Chlorine in PDB 8ped: Crystal Structure of Paradendryphiella Salina PL7C Alginate Lyase Soaked with Trimannuronic Acid

The structure of Crystal Structure of Paradendryphiella Salina PL7C Alginate Lyase Soaked with Trimannuronic Acid, PDB code: 8ped was solved by C.Wilkens, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	38.05 / 1.10
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	42.06, 59.77, 89.34, 90, 90, 90
R / Rfree (%)	12.9 / 14.6

The binding sites of Chlorine atom in the Crystal Structure of Paradendryphiella Salina PL7C Alginate Lyase Soaked with Trimannuronic Acid (pdb code 8ped). 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 Paradendryphiella Salina PL7C Alginate Lyase Soaked with Trimannuronic Acid, PDB code: 8ped:

Chlorine binding site 1 out of 1 in the Crystal Structure of Paradendryphiella Salina PL7C Alginate Lyase Soaked with Trimannuronic Acid


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 Paradendryphiella Salina PL7C Alginate Lyase Soaked with Trimannuronic Acid within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl301 b:66.6 occ:1.00 HH22 A:ARG132 2.0 21.9 1.0 HZ1 A:LYS167 2.3 23.7 0.3 HZ2 A:LYS167 2.4 23.7 0.3 O A:HOH437 2.5 35.7 1.0 NZ A:LYS167 2.6 19.8 0.3 HZ3 A:LYS167 2.6 23.7 0.3 HE1 A:MET151 2.7 22.4 1.0 OE2 A:GLU117 2.7 14.5 1.0 NH2 A:ARG132 2.8 18.3 1.0 HE3 A:MET151 2.8 22.4 1.0 HE2 A:LYS167 3.0 29.6 0.7 HO2 C:BEM2 3.1 23.9 1.0 CE A:MET151 3.1 18.7 1.0 HG1 A:THR153 3.1 16.3 1.0 OG1 A:THR153 3.2 13.6 1.0 O A:HOH533 3.2 17.9 1.0 HH21 A:ARG132 3.2 21.9 1.0 O2 C:BEM2 3.3 19.9 1.0 HH12 A:ARG132 3.3 18.1 1.0 HE2 A:MET151 3.3 22.4 1.0 OE1 A:GLU117 3.5 16.1 1.0 CD A:GLU117 3.5 14.1 1.0 CZ A:ARG132 3.7 15.8 1.0 HG21 A:THR153 3.7 17.4 1.0 HG A:SER134 3.8 15.4 1.0 NH1 A:ARG132 3.8 15.1 1.0 HD13 A:ILE136 3.8 22.6 1.0 CE A:LYS167 3.9 24.7 0.7 HZ1 A:LYS167 4.0 29.4 0.7 HE3 A:LYS139 4.0 28.0 1.0 O A:HOH474 4.0 14.9 1.0 CE A:LYS167 4.1 20.6 0.3 HZ3 A:LYS167 4.2 29.4 0.7 CB A:THR153 4.2 13.5 1.0 NZ A:LYS167 4.3 24.5 0.7 HD11 A:ILE136 4.3 22.6 1.0 HB A:THR153 4.3 16.2 1.0 HD3 A:LYS167 4.3 26.7 0.7 HE3 A:LYS167 4.4 24.7 0.3 CG2 A:THR153 4.4 14.5 1.0 OG A:SER134 4.5 12.8 1.0 HE2 A:LYS167 4.5 24.7 0.3 CD1 A:ILE136 4.5 18.8 1.0 HE3 A:LYS167 4.6 29.6 0.7 O A:HOH643 4.6 27.2 1.0 HH11 A:ARG132 4.7 18.1 1.0 C2 C:BEM2 4.7 20.0 1.0 CD A:LYS167 4.7 22.3 0.7 HD3 A:LYS167 4.7 23.5 0.3 HG2 A:LYS167 4.7 24.4 0.7 HG2 A:LYS167 4.7 21.8 0.3 HG23 A:THR153 4.8 17.4 1.0 SD A:MET151 4.8 16.6 1.0 H2 C:BEM2 4.9 24.0 1.0 CG A:GLU117 4.9 13.2 1.0 O4 C:MAV1 4.9 17.9 1.0 CD A:LYS167 4.9 19.6 0.3 NE A:ARG132 4.9 15.8 1.0 CE A:LYS139 5.0 23.4 1.0

C.Wilkens, C.Wilkens. N/A N/A.