0 CB B:ASN141 4.2 17.5 1.0 CG B:ARG143 4.2 16.9 1.0 NH1 B:ARG143 4.4 19.9 1.0 O B:ASN141 4.4 16.1 1.0 ND2 B:ASN141 4.5 16.2 1.0 NE B:ARG143 4.5 20.5 1.0 CG B:ASN141 4.7 16.9 1.0 CZ B:ARG143 4.8 21.2 1.0

Chlorine binding site 5 out of 6 in the Crystal Structure of the Escherichia Coli Twin Arginine Leader Peptide Binding Protein Dmsd in A Monomeric Form


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 5 of Crystal Structure of the Escherichia Coli Twin Arginine Leader Peptide Binding Protein Dmsd in A Monomeric Form within 5.0Å range: probe atom residue distance (Å) B Occ B:Cl210 b:70.8 occ:1.00 O B:HOH735 3.1 25.7 1.0 O B:HOH855 3.9 47.1 1.0 O B:HOH769 4.0 31.1 1.0 O B:HOH804 4.2 36.1 1.0 CE1 B:PHE117 4.2 18.6 1.0 CZ B:PHE117 4.4 18.8 1.0 CB B:LEU133 4.6 17.9 1.0 CD2 B:LEU133 4.7 15.5 1.0 SD B:MET119 4.8 25.9 1.0 CD1 B:LEU133 4.9 17.4 1.0 CG B:LEU133 5.0 17.8 1.0

Chlorine binding site 6 out of 6 in the Crystal Structure of the Escherichia Coli Twin Arginine Leader Peptide Binding Protein Dmsd in A Monomeric Form


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 6 of Crystal Structure of the Escherichia Coli Twin Arginine Leader Peptide Binding Protein Dmsd in A Monomeric Form within 5.0Å range: probe atom residue distance (Å) B Occ B:Cl211 b:54.7 occ:1.00 O B:HOH802 2.7 37.5 1.0 O B:HOH829 2.8 30.6 1.0 OE1 B:GLN6 2.8 17.0 1.0 O B:HOH801 2.9 29.2 1.0 O B:ALA139 3.2 17.9 1.0 CD B:GLN6 3.6 18.8 1.0 O B:HOH805 3.7 37.3 1.0 NE2 B:GLN6 4.0 18.2 1.0 C B:ALA139 4.2 17.6 1.0 CA B:GLN6 4.3 18.2 1.0 CA B:GLU140 4.3 18.1 1.0 O B:GLU140 4.4 17.6 1.0 O B:HOH685 4.4 17.1 1.0 CB B:GLN6 4.6 18.1 1.0 C B:GLU140 4.6 17.6 1.0 N B:GLU140 4.6 17.6 1.0 O B:SER5 4.7 18.6 1.0 CG B:GLN6 4.7 18.6 1.0 O B:GLN6 4.7 18.9 1.0 C B:GLN6 4.8 18.5 1.0

C.M.Stevens, T.M.Winstone, R.J.Turner, M.Paetzel. Structural Analysis of A Monomeric Form of the Twin-Arginine Leader Peptide Binding Chaperone Escherichia Coli Dmsd. J.Mol.Biol. V. 389 124 2009.
ISSN: ISSN 0022-2836
PubMed: 19361518
DOI: 10.1016/J.JMB.2009.03.069