Chlorine in PDB 2h03: Structural Studies of Protein Tyrosine Phosphatase Beta Catalytic Domain in Complex with Inhibitors

All present enzymatic activity of Structural Studies of Protein Tyrosine Phosphatase Beta Catalytic Domain in Complex with Inhibitors:
3.1.3.48;

The structure of Structural Studies of Protein Tyrosine Phosphatase Beta Catalytic Domain in Complex with Inhibitors, PDB code: 2h03 was solved by A.G.Evdokimov, M.E.Pokross, R.L.Walter, M.Mekel, J.L.Gray, K.G.Peters, M.B.Maier, K.D.Amarasinghe, C.M.Clark, R.Nichols, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	27.60 / 1.65
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	112.316, 38.934, 66.062, 90.00, 103.91, 90.00
R / Rfree (%)	18 / 21.7

The structure of Structural Studies of Protein Tyrosine Phosphatase Beta Catalytic Domain in Complex with Inhibitors also contains other interesting chemical elements:

Magnesium

(Mg)

2 atoms

The binding sites of Chlorine atom in the Structural Studies of Protein Tyrosine Phosphatase Beta Catalytic Domain in Complex with Inhibitors (pdb code 2h03). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 2 binding sites of Chlorine where determined in the Structural Studies of Protein Tyrosine Phosphatase Beta Catalytic Domain in Complex with Inhibitors, PDB code: 2h03:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in the Structural Studies of Protein Tyrosine Phosphatase Beta Catalytic Domain in Complex with Inhibitors


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Structural Studies of Protein Tyrosine Phosphatase Beta Catalytic Domain in Complex with Inhibitors within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl302 b:24.9 occ:1.00 N A:ASN1767 3.3 19.7 1.0 CA A:GLY1765 3.5 18.9 1.0 N A:PHE1768 3.5 18.9 1.0 N A:ASN1766 3.6 23.0 1.0 CB A:ASN1767 3.7 20.9 1.0 C A:GLY1765 3.7 21.6 1.0 O A:PHE1768 3.8 20.5 1.0 CA A:ASN1767 3.8 20.0 1.0 C A:ASN1767 4.0 19.9 1.0 OE2 A:GLU1771 4.3 22.8 1.0 CD A:GLU1771 4.3 22.0 1.0 O A:HOH95 4.4 32.5 1.0 C A:ASN1766 4.4 21.6 1.0 ND2 A:ASN1767 4.4 29.8 1.0 CA A:PHE1768 4.4 17.6 1.0 N A:GLY1765 4.4 17.1 1.0 CB A:PHE1768 4.5 19.8 1.0 CG A:ASN1767 4.5 23.6 1.0 C A:PHE1768 4.5 18.3 1.0 CA A:ASN1766 4.5 22.7 1.0 O A:GLY1765 4.6 23.3 1.0 CB A:GLU1771 4.6 16.7 1.0 CG A:GLU1771 4.7 17.4 1.0 OE1 A:GLU1771 4.7 26.8 1.0 O A:HOH42 4.9 23.7 1.0

Chlorine binding site 2 out of 2 in the Structural Studies of Protein Tyrosine Phosphatase Beta Catalytic Domain in Complex with Inhibitors


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Structural Studies of Protein Tyrosine Phosphatase Beta Catalytic Domain in Complex with Inhibitors within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl305 b:26.1 occ:1.00 N A:ARG1770 3.1 18.6 1.0 O A:HOH82 3.1 25.5 1.0 N A:PRO1764 3.6 19.9 1.0 CA A:PRO1764 3.6 21.5 1.0 CB A:TYR1762 3.6 18.1 1.0 CB A:PRO1764 3.6 21.4 1.0 CB A:ARG1769 3.7 18.6 1.0 CA A:ARG1770 3.9 17.9 1.0 CD A:PRO1764 3.9 22.4 1.0 CG A:ARG1770 3.9 18.8 1.0 CA A:ARG1769 3.9 16.8 1.0 C A:ARG1769 4.0 19.3 1.0 C A:ILE1763 4.0 20.4 1.0 CG A:PRO1764 4.3 22.7 1.0 O A:HOH199 4.3 36.9 1.0 C A:TYR1762 4.4 18.8 1.0 O A:ILE1763 4.4 19.6 1.0 CG A:TYR1762 4.4 19.5 1.0 O A:TYR1762 4.5 22.3 1.0 CB A:ARG1770 4.5 16.5 1.0 N A:ILE1763 4.5 16.7 1.0 CA A:TYR1762 4.7 16.9 1.0 CA A:ILE1763 4.7 18.6 1.0 CG A:ARG1769 4.8 15.7 1.0

K.K.Amarasinghe, A.G.Evdokimov, K.Xu, C.M.Clark, M.B.Maier, A.Srivastava, A.O.Colson, G.S.Gerwe, G.E.Stake, B.W.Howard, M.E.Pokross, J.L.Gray, K.G.Peters. Design and Synthesis of Potent, Non-Peptidic Inhibitors of Hptpbeta. Bioorg.Med.Chem.Lett. V. 16 4252 2006.
ISSN: ISSN 0960-894X
PubMed: 16759857
DOI: 10.1016/J.BMCL.2006.05.074