Chlorine in PDB 4g9s: Crystal Structure of Escherichia Coli Plig in Complex with Atlantic Salmon G-Type Lysozyme

The structure of Crystal Structure of Escherichia Coli Plig in Complex with Atlantic Salmon G-Type Lysozyme, PDB code: 4g9s was solved by S.Leysen, L.Vanderkelen, S.D.Weeks, C.W.Michiels, S.V.Strelkov, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	43.27 / 0.95
Space group	P 65
Cell size a, b, c (Å), α, β, γ (°)	132.182, 132.182, 42.902, 90.00, 90.00, 120.00
R / Rfree (%)	12.9 / 13.6

The binding sites of Chlorine atom in the Crystal Structure of Escherichia Coli Plig in Complex with Atlantic Salmon G-Type Lysozyme (pdb code 4g9s). 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 Escherichia Coli Plig in Complex with Atlantic Salmon G-Type Lysozyme, PDB code: 4g9s:

Chlorine binding site 1 out of 1 in the Crystal Structure of Escherichia Coli Plig in Complex with Atlantic Salmon G-Type Lysozyme


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 Escherichia Coli Plig in Complex with Atlantic Salmon G-Type Lysozyme within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl201 b:12.8 occ:0.58 HB2 A:ASP86 1.2 25.7 0.4 CB A:ASP86 1.3 21.4 0.4 HB3 A:ASP86 1.5 25.7 0.4 CA A:ASP86 1.7 18.6 0.4 O A:GLY85 1.9 12.6 0.4 C A:ASP86 2.0 20.3 0.4 O A:ASP86 2.0 19.2 0.4 N A:ASP86 2.3 14.9 0.4 C A:GLY85 2.3 12.7 0.4 H A:GLY90 2.4 11.2 1.0 H A:HIS87 2.5 20.8 0.6 H A:LYS89 2.5 14.1 1.0 HA A:ASP86 2.6 22.3 0.4 HE B:ARG115 2.6 19.0 0.6 CG A:ASP86 2.8 24.4 0.4 HB2 A:HIS87 2.9 26.1 0.6 H A:ASP86 3.1 17.8 0.4 HA3 A:GLY85 3.1 12.3 0.6 HB2 A:LYS89 3.2 14.7 1.0 N A:HIS87 3.2 20.8 0.4 NH2 B:ARG115 3.2 18.1 0.6 N A:GLY90 3.2 9.3 1.0 N A:HIS87 3.3 17.4 0.6 H A:GLY88 3.3 20.2 0.4 N A:LYS89 3.3 11.8 1.0 NE B:ARG115 3.3 15.8 0.6 OD2 A:ASP86 3.5 26.3 0.4 H A:GLY88 3.6 20.2 0.6 C A:GLY85 3.6 12.3 0.6 OD1 A:ASP86 3.6 18.8 0.4 H A:HIS87 3.6 24.9 0.4 CB A:HIS87 3.7 21.8 0.6 CZ B:ARG115 3.7 16.5 0.6 N A:GLY88 3.7 16.8 1.0 CA A:HIS87 3.7 18.8 0.6 CA A:GLY85 3.8 10.2 0.6 HD1 A:HIS87 3.8 38.8 0.4 CA A:GLY85 3.8 11.8 0.4 C A:HIS87 3.8 18.1 0.6 N A:ASP86 3.8 13.2 0.6 H A:ASP86 3.8 15.9 0.6 HD3 B:ARG115 3.8 20.6 0.4 HA3 A:GLY90 3.9 10.0 1.0 CA A:LYS89 3.9 10.7 1.0 CB A:LYS89 3.9 12.2 1.0 HD2 B:ARG115 3.9 20.6 0.4 HG2 A:LYS89 3.9 17.6 1.0 O A:GLY85 4.0 13.0 0.6 C A:LYS89 4.0 9.8 1.0 HA3 A:GLY85 4.1 14.1 0.4 H A:GLY85 4.1 11.7 0.6 H A:GLY85 4.1 12.1 0.4 CA A:GLY90 4.1 8.4 1.0 C A:HIS87 4.2 20.9 0.4 HB3 A:HIS87 4.2 26.1 0.6 CA A:HIS87 4.2 23.8 0.4 CD B:ARG115 4.3 17.1 0.4 HA2 A:GLY85 4.3 14.1 0.4 HG2 B:ARG115 4.3 20.2 0.4 C A:GLY88 4.3 13.2 1.0 N A:GLY85 4.4 9.8 0.6 C A:ASP86 4.4 17.6 0.6 N A:GLY85 4.4 10.1 0.4 CG A:LYS89 4.4 14.7 1.0 HB2 A:HIS87 4.5 34.3 0.4 O A:HIS87 4.5 18.9 0.6 CA A:GLY88 4.5 15.3 1.0 HD2 B:ARG115 4.5 17.4 0.6 CD B:ARG115 4.5 14.5 0.6 HE1 B:TYR47 4.5 17.0 1.0 HA2 A:GLY85 4.6 12.3 0.6 ND1 A:HIS87 4.6 32.3 0.4 HD2 A:HIS87 4.6 36.9 0.6 CA A:ASP86 4.7 15.4 0.6 HG2 B:ARG115 4.7 16.2 0.6 HA A:HIS87 4.7 22.5 0.6 HB3 A:LYS89 4.7 14.7 1.0 HH B:TYR47 4.7 24.0 1.0 O A:HOH458 4.7 19.0 0.5 HA2 A:GLY88 4.7 18.3 1.0 OE1 A:GLN95 4.8 10.1 1.0 CG A:HIS87 4.8 27.3 0.6 O A:GLY90 4.8 8.3 1.0 HH11 B:ARG115 4.8 21.3 0.4 HA A:LYS89 4.8 12.9 1.0 CB A:HIS87 4.8 28.6 0.4 HA2 A:GLY90 4.9 10.0 1.0 CE1 B:TYR47 4.9 14.2 1.0 CG B:ARG115 4.9 16.8 0.4 HG3 A:LYS89 4.9 17.6 1.0 NH1 B:ARG115 5.0 19.9 0.6 HB2 A:ASP86 5.0 23.7 0.6 C A:GLY90 5.0 7.7 1.0

S.Leysen, L.Vanderkelen, S.D.Weeks, C.W.Michiels, S.V.Strelkov. Structural Basis of Bacterial Defense Against G-Type Lysozyme-Based Innate Immunity. Cell.Mol.Life Sci. V. 70 1113 2013.
ISSN: ISSN 1420-682X
PubMed: 23086131
DOI: 10.1007/S00018-012-1184-1