Chlorine in PDB 8h2v: 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: 8h2v 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)	43.44 / 1.68
Space group	P 1
Cell size a, b, c (Å), α, β, γ (°)	82.277, 88.52, 88.54, 98.41, 110.69, 110.65
R / Rfree (%)	18.4 / 21.7

The binding sites of Chlorine atom in the Cellodextrin Phosphorylase From Clostridium Thermocellum Mutant - All Cysteine Residues Were Substituted with Serines (pdb code 8h2v). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 4 binding sites of Chlorine where determined in the Cellodextrin Phosphorylase From Clostridium Thermocellum Mutant - All Cysteine Residues Were Substituted with Serines, PDB code: 8h2v:
Jump to Chlorine binding site number: 1; 2; 3; 4;

Chlorine binding site 1 out of 4 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:Cl1014 b:18.5 occ:1.00 H A:LEU888 2.4 24.7 1.0 H A:THR492 2.5 19.0 1.0 H A:GLN491 2.7 22.5 1.0 HA3 A:GLY490 2.9 22.5 1.0 HB3 A:PRO887 3.0 27.1 1.0 HB2 A:LEU888 3.1 21.3 1.0 HD2 A:HIS141 3.1 17.8 1.0 H A:GLN493 3.1 23.9 1.0 HG2 A:GLN493 3.1 35.5 1.0 N A:GLN491 3.2 18.8 1.0 HA A:PRO887 3.2 22.1 1.0 N A:LEU888 3.2 20.6 1.0 HD11 A:LEU888 3.3 32.7 1.0 HB3 A:GLN491 3.3 20.1 1.0 N A:THR492 3.3 15.8 1.0 HE2 A:HIS141 3.4 18.5 0.0 OG1 A:THR492 3.5 18.2 1.0 CB A:PRO887 3.6 22.5 1.0 HG A:LEU888 3.6 22.9 1.0 HB2 A:PRO887 3.7 27.1 1.0 CA A:GLY490 3.7 18.7 1.0 CA A:PRO887 3.7 18.4 1.0 C A:GLY490 3.7 19.5 1.0 CD2 A:HIS141 3.7 14.8 1.0 CB A:LEU888 3.8 17.7 1.0 NE2 A:HIS141 3.9 15.4 1.0 N A:GLN493 3.9 19.9 1.0 CA A:GLN491 3.9 15.2 1.0 C A:PRO887 4.0 20.6 1.0 CG A:GLN493 4.0 29.6 1.0 HD21 A:LEU889 4.0 42.6 1.0 CB A:GLN491 4.0 16.7 1.0 CG A:LEU888 4.0 19.1 1.0 CD1 A:LEU888 4.1 27.3 1.0 HG3 A:GLN493 4.1 35.5 1.0 HG1 A:THR492 4.1 21.9 0.0 CA A:LEU888 4.1 21.3 1.0 C A:GLN491 4.1 17.7 1.0 HB2 A:GLN493 4.2 30.3 1.0 CA A:THR492 4.3 16.0 1.0 HA2 A:GLY490 4.3 22.5 1.0 H A:LEU889 4.3 26.5 1.0 HD23 A:LEU889 4.4 42.6 1.0 HB2 A:GLN491 4.4 20.1 1.0 CB A:THR492 4.5 16.3 1.0 C A:THR492 4.5 21.6 1.0 CD2 A:LEU889 4.5 35.5 1.0 CB A:GLN493 4.6 25.2 1.0 HD12 A:LEU888 4.6 32.7 1.0 N A:GLY490 4.6 18.9 1.0 HD22 A:LEU889 4.6 42.6 1.0 HB3 A:LEU888 4.6 21.3 1.0 H A:GLY490 4.6 22.7 1.0 O A:GLY490 4.7 17.5 1.0 HD13 A:LEU888 4.7 32.7 1.0 HG23 A:THR492 4.8 18.1 1.0 HA A:GLN491 4.8 18.3 1.0 HA A:LEU888 4.9 25.5 1.0 N A:LEU889 4.9 22.0 1.0 CA A:GLN493 4.9 20.0 1.0 C A:LEU888 4.9 26.4 1.0

Chlorine binding site 2 out of 4 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:Cl1015 b:29.4 occ:1.00 HH11 A:ARG718 2.0 33.3 0.2 NH1 A:ARG718 2.3 27.7 0.2 HH12 A:ARG718 2.4 33.3 0.2 HE A:ARG718 2.5 30.7 0.8 HD22 A:ASN752 2.5 39.0 1.0 HH21 A:ARG718 2.7 35.9 0.8 HB2 A:ASN752 2.7 33.7 1.0 HD21 A:ASN624 2.7 37.6 1.0 HB2 A:ASN624 2.7 45.8 1.0 O A:HOH1386 3.0 29.8 1.0 HD2 A:PHE750 3.2 34.5 1.0 CZ A:ARG718 3.2 29.7 0.2 NE A:ARG718 3.3 25.5 0.8 ND2 A:ASN752 3.3 32.5 1.0 HE3 A:TRP623 3.4 42.0 1.0 ND2 A:ASN624 3.4 31.4 1.0 NH2 A:ARG718 3.4 29.9 0.8 HZ3 A:TRP623 3.5 31.6 1.0 CB A:ASN752 3.5 28.1 1.0 HH22 A:ARG718 3.5 36.4 0.2 CB A:ASN624 3.6 38.2 1.0 HB3 A:ASN752 3.6 33.7 1.0 NH2 A:ARG718 3.7 30.3 0.2 CZ A:ARG718 3.8 30.2 0.8 HB3 A:PHE750 3.9 36.4 1.0 HD12 A:LEU787 3.9 33.3 1.0 CG A:ASN752 3.9 32.4 1.0 CE3 A:TRP623 3.9 35.0 1.0 HB3 A:ASN624 4.0 45.8 1.0 HD3 A:ARG718 4.0 34.0 0.2 HD21 A:ASN752 4.0 39.0 1.0 CG A:ASN624 4.0 39.8 1.0 CD2 A:PHE750 4.0 28.7 1.0 CZ3 A:TRP623 4.0 26.3 1.0 HD22 A:ASN624 4.0 37.6 1.0 H A:ASN752 4.1 33.1 1.0 HH22 A:ARG718 4.1 35.9 0.8 NE A:ARG718 4.2 28.1 0.2 HD3 A:ARG718 4.3 31.8 0.8 HG3 A:ARG718 4.4 37.4 0.2 CD A:ARG718 4.4 26.4 0.8 SD A:MET667 4.5 28.9 1.0 HD12 A:LEU627 4.5 45.6 1.0 CD A:ARG718 4.5 28.3 0.2 HH21 A:ARG718 4.5 36.4 0.2 HD22 A:LEU787 4.5 41.9 1.0 HE2 A:PHE750 4.5 41.2 1.0 HD11 A:LEU787 4.5 33.3 1.0 CD1 A:LEU787 4.6 27.7 1.0 HG A:LEU787 4.6 39.9 1.0 CE2 A:PHE750 4.7 34.3 1.0 HA A:ASN624 4.7 47.8 1.0 CA A:ASN624 4.7 39.8 1.0 CB A:PHE750 4.7 30.3 1.0 CA A:ASN752 4.7 28.8 1.0 CG A:PHE750 4.8 31.1 1.0 HG2 A:ARG718 4.8 36.8 0.8 N A:ASN752 4.8 27.6 1.0 HE A:ARG718 4.9 33.8 0.2 H A:ASN624 5.0 40.2 1.0 CG A:ARG718 5.0 31.2 0.2

Chlorine binding site 3 out of 4 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:Cl1016 b:18.5 occ:1.00 H B:LEU888 2.4 26.4 1.0 H B:THR492 2.5 19.2 1.0 H B:GLN491 2.6 19.4 1.0 HA3 B:GLY490 2.9 21.4 1.0 HB3 B:PRO887 3.0 25.7 1.0 HD2 B:HIS141 3.1 17.9 1.0 N B:GLN491 3.1 16.1 1.0 HB2 B:LEU888 3.1 20.1 1.0 H B:GLN493 3.1 23.1 1.0 HG2 B:GLN493 3.1 31.7 1.0 HA B:PRO887 3.2 22.8 1.0 N B:LEU888 3.2 22.0 1.0 HB3 B:GLN491 3.3 22.4 1.0 HD11 B:LEU888 3.3 34.1 1.0 N B:THR492 3.4 16.0 1.0 HB2 B:PRO887 3.4 25.7 1.0 HE2 B:HIS141 3.5 19.9 0.0 CB B:PRO887 3.5 21.4 1.0 OG1 B:THR492 3.6 17.4 1.0 CA B:PRO887 3.6 19.0 1.0 C B:GLY490 3.7 17.4 1.0 CA B:GLY490 3.7 17.8 1.0 CD2 B:HIS141 3.7 14.9 1.0 HG B:LEU888 3.8 24.1 1.0 CB B:LEU888 3.8 16.7 1.0 HD21 B:LEU889 3.9 47.3 1.0 N B:GLN493 3.9 19.2 1.0 NE2 B:HIS141 3.9 16.5 1.0 CA B:GLN491 3.9 17.7 1.0 C B:PRO887 4.0 22.3 1.0 CG B:GLN493 4.0 26.4 1.0 CB B:GLN491 4.0 18.6 1.0 HG3 B:GLN493 4.1 31.7 1.0 CA B:LEU888 4.1 22.2 1.0 CG B:LEU888 4.1 20.1 1.0 HG1 B:THR492 4.1 20.9 0.0 CD1 B:LEU888 4.1 28.4 1.0 C B:GLN491 4.1 18.5 1.0 HB2 B:GLN493 4.2 27.8 1.0 HD23 B:LEU889 4.2 47.3 1.0 CA B:THR492 4.3 14.5 1.0 HA2 B:GLY490 4.3 21.4 1.0 H B:LEU889 4.3 27.1 1.0 CD2 B:LEU889 4.4 39.4 1.0 HB2 B:GLN491 4.4 22.4 1.0 HD22 B:LEU889 4.5 47.3 1.0 C B:THR492 4.5 20.6 1.0 CB B:THR492 4.5 17.9 1.0 CB B:GLN493 4.5 23.1 1.0 N B:GLY490 4.6 20.4 1.0 H B:GLY490 4.6 24.4 1.0 O B:GLY490 4.7 17.4 1.0 HD13 B:LEU888 4.7 34.1 1.0 HB3 B:LEU888 4.7 20.1 1.0 HD12 B:LEU888 4.8 34.1 1.0 HA B:GLN491 4.8 21.2 1.0 N B:LEU889 4.8 22.6 1.0 HA B:LEU888 4.8 26.7 1.0 HG23 B:THR492 4.9 21.3 1.0 CA B:GLN493 4.9 20.7 1.0 C B:LEU888 4.9 25.2 1.0 CG B:PRO887 5.0 24.8 1.0 N B:PRO887 5.0 18.1 1.0

Chlorine binding site 4 out of 4 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:Cl1017 b:28.9 occ:1.00 HD21 B:ASN752 2.5 41.5 1.0 HE B:ARG718 2.5 34.2 1.0 HE3 B:MET667 2.5 24.7 0.4 HD21 B:ASN624 2.5 40.5 1.0 HH21 B:ARG718 2.6 41.2 1.0 HB2 B:ASN752 2.7 34.5 1.0 HB2 B:ASN624 2.8 45.5 1.0 O B:HOH1293 3.0 30.4 1.0 HE1 B:MET667 3.1 24.7 0.4 HD2 B:PHE750 3.2 37.1 1.0 CE B:MET667 3.2 20.7 0.4 ND2 B:ASN752 3.3 34.5 1.0 ND2 B:ASN624 3.3 33.7 1.0 NE B:ARG718 3.3 28.5 1.0 HE3 B:TRP623 3.4 44.4 1.0 NH2 B:ARG718 3.4 34.4 1.0 CB B:ASN752 3.5 28.7 1.0 HZ3 B:TRP623 3.5 31.1 1.0 HE2 B:MET667 3.5 24.7 0.4 CB B:ASN624 3.7 37.9 1.0 HB3 B:ASN752 3.7 34.5 1.0 HD12 B:LEU787 3.8 33.0 1.0 CZ B:ARG718 3.8 31.2 1.0 HB3 B:PHE750 3.8 34.6 1.0 HD22 B:ASN624 3.9 40.5 1.0 CG B:ASN752 3.9 31.3 1.0 HD22 B:ASN752 3.9 41.5 1.0 CD2 B:PHE750 3.9 30.9 1.0 CG B:ASN624 3.9 41.8 1.0 CE3 B:TRP623 4.0 37.0 1.0 CZ3 B:TRP623 4.0 25.9 1.0 HG3 B:MET667 4.0 38.1 0.4 H B:ASN752 4.1 33.5 1.0 HH22 B:ARG718 4.1 41.2 1.0 HB3 B:ASN624 4.1 45.5 1.0 HD3 B:ARG718 4.3 33.3 1.0 SD B:MET667 4.4 24.9 0.6 CD B:ARG718 4.4 27.8 1.0 HD22 B:LEU787 4.4 36.0 1.0 HD12 B:LEU627 4.4 49.6 1.0 HE2 B:PHE750 4.5 42.6 1.0 HG B:LEU787 4.6 38.8 1.0 CD1 B:LEU787 4.6 27.5 1.0 HD11 B:LEU787 4.6 33.0 1.0 HA B:ASN624 4.6 47.1 1.0 CE2 B:PHE750 4.7 35.5 1.0 CB B:PHE750 4.7 28.8 1.0 CA B:ASN752 4.7 28.2 1.0 CA B:ASN624 4.7 39.2 1.0 CG B:PHE750 4.7 29.2 1.0 SD B:MET667 4.8 26.7 0.4 N B:ASN752 4.8 27.9 1.0 HG2 B:ARG718 4.8 42.1 1.0 CG B:MET667 4.8 31.7 0.4 HD11 B:LEU627 4.9 49.6 1.0 CG B:LEU787 5.0 32.3 1.0

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