Chlorine in PDB 5e97: Glycoside Hydrolase Ligand Structure 1

All present enzymatic activity of Glycoside Hydrolase Ligand Structure 1:
3.2.1.166;

The structure of Glycoside Hydrolase Ligand Structure 1, PDB code: 5e97 was solved by L.Wu, G.J.Davies, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	38.42 / 1.63
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	45.880, 70.890, 78.230, 90.00, 94.91, 90.00
R / Rfree (%)	16.6 / 19.7

The binding sites of Chlorine atom in the Glycoside Hydrolase Ligand Structure 1 (pdb code 5e97). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 4 binding sites of Chlorine where determined in the Glycoside Hydrolase Ligand Structure 1, PDB code: 5e97:
Jump to Chlorine binding site number: 1; 2; 3; 4;

Chlorine binding site 1 out of 4 in the Glycoside Hydrolase Ligand Structure 1


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Glycoside Hydrolase Ligand Structure 1 within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl605 b:32.5 occ:1.00 O A:HOH889 2.9 39.1 1.0 O A:HOH861 3.0 32.2 1.0 N A:GLY239 3.3 27.2 1.0 CA A:MET278 3.6 24.8 1.0 CB A:MET278 3.7 24.3 1.0 CA A:ASN238 3.9 29.6 1.0 CB A:ASN238 3.9 31.0 1.0 CZ A:PHE236 4.0 35.7 1.0 OG A:SER281 4.0 37.3 1.0 N A:MET278 4.0 24.8 1.0 C A:ASN238 4.1 27.5 1.0 CE A:MET278 4.1 27.9 1.0 CG A:MET278 4.1 27.9 1.0 CA A:GLY239 4.3 28.1 1.0 O A:HOH865 4.5 26.3 1.0 C A:LYS277 4.5 25.8 1.0 CG A:LYS277 4.7 32.8 1.0 O A:LYS277 4.7 28.1 1.0 CE2 A:PHE236 4.7 36.5 1.0 CE1 A:PHE236 4.8 36.8 1.0 C A:MET278 4.8 23.6 1.0 CE A:LYS277 4.9 41.9 1.0 SD A:MET278 5.0 27.8 1.0

Chlorine binding site 2 out of 4 in the Glycoside Hydrolase Ligand Structure 1


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Glycoside Hydrolase Ligand Structure 1 within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl606 b:55.5 occ:1.00 O A:HOH892 3.5 30.1 1.0 O A:HOH955 3.5 45.6 1.0 ND1 A:HIS458 3.6 23.8 1.0 NZ A:LYS430 3.9 39.1 1.0 CD A:LYS430 4.1 27.2 1.0 CE1 A:HIS458 4.1 23.9 1.0 CE A:LYS430 4.5 34.8 1.0 CG A:HIS458 4.9 21.6 1.0

Chlorine binding site 3 out of 4 in the Glycoside Hydrolase Ligand Structure 1


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 3 of Glycoside Hydrolase Ligand Structure 1 within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl607 b:53.4 occ:1.00 NE2 A:GLN270 2.6 28.1 1.0 O A:HOH826 3.1 36.0 1.0 OE1 A:GLU225 3.2 32.3 1.0 N A:GLN270 3.3 20.1 1.0 N1 A:NPO612 3.4 36.3 1.0 O3 A:NPO612 3.5 39.4 1.0 C1 A:NPO612 3.5 31.2 1.0 CD A:GLN270 3.5 31.6 1.0 CA A:GLY269 3.5 20.1 1.0 CG A:GLN270 3.5 30.2 1.0 O A:HIS296 3.8 18.1 1.0 C2 A:NPO612 3.9 27.6 1.0 C A:GLY269 3.9 19.8 1.0 C6 A:NPO612 3.9 31.0 1.0 CD A:GLU225 4.1 30.0 1.0 O2 A:NPO612 4.1 42.2 1.0 OE2 A:GLU225 4.1 29.4 1.0 CB A:GLN270 4.2 25.9 1.0 C A:HIS296 4.2 17.6 1.0 CA A:GLN270 4.3 21.5 1.0 CB A:HIS296 4.4 18.6 1.0 O A:HOH951 4.5 57.6 1.0 C3 A:NPO612 4.6 25.7 1.0 N A:HIS297 4.6 17.0 1.0 CA A:HIS297 4.6 17.4 1.0 C5 A:NPO612 4.6 28.1 1.0 CD1 A:TYR298 4.7 18.4 1.0 OE1 A:GLN270 4.7 34.6 1.0 O A:HOH707 4.7 28.2 1.0 N A:TYR298 4.7 16.6 1.0 O A:HOH756 4.8 28.6 1.0 N A:GLY269 4.8 20.0 1.0 C4 A:NPO612 4.9 25.5 1.0 CA A:HIS296 5.0 18.2 1.0

Chlorine binding site 4 out of 4 in the Glycoside Hydrolase Ligand Structure 1


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 4 of Glycoside Hydrolase Ligand Structure 1 within 5.0Å range: probe atom residue distance (Å) B Occ B:Cl201 b:75.3 occ:1.00 O B:HOH338 3.2 45.1 1.0 CD B:ARG81 3.6 38.6 1.0 NH1 B:ARG81 3.7 48.5 1.0 NH1 B:ARG85 4.1 46.8 1.0 CB B:ARG81 4.2 32.3 1.0 NE B:ARG81 4.5 38.8 1.0 CZ B:ARG81 4.6 46.0 1.0 CG B:ARG81 4.6 34.8 1.0 CA B:PRO78 4.7 34.8 1.0 CB A:CYS179 4.9 42.8 1.0 CB B:PRO78 4.9 38.7 1.0

L.Wu, C.M.Viola, A.M.Brzozowski, G.J.Davies. Structural Characterization of Human Heparanase Reveals Insights Into Substrate Recognition. Nat.Struct.Mol.Biol. V. 22 1016 2015.
ISSN: ESSN 1545-9985
PubMed: 26575439
DOI: 10.1038/NSMB.3136