Chlorine in PDB 3faw: Crystal Structure of the Group B Streptococcus Pullulanase Sap

The structure of Crystal Structure of the Group B Streptococcus Pullulanase Sap, PDB code: 3faw was solved by L.J.Gourlay, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	40.00 / 2.10
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	48.949, 102.834, 172.438, 90.00, 90.00, 90.00
R / Rfree (%)	19.4 / 23.5

The structure of Crystal Structure of the Group B Streptococcus Pullulanase Sap also contains other interesting chemical elements:

Calcium

(Ca)

4 atoms

The binding sites of Chlorine atom in the Crystal Structure of the Group B Streptococcus Pullulanase Sap (pdb code 3faw). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 5 binding sites of Chlorine where determined in the Crystal Structure of the Group B Streptococcus Pullulanase Sap, PDB code: 3faw:
Jump to Chlorine binding site number: 1; 2; 3; 4; 5;

Chlorine binding site 1 out of 5 in the Crystal Structure of the Group B Streptococcus Pullulanase Sap


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 Group B Streptococcus Pullulanase Sap within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl1223 b:13.6 occ:1.00 O A:HOH197 2.9 13.9 1.0 ND1 A:HIS963 3.3 14.2 1.0 N A:LEU923 3.3 10.2 1.0 CA A:GLN966 3.6 14.8 1.0 CB A:THR922 3.6 13.4 1.0 N A:GLN966 3.8 14.7 1.0 CB A:GLN966 3.8 15.7 1.0 CA A:THR922 3.9 13.5 1.0 CB A:LEU923 4.0 11.4 1.0 CB A:ALA916 4.0 8.9 1.0 CG A:HIS963 4.1 10.8 1.0 C A:THR922 4.1 12.8 1.0 CG A:GLN966 4.2 13.8 1.0 CA A:LEU923 4.3 10.9 1.0 CB A:HIS963 4.3 12.2 1.0 C A:GLY965 4.3 13.1 1.0 CG2 A:THR922 4.3 12.5 1.0 CE1 A:HIS963 4.3 13.4 1.0 O A:GLY965 4.5 13.5 1.0 CB A:ARG970 4.6 10.6 1.0 OG1 A:THR922 4.7 13.1 1.0 O A:ARG970 4.7 10.3 1.0 O A:SER964 4.8 9.8 1.0 O A:HIS963 4.9 13.3 1.0 N A:HIS924 4.9 11.4 1.0 OE1 A:GLN966 4.9 14.8 1.0

Chlorine binding site 2 out of 5 in the Crystal Structure of the Group B Streptococcus Pullulanase Sap


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 Group B Streptococcus Pullulanase Sap within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl1224 b:35.7 occ:1.00 OE2 A:GLU939 3.2 22.2 0.1 N A:ILE1031 3.5 13.2 1.0 CB A:ILE1031 3.6 12.9 1.0 CA A:HIS1029 3.6 17.5 1.0 CD A:GLU939 3.7 21.7 1.0 OE1 A:GLU939 3.8 22.5 0.1 C A:HIS1029 3.8 16.9 1.0 CD A:PRO1030 3.8 17.0 1.0 N A:PRO1030 3.8 16.4 1.0 CG1 A:ILE1031 3.9 14.1 1.0 O A:HOH1235 4.0 24.7 1.0 CB A:HIS1029 4.1 17.3 1.0 CA A:ILE1031 4.1 13.3 1.0 CD1 A:ILE1031 4.2 16.4 1.0 N A:SER1032 4.2 11.9 1.0 O A:HIS1029 4.4 15.0 1.0 CG A:PRO1030 4.5 16.7 1.0 O A:HOH139 4.5 18.5 1.0 C A:PRO1030 4.6 15.1 1.0 O A:LYS1028 4.7 20.9 1.0 CD2 A:HIS1029 4.7 19.3 1.0 CG A:HIS1029 4.7 17.3 1.0 C A:ILE1031 4.7 13.1 1.0 CA A:PRO1030 4.7 15.6 1.0 OG A:SER1032 4.8 11.4 1.0 CG2 A:ILE1031 4.8 8.8 1.0 CG A:GLU939 4.9 20.6 1.0 N A:HIS1029 4.9 19.0 1.0

Chlorine binding site 3 out of 5 in the Crystal Structure of the Group B Streptococcus Pullulanase Sap


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 Group B Streptococcus Pullulanase Sap within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl1225 b:32.8 occ:1.00 OG A:SER704 2.7 14.3 1.0 O A:ASP709 2.7 10.7 1.0 O A:LYS706 2.9 14.0 1.0 CD A:ARG713 3.1 17.0 1.0 N A:ARG713 3.1 12.4 1.0 CB A:SER704 3.4 15.9 1.0 CB A:ARG713 3.5 11.5 1.0 CB A:ALA712 3.5 13.1 1.0 C A:LYS706 3.6 14.6 1.0 NH1 A:ARG713 3.7 17.5 1.0 CA A:PRO707 3.7 13.8 1.0 CG A:ARG713 3.7 13.1 1.0 CA A:ARG713 3.8 12.1 1.0 C A:ASP709 3.8 12.5 1.0 C A:ALA712 4.0 12.5 1.0 N A:PRO707 4.0 13.9 1.0 CA A:ALA712 4.1 13.1 1.0 NE A:ARG713 4.1 16.8 1.0 OE1 A:GLU716 4.1 16.1 1.0 C A:PRO707 4.1 13.5 1.0 O A:PRO707 4.1 13.7 1.0 N A:ALA712 4.1 13.5 1.0 CZ A:ARG713 4.3 13.8 1.0 CA A:PRO710 4.5 11.1 1.0 C A:PRO710 4.6 11.1 1.0 N A:PRO710 4.6 12.3 1.0 N A:ASP709 4.7 11.2 1.0 O A:PRO710 4.7 10.2 1.0 CA A:LYS706 4.7 16.7 1.0 CA A:ASP709 4.8 11.8 1.0 CA A:SER704 4.9 15.8 1.0 N A:LYS706 4.9 16.9 1.0 CB A:PRO707 5.0 14.1 1.0

Chlorine binding site 4 out of 5 in the Crystal Structure of the Group B Streptococcus Pullulanase Sap


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 Group B Streptococcus Pullulanase Sap within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl1226 b:41.3 occ:1.00 NH1 A:ARG866 3.6 16.1 1.0 ND2 A:ASN920 3.6 17.4 1.0 O A:HOH338 3.6 12.5 1.0 CZ2 A:TRP833 4.5 12.0 1.0 NE1 A:TRP833 4.5 13.2 1.0 CZ A:ARG866 4.6 16.2 1.0 CG A:ASN920 4.6 16.1 1.0 CE2 A:TRP833 4.6 12.1 1.0 OD1 A:ASN920 4.7 17.8 1.0 O A:HOH1284 4.7 25.1 1.0 O A:HOH1312 4.7 2.0 0.5 NH2 A:ARG866 4.7 13.3 1.0 CB A:PHE873 4.9 26.4 1.0

Chlorine binding site 5 out of 5 in the Crystal Structure of the Group B Streptococcus Pullulanase Sap


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 Group B Streptococcus Pullulanase Sap within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl5 b:46.5 occ:1.00 NE2 A:HIS924 2.8 9.7 1.0 CG A:GLU939 3.2 20.6 1.0 CB A:GLU939 3.3 19.2 1.0 CA A:GLU939 3.5 18.2 1.0 CD A:GLU939 3.6 21.7 1.0 CE1 A:HIS924 3.6 10.6 1.0 CB A:PRO935 3.6 23.3 1.0 OE2 A:GLU939 3.7 22.2 0.1 CE1 A:HIS943 3.7 13.7 1.0 CD2 A:HIS924 3.8 12.6 1.0 O A:PRO935 4.0 26.6 1.0 ND1 A:HIS943 4.2 15.9 1.0 O A:HOH54 4.2 22.9 1.0 CA A:PRO935 4.3 22.8 1.0 O A:GLU939 4.4 16.0 1.0 OE1 A:GLU939 4.4 22.5 0.1 C A:GLU939 4.4 17.3 1.0 N A:GLU939 4.6 18.5 1.0 C A:PRO935 4.6 24.5 1.0 CG A:PRO935 4.7 21.4 1.0 ND1 A:HIS924 4.8 10.5 1.0 CD1 A:ILE942 4.8 15.2 1.0 NE2 A:HIS943 4.9 14.1 1.0 CG A:HIS924 4.9 11.5 1.0

L.J.Gourlay, I.Santi, A.Pezzicoli, G.Grandi, M.Soriani, M.Bolognesi. Group B Streptococcus Pullulanase Crystal Structures in the Context of A Novel Strategy For Vaccine Development J.Bacteriol. V. 191 3544 2009.
ISSN: ISSN 0021-9193
PubMed: 19329633
DOI: 10.1128/JB.01755-08