Chlorine in PDB 8h2w: Cellodextrin Phosphorylase From Clostridium Thermocellum Mutant - All Cysteine Residues Were Substituted with Serines

The structure of Cellodextrin Phosphorylase From Clostridium Thermocellum Mutant - All Cysteine Residues Were Substituted with Serines, PDB code: 8h2w was solved by T.Kuga, N.Sunagawa, K.Igarashi, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	43.82 / 1.21
Space group	P 1
Cell size a, b, c (Å), α, β, γ (°)	83.208, 88.778, 88.761, 98.58, 110.55, 110.56
R / Rfree (%)	14.3 / 16.3

The binding sites of Chlorine atom in the Cellodextrin Phosphorylase From Clostridium Thermocellum Mutant - All Cysteine Residues Were Substituted with Serines (pdb code 8h2w). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 5 binding sites of Chlorine where determined in the Cellodextrin Phosphorylase From Clostridium Thermocellum Mutant - All Cysteine Residues Were Substituted with Serines, PDB code: 8h2w:
Jump to Chlorine binding site number: 1; 2; 3; 4; 5;

Chlorine binding site 1 out of 5 in the Cellodextrin Phosphorylase From Clostridium Thermocellum Mutant - All Cysteine Residues Were Substituted with Serines


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Cellodextrin Phosphorylase From Clostridium Thermocellum Mutant - All Cysteine Residues Were Substituted with Serines within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl1022 b:12.6 occ:1.00 HE A:ARG718 2.4 14.2 1.0 HD22 A:ASN624 2.4 19.8 1.0 HD21 A:ASN752 2.4 15.1 1.0 HH21 A:ARG718 2.6 15.8 1.0 HB2 A:ASN624 2.8 17.0 1.0 HB2 A:ASN752 2.9 14.8 1.0 HD2 A:PHE750 3.1 14.9 1.0 O A:HOH1528 3.1 13.3 1.0 NE A:ARG718 3.2 11.9 1.0 ND2 A:ASN624 3.2 16.5 1.0 HZ3 A:TRP623 3.2 16.3 1.0 ND2 A:ASN752 3.3 12.5 1.0 NH2 A:ARG718 3.3 13.2 1.0 HE3 A:TRP623 3.3 15.1 1.0 CB A:ASN624 3.7 14.2 1.0 HD12 A:LEU787 3.7 18.8 1.0 CZ A:ARG718 3.7 12.4 1.0 CB A:ASN752 3.7 12.3 1.0 HD21 A:ASN624 3.8 19.8 1.0 CZ3 A:TRP623 3.8 13.6 1.0 CE3 A:TRP623 3.8 12.6 1.0 HD22 A:ASN752 3.8 15.1 1.0 HB3 A:PHE750 3.9 14.1 1.0 CD2 A:PHE750 3.9 12.4 1.0 CG A:ASN624 3.9 15.4 1.0 HB3 A:ASN624 4.0 17.0 1.0 HB3 A:ASN752 4.0 14.8 1.0 CG A:ASN752 4.0 12.1 1.0 HH22 A:ARG718 4.0 15.8 1.0 H A:ASN752 4.2 12.2 1.0 HD3 A:ARG718 4.2 14.0 1.0 CD A:ARG718 4.3 11.6 1.0 HG A:LEU787 4.3 17.2 1.0 HD22 A:LEU787 4.4 21.1 1.0 HE2 A:PHE750 4.4 15.7 1.0 HD12 A:LEU627 4.5 20.1 1.0 SD A:MET667 4.5 12.3 1.0 CD1 A:LEU787 4.5 15.6 1.0 CE2 A:PHE750 4.6 13.1 1.0 HG2 A:ARG718 4.7 14.5 1.0 CB A:PHE750 4.7 11.7 1.0 HD11 A:LEU787 4.8 18.8 1.0 CG A:PHE750 4.8 11.4 1.0 CA A:ASN624 4.8 14.9 1.0 CG A:LEU787 4.9 14.3 1.0 H A:ASN624 4.9 15.6 1.0 N A:ASN752 4.9 10.2 1.0 CA A:ASN752 4.9 11.4 1.0 HA A:ASN624 5.0 17.9 1.0 CH2 A:TRP623 5.0 14.0 1.0

Chlorine binding site 2 out of 5 in the Cellodextrin Phosphorylase From Clostridium Thermocellum Mutant - All Cysteine Residues Were Substituted with Serines


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Cellodextrin Phosphorylase From Clostridium Thermocellum Mutant - All Cysteine Residues Were Substituted with Serines within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl1023 b:12.7 occ:1.00 H A:LEU888 2.5 13.9 0.3 H A:LEU888 2.5 13.3 0.7 H A:THR492 2.5 12.8 1.0 H A:GLN491 2.7 12.3 1.0 HA3 A:GLY490 2.8 14.3 1.0 HD2 A:HIS141 3.0 13.6 1.0 HB2 A:LEU888 3.1 14.5 0.3 N A:GLN491 3.1 10.2 1.0 HD11 A:LEU888 3.1 19.3 0.7 HA A:PRO887 3.1 12.9 1.0 H A:GLN493 3.2 14.1 0.5 HE2 A:HIS141 3.3 13.9 0.0 N A:LEU888 3.3 11.6 0.3 HB2 A:PRO887 3.3 14.9 1.0 HB3 A:GLN491 3.3 13.8 1.0 N A:LEU888 3.3 11.1 0.7 HD11 A:LEU888 3.3 17.1 0.3 N A:THR492 3.3 10.7 1.0 HB3 A:PRO887 3.4 14.9 1.0 HB2 A:LEU888 3.4 14.3 0.7 HG A:LEU888 3.4 14.7 0.7 OG1 A:THR492 3.5 11.7 1.0 HG A:LEU888 3.6 16.2 0.3 CB A:PRO887 3.6 12.4 1.0 CD2 A:HIS141 3.6 11.3 1.0 CA A:GLY490 3.6 11.9 1.0 CA A:PRO887 3.7 10.8 1.0 C A:GLY490 3.7 12.2 1.0 NE2 A:HIS141 3.7 11.6 1.0 CB A:LEU888 3.8 12.0 0.3 CA A:GLN491 3.9 10.4 1.0 CD1 A:LEU888 3.9 16.1 0.7 CG A:LEU888 3.9 12.2 0.7 N A:GLN493 4.0 11.7 1.0 CB A:LEU888 4.0 11.9 0.7 HG1 A:THR492 4.0 14.1 0.0 CG A:LEU888 4.0 13.5 0.3 CB A:GLN491 4.0 11.5 1.0 C A:PRO887 4.0 11.2 1.0 CD1 A:LEU888 4.1 14.2 0.3 HA2 A:GLY490 4.1 14.3 1.0 C A:GLN491 4.1 10.6 1.0 CA A:LEU888 4.1 11.7 0.3 HB3 A:GLN493 4.2 18.9 0.5 CA A:LEU888 4.3 11.8 0.7 CA A:THR492 4.3 10.8 1.0 HD12 A:LEU888 4.3 19.3 0.7 HB2 A:GLN493 4.3 18.9 0.6 HB2 A:GLN491 4.4 13.8 1.0 H A:LEU889 4.4 18.2 0.7 CB A:THR492 4.5 11.2 1.0 H A:LEU889 4.5 16.1 0.3 C A:THR492 4.5 13.2 1.0 HD12 A:LEU888 4.6 17.1 0.3 HD23 A:LEU889 4.6 25.0 0.3 HB3 A:LEU888 4.7 14.5 0.3 HD13 A:LEU888 4.7 19.3 0.7 CB A:GLN493 4.7 15.8 1.0 N A:GLY490 4.7 11.9 1.0 O A:GLY490 4.7 15.9 1.0 HG23 A:THR492 4.7 12.8 1.0 HD13 A:LEU888 4.8 17.1 0.3 HA A:GLN491 4.8 12.5 1.0 HA A:LEU888 4.8 14.0 0.3 HB3 A:LEU888 4.9 14.3 0.7 HD22 A:LEU889 4.9 25.0 0.3 O A:PHE489 4.9 10.8 0.6 HA A:LEU888 4.9 14.2 0.7 CA A:GLN493 5.0 13.0 1.0 CG A:HIS141 5.0 11.2 1.0 HA3 A:GLY886 5.0 13.8 1.0

Chlorine binding site 3 out of 5 in the Cellodextrin Phosphorylase From Clostridium Thermocellum Mutant - All Cysteine Residues Were Substituted with Serines


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 3 of Cellodextrin Phosphorylase From Clostridium Thermocellum Mutant - All Cysteine Residues Were Substituted with Serines within 5.0Å range: probe atom residue distance (Å) B Occ B:Cl1021 b:46.3 occ:1.00 H B:LYS117 2.2 20.9 1.0 HG3 B:PRO52 2.9 32.3 1.0 NZ B:LYS117 2.9 38.4 1.0 HA B:ASP115 3.0 20.8 1.0 N B:LYS117 3.0 17.4 1.0 CG B:LYS117 3.1 30.5 1.0 CD B:LYS117 3.1 34.6 1.0 H B:VAL116 3.1 21.1 1.0 N B:VAL116 3.3 17.5 1.0 CE B:LYS117 3.4 37.6 1.0 CB B:LYS117 3.5 24.9 1.0 O B:SER114 3.5 23.1 1.0 C B:ASP115 3.6 16.6 1.0 HB B:VAL116 3.6 21.1 1.0 CA B:ASP115 3.7 17.3 1.0 CG B:PRO52 3.8 26.9 1.0 CA B:LYS117 3.8 19.8 1.0 HG2 B:PRO52 4.0 32.3 1.0 C B:VAL116 4.0 16.8 1.0 CA B:VAL116 4.0 16.6 1.0 C B:SER114 4.1 19.9 1.0 N B:ASP115 4.1 19.0 1.0 O B:VAL113 4.2 26.4 1.0 O B:ASP115 4.3 16.0 1.0 CB B:VAL116 4.3 17.5 1.0 O B:HOH1109 4.4 45.3 1.0 HA B:LYS117 4.4 23.8 1.0 HB3 B:PRO52 4.5 32.2 1.0 H B:HIS118 4.5 18.6 1.0 CB B:PRO52 4.5 26.8 1.0 HB2 B:PRO52 4.5 32.2 1.0 OD1 B:ASP115 4.6 19.8 1.0 H B:ASP115 4.7 22.9 1.0 HD3 B:PRO52 4.8 30.3 1.0 CD B:PRO52 4.8 25.2 1.0 O B:HOH1475 4.9 51.6 1.0 C B:LYS117 4.9 16.8 1.0 HA B:VAL116 4.9 19.9 1.0 HG23 B:VAL116 5.0 22.4 1.0

Chlorine binding site 4 out of 5 in the Cellodextrin Phosphorylase From Clostridium Thermocellum Mutant - All Cysteine Residues Were Substituted with Serines


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 4 of Cellodextrin Phosphorylase From Clostridium Thermocellum Mutant - All Cysteine Residues Were Substituted with Serines within 5.0Å range: probe atom residue distance (Å) B Occ B:Cl1022 b:14.3 occ:1.00 HE B:ARG718 2.4 15.0 1.0 HD22 B:ASN624 2.4 19.1 1.0 HD22 B:ASN752 2.4 14.7 1.0 HH21 B:ARG718 2.5 16.2 1.0 HB2 B:ASN624 2.8 16.4 1.0 HB2 B:ASN752 2.9 13.4 1.0 HD2 B:PHE750 3.1 15.4 1.0 O B:HOH1532 3.1 13.8 1.0 NE B:ARG718 3.2 12.5 1.0 HZ3 B:TRP623 3.2 15.6 1.0 ND2 B:ASN624 3.2 15.9 1.0 NH2 B:ARG718 3.3 13.5 1.0 ND2 B:ASN752 3.3 12.3 1.0 HE3 B:TRP623 3.3 15.6 1.0 CB B:ASN624 3.7 13.7 1.0 HD12 B:LEU787 3.7 18.1 1.0 CZ B:ARG718 3.7 12.8 1.0 CZ3 B:TRP623 3.8 13.0 1.0 CB B:ASN752 3.8 11.2 1.0 HD21 B:ASN624 3.8 19.1 1.0 CE3 B:TRP623 3.8 13.0 1.0 HD21 B:ASN752 3.8 14.7 1.0 CD2 B:PHE750 3.9 12.8 1.0 HB3 B:PHE750 3.9 14.3 1.0 CG B:ASN624 4.0 15.3 1.0 HH22 B:ARG718 4.0 16.2 1.0 HB3 B:ASN624 4.0 16.4 1.0 CG B:ASN752 4.0 11.4 1.0 HB3 B:ASN752 4.1 13.4 1.0 H B:ASN752 4.2 11.8 1.0 HD3 B:ARG718 4.3 14.5 1.0 CD B:ARG718 4.3 12.1 1.0 HG B:LEU787 4.3 16.5 1.0 HD22 B:LEU787 4.4 21.0 1.0 HE2 B:PHE750 4.4 15.6 1.0 CD1 B:LEU787 4.5 15.1 1.0 SD B:MET667 4.5 12.2 1.0 HD12 B:LEU627 4.6 19.6 1.0 CE2 B:PHE750 4.6 13.0 1.0 HG2 B:ARG718 4.7 13.5 1.0 HD11 B:LEU787 4.7 18.1 1.0 CB B:PHE750 4.7 11.9 1.0 CG B:PHE750 4.7 11.7 1.0 CA B:ASN624 4.8 13.9 1.0 CG B:LEU787 4.8 13.7 1.0 H B:ASN624 4.9 15.3 1.0 N B:ASN752 4.9 9.8 1.0 HA B:ASN624 4.9 16.7 1.0 CA B:ASN752 5.0 10.5 1.0 CH2 B:TRP623 5.0 14.3 1.0

Chlorine binding site 5 out of 5 in the Cellodextrin Phosphorylase From Clostridium Thermocellum Mutant - All Cysteine Residues Were Substituted with Serines


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 5 of Cellodextrin Phosphorylase From Clostridium Thermocellum Mutant - All Cysteine Residues Were Substituted with Serines within 5.0Å range: probe atom residue distance (Å) B Occ B:Cl1023 b:12.9 occ:1.00 H B:LEU888 2.4 13.4 1.0 H B:THR492 2.5 12.6 1.0 H B:GLN491 2.6 12.2 1.0 HA3 B:GLY490 2.8 15.8 1.0 HD2 B:HIS141 3.1 14.2 1.0 N B:GLN491 3.1 10.2 1.0 HA B:PRO887 3.2 12.8 1.0 HD11 B:LEU888 3.2 18.3 1.0 HG2 B:GLN493 3.2 22.2 0.3 O B:HOH1761 3.2 18.1 1.0 H B:GLN493 3.2 15.3 0.3 HB2 B:PRO887 3.2 14.6 1.0 H B:GLN493 3.3 13.4 0.7 N B:LEU888 3.3 11.1 1.0 HE2 B:HIS141 3.3 13.7 0.0 HB3 B:GLN491 3.3 13.8 1.0 HB2 B:LEU888 3.3 14.2 1.0 N B:THR492 3.4 10.5 1.0 HB3 B:PRO887 3.4 14.6 1.0 HG B:LEU888 3.4 14.7 1.0 OG1 B:THR492 3.5 11.5 1.0 CB B:PRO887 3.6 12.1 1.0 CD2 B:HIS141 3.7 11.8 1.0 CA B:GLY490 3.7 13.2 1.0 CA B:PRO887 3.7 10.7 1.0 C B:GLY490 3.7 13.0 1.0 NE2 B:HIS141 3.7 11.4 1.0 CB B:LEU888 3.9 11.8 1.0 CA B:GLN491 3.9 10.5 1.0 CG B:LEU888 3.9 12.2 1.0 HG3 B:GLN493 3.9 22.2 0.3 CD1 B:LEU888 3.9 15.2 1.0 CG B:GLN493 4.0 18.5 0.3 N B:GLN493 4.0 12.8 0.3 N B:GLN493 4.0 11.2 0.7 HG1 B:THR492 4.0 13.8 0.0 C B:PRO887 4.0 11.4 1.0 CB B:GLN491 4.0 11.5 1.0 C B:GLN491 4.1 11.0 1.0 HA2 B:GLY490 4.2 15.8 1.0 HB3 B:GLN493 4.2 17.0 0.7 CA B:LEU888 4.2 12.5 1.0 CA B:THR492 4.3 11.2 1.0 H B:LEU889 4.3 18.6 1.0 HB2 B:GLN493 4.3 17.0 0.7 HB2 B:GLN493 4.4 19.9 0.3 HD12 B:LEU888 4.4 18.3 1.0 HB2 B:GLN491 4.4 13.8 1.0 CB B:THR492 4.5 11.4 1.0 C B:THR492 4.6 13.0 1.0 CB B:GLN493 4.6 16.6 0.3 CB B:GLN493 4.6 14.2 0.7 HD13 B:LEU888 4.7 18.3 1.0 N B:GLY490 4.7 12.0 1.0 O B:GLY490 4.7 15.6 1.0 HG23 B:THR492 4.8 13.5 1.0 HB3 B:LEU888 4.8 14.2 1.0 HA B:GLN491 4.8 12.7 1.0 HA B:LEU888 4.9 15.0 1.0 CA B:GLN493 4.9 14.0 0.3 O B:PHE489 4.9 17.6 1.0 CA B:GLN493 5.0 12.4 0.7 CG B:HIS141 5.0 10.8 1.0 HA3 B:GLY886 5.0 13.8 1.0

T.Kuga, N.Sunagawa, K.Igarashi. 11 Cysteine-to-Serine Mutations Improve Stability of Cellodextrin Phosphorylase From Clostridium Thermocellum To Be Published.