Chlorine in PDB 9gf1: Cysteine-Less Human Galectin-3 C173S Mutant Carbohydrate Recognition Domain

The structure of Cysteine-Less Human Galectin-3 C173S Mutant Carbohydrate Recognition Domain, PDB code: 9gf1 was solved by J.Blaha, Y.Dubanych, O.Skorepa, O.Vanek, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	42.75 / 1.50
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	37.02, 58.047, 63.184, 90, 90, 90
R / Rfree (%)	16.1 / 18.6

The binding sites of Chlorine atom in the Cysteine-Less Human Galectin-3 C173S Mutant Carbohydrate Recognition Domain (pdb code 9gf1). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 3 binding sites of Chlorine where determined in the Cysteine-Less Human Galectin-3 C173S Mutant Carbohydrate Recognition Domain, PDB code: 9gf1:
Jump to Chlorine binding site number: 1; 2; 3;

Chlorine binding site 1 out of 3 in the Cysteine-Less Human Galectin-3 C173S Mutant Carbohydrate Recognition Domain


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Cysteine-Less Human Galectin-3 C173S Mutant Carbohydrate Recognition Domain within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl202 b:18.6 occ:1.00 H A:LYS115 2.4 13.7 1.0 H A:LYS116 2.8 13.6 1.0 HG13 A:VAL114 3.0 13.5 1.0 O A:HOH435 3.1 19.3 1.0 HG3 A:LYS116 3.1 15.1 1.0 N A:LYS115 3.3 13.3 1.0 HA A:VAL114 3.4 13.3 1.0 HD2 A:LYS116 3.4 16.5 1.0 HB2 A:LYS115 3.5 17.6 1.0 N A:LYS116 3.6 13.5 1.0 HB2 A:LYS116 3.7 13.7 1.0 CG A:LYS116 3.8 15.2 1.0 HG2 A:LYS115 3.8 19.9 1.0 CG1 A:VAL114 4.0 13.6 1.0 CD A:LYS116 4.0 16.6 1.0 CA A:LYS115 4.1 14.5 1.0 C A:VAL114 4.1 13.7 1.0 HE3 A:LYS116 4.1 17.8 1.0 CA A:VAL114 4.1 13.5 1.0 CB A:LYS115 4.1 17.5 1.0 CB A:LYS116 4.1 13.3 1.0 C A:LYS115 4.2 14.4 1.0 HG11 A:VAL114 4.4 13.5 1.0 CG A:LYS115 4.4 21.4 1.0 HH11 A:ARG40 4.5 18.5 1.0 CA A:LYS116 4.5 13.2 1.0 NH1 A:ARG40 4.5 18.7 1.0 HG12 A:VAL114 4.5 13.5 1.0 CE A:LYS116 4.5 17.8 1.0 HD3 A:ARG40 4.6 15.9 1.0 O A:HOH365 4.6 22.1 1.0 CB A:VAL114 4.6 13.3 1.0 HG21 A:VAL114 4.6 13.9 1.0 O A:HOH332 4.6 17.5 1.0 HG2 A:LYS116 4.6 15.1 1.0 HG3 A:LYS115 4.7 19.9 1.0 CZ A:ARG40 4.7 18.4 1.0 HZ1 A:LYS116 4.7 18.6 1.0 HH12 A:ARG40 4.8 18.5 1.0 NE A:ARG40 4.8 16.5 1.0 HD3 A:LYS116 4.8 16.5 1.0 O A:ARG113 5.0 14.8 1.0 HA A:LYS115 5.0 14.8 1.0 HB3 A:LYS115 5.0 17.6 1.0

Chlorine binding site 2 out of 3 in the Cysteine-Less Human Galectin-3 C173S Mutant Carbohydrate Recognition Domain


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Cysteine-Less Human Galectin-3 C173S Mutant Carbohydrate Recognition Domain within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl203 b:32.8 occ:1.00 HH11 A:ARG113 2.3 13.3 1.0 O A:HOH394 2.7 18.4 1.0 HA3 A:GLY71 2.8 15.2 1.0 O A:HOH449 2.8 31.7 1.0 HB A:THR64 2.8 12.0 1.0 O A:HOH381 2.9 20.8 1.0 HD3 A:ARG113 3.0 13.3 1.0 NH1 A:ARG113 3.1 13.2 1.0 HD2 A:ARG113 3.1 13.3 1.0 CD A:ARG113 3.5 13.5 1.0 HH12 A:ARG113 3.5 13.3 1.0 HG22 A:THR64 3.7 11.9 1.0 CB A:THR64 3.7 11.9 1.0 CA A:GLY71 3.8 15.4 1.0 HG21 A:THR64 3.9 11.9 1.0 HD12 A:LEU66 3.9 16.4 1.0 H A:ARG72 3.9 16.5 1.0 HD11 A:LEU66 3.9 16.4 1.0 CG2 A:THR64 4.0 12.0 1.0 HA2 A:GLY71 4.0 15.2 1.0 CZ A:ARG113 4.1 13.3 1.0 O A:THR64 4.1 12.5 1.0 HG A:LEU66 4.1 15.4 1.0 HB3 A:ARG113 4.2 12.4 1.0 NE A:ARG113 4.2 13.1 1.0 H A:GLY71 4.3 15.9 1.0 H A:THR64 4.3 12.3 1.0 CD1 A:LEU66 4.3 16.9 1.0 N A:GLY71 4.4 15.6 1.0 HG1 A:THR64 4.4 12.4 0.0 N A:ARG72 4.6 16.2 1.0 OG1 A:THR64 4.6 12.4 1.0 O A:HOH427 4.6 35.8 1.0 O A:HOH303 4.6 38.1 1.0 OD1 A:ASN63 4.6 12.7 1.0 CA A:THR64 4.6 11.6 1.0 C A:THR64 4.7 11.8 1.0 CG A:ARG113 4.7 13.0 1.0 C A:GLY71 4.7 14.5 1.0 CG A:LEU66 4.8 15.3 1.0 HB2 A:ARG113 4.8 12.4 1.0 CB A:ARG113 4.8 12.2 1.0 N A:THR64 4.9 12.2 1.0 HG23 A:THR64 5.0 11.9 1.0

Chlorine binding site 3 out of 3 in the Cysteine-Less Human Galectin-3 C173S Mutant Carbohydrate Recognition Domain


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 3 of Cysteine-Less Human Galectin-3 C173S Mutant Carbohydrate Recognition Domain within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl204 b:45.7 occ:1.00 H A:TYR136 2.4 14.6 1.0 HB2 A:SER135 3.0 18.0 1.0 HA A:SER135 3.1 15.6 1.0 N A:TYR136 3.3 14.4 1.0 O A:TYR136 3.5 15.6 1.0 CB A:SER135 3.7 18.3 1.0 CA A:SER135 3.7 14.7 1.0 CE1 A:TYR136 3.9 16.0 1.0 CD1 A:TYR136 3.9 14.6 1.0 CZ A:TYR136 3.9 16.1 1.0 CG A:TYR136 4.0 14.3 1.0 C A:SER135 4.0 15.4 1.0 CD2 A:TYR136 4.0 15.8 1.0 CE2 A:TYR136 4.1 16.2 1.0 HB3 A:SER135 4.1 18.0 1.0 CA A:TYR136 4.2 14.2 1.0 C A:TYR136 4.3 13.8 1.0 HE1 A:TYR136 4.3 15.7 1.0 HD1 A:TYR136 4.3 14.9 1.0 HD2 A:TYR136 4.5 15.6 1.0 O A:HOH402 4.5 34.9 1.0 HE2 A:TYR136 4.5 16.0 1.0 HD12 A:LEU9 4.5 20.1 1.0 OH A:TYR136 4.6 17.7 1.0 CB A:TYR136 4.7 14.5 1.0 OG A:SER135 4.8 21.1 1.0 HH A:TYR136 4.8 17.7 0.0

J.Blaha, Y.Dubanych, O.Skorepa, O.Vanek. Galectin-3 Carbohydrate Recognition Is Solely Responsible For Its Binding to the Nk Cell Activation Receptor NKP30. To Be Published.