Chlorine in PDB 2bgd: Structure-Based Design of Protein Tyrosine Phosphatase-1B Inhibitors

All present enzymatic activity of Structure-Based Design of Protein Tyrosine Phosphatase-1B Inhibitors:
3.1.3.48;

The structure of Structure-Based Design of Protein Tyrosine Phosphatase-1B Inhibitors, PDB code: 2bgd was solved by E.Black, J.Breed, A.L.Breeze, K.Embrey, R.Garcia, T.W.Gero, L.Godfrey, P.W.Kenny, A.D.Morley, C.A.Minshull, A.D.Pannifer, J.Read, A.Rees, D.J.Russell, D.Toader, J.Tucker, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	29.11 / 2.40
Space group	P 31 2 1
Cell size a, b, c (Å), α, β, γ (°)	88.908, 88.908, 104.548, 90.00, 90.00, 120.00
R / Rfree (%)	16.4 / 20

The structure of Structure-Based Design of Protein Tyrosine Phosphatase-1B Inhibitors also contains other interesting chemical elements:

Sodium

(Na)

1 atom

The binding sites of Chlorine atom in the Structure-Based Design of Protein Tyrosine Phosphatase-1B Inhibitors (pdb code 2bgd). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 3 binding sites of Chlorine where determined in the Structure-Based Design of Protein Tyrosine Phosphatase-1B Inhibitors, PDB code: 2bgd:
Jump to Chlorine binding site number: 1; 2; 3;

Chlorine binding site 1 out of 3 in the Structure-Based Design of Protein Tyrosine Phosphatase-1B Inhibitors


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Structure-Based Design of Protein Tyrosine Phosphatase-1B Inhibitors within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl1299 b:26.1 occ:1.00 NH2 A:ARG45 3.2 20.7 1.0 NH1 A:ARG45 3.4 21.8 1.0 N A:ALA122 3.5 20.4 1.0 C A:CYS121 3.6 20.7 1.0 CD A:PRO89 3.7 20.5 1.0 CZ A:ARG45 3.7 20.9 1.0 CA A:ALA122 3.8 20.0 1.0 O A:CYS121 3.9 20.6 1.0 CB A:ALA122 4.0 19.7 1.0 O A:LEU119 4.1 20.7 1.0 CG A:PRO89 4.2 19.9 1.0 O A:PRO87 4.2 20.5 1.0 CD2 A:LEU88 4.3 21.9 1.0 CA A:CYS121 4.3 20.3 1.0 O A:HOH2088 4.3 18.4 1.0 N A:CYS121 4.4 20.2 1.0 CA A:LEU88 4.4 20.0 1.0 N A:PRO89 4.5 20.0 1.0 CB A:LEU119 4.6 22.2 1.0 C A:LEU119 4.7 21.5 1.0 C A:LEU88 4.9 20.0 1.0

Chlorine binding site 2 out of 3 in the Structure-Based Design of Protein Tyrosine Phosphatase-1B Inhibitors


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Structure-Based Design of Protein Tyrosine Phosphatase-1B Inhibitors within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl1300 b:32.2 occ:1.00 N A:GLY117 3.2 23.6 1.0 O A:HOH2085 3.4 34.6 1.0 N A:LYS116 3.7 24.4 1.0 CG A:MET114 3.9 25.3 1.0 CA A:GLY117 4.0 23.7 1.0 CA A:LYS116 4.1 24.9 1.0 C A:LYS116 4.1 24.5 1.0 SD A:MET114 4.2 28.0 1.0 C A:GLU115 4.4 23.1 1.0 CA A:GLU115 4.7 23.0 1.0 O A:MET114 4.8 22.6 1.0 N A:GLU115 4.9 23.1 1.0 C A:MET114 4.9 23.4 1.0

Chlorine binding site 3 out of 3 in the Structure-Based Design of Protein Tyrosine Phosphatase-1B Inhibitors


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 3 of Structure-Based Design of Protein Tyrosine Phosphatase-1B Inhibitors within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl1301 b:33.2 occ:1.00 O A:HOH2090 3.0 26.2 1.0 N A:VAL113 3.2 24.0 1.0 O A:HOH2084 3.3 21.6 1.0 CE1 A:HIS175 3.5 23.1 1.0 CG2 A:VAL113 3.7 23.8 1.0 CA A:ARG112 3.7 24.4 1.0 CB A:VAL113 3.8 24.3 1.0 CB A:ARG112 4.0 25.6 1.0 C A:ARG112 4.0 24.1 1.0 NE2 A:HIS175 4.1 24.0 1.0 CA A:VAL113 4.1 24.0 1.0 CG A:ARG112 4.1 28.6 1.0 O A:HOH2113 4.2 25.3 1.0 O A:HOH2112 4.4 35.5 1.0 CH2 A:TRP125 4.5 22.2 1.0 CE A:MET109 4.5 21.1 1.0 ND1 A:HIS175 4.7 23.4 1.0 O A:HOH2025 4.9 35.2 1.0 O A:ASN111 4.9 20.5 1.0 CZ2 A:TRP125 4.9 20.9 1.0

E.Black, J.Breed, A.L.Breeze, K.Embrey, R.Garcia, T.W.Gero, L.Godfrey, P.W.Kenny, A.D.Morley, C.A.Minshull, A.D.Pannifer, J.Read, A.Rees, D.J.Russell, D.Toader, J.Tucker. Structure-Based Design of Protein Tyrosine Phosphatase-1B Inhibitors Bioorg.Med.Chem.Lett. V. 15 2503 2005.
ISSN: ISSN 0960-894X
PubMed: 15863305
DOI: 10.1016/J.BMCL.2005.03.068