Magnesium in PDB 2f71: Protein Tyrosine Phosphatase 1B with Sulfamic Acid Inhibitors

All present enzymatic activity of Protein Tyrosine Phosphatase 1B with Sulfamic Acid Inhibitors:
3.1.3.48;

The structure of Protein Tyrosine Phosphatase 1B with Sulfamic Acid Inhibitors, PDB code: 2f71 was solved by A.G.Evdokimov, M.E.Pokross, S.R.Klopfenstein, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	36.00 / 1.55
Space group	P 31 2 1
Cell size a, b, c (Å), α, β, γ (°)	88.189, 88.189, 105.115, 90.00, 90.00, 120.00
R / Rfree (%)	15.2 / 17.2

The structure of Protein Tyrosine Phosphatase 1B with Sulfamic Acid Inhibitors also contains other interesting chemical elements:

Chlorine

(Cl)

4 atoms

The binding sites of Magnesium atom in the Protein Tyrosine Phosphatase 1B with Sulfamic Acid Inhibitors (pdb code 2f71). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total only one binding site of Magnesium was determined in the Protein Tyrosine Phosphatase 1B with Sulfamic Acid Inhibitors, PDB code: 2f71:

Magnesium binding site 1 out of 1 in the Protein Tyrosine Phosphatase 1B with Sulfamic Acid Inhibitors


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Protein Tyrosine Phosphatase 1B with Sulfamic Acid Inhibitors within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg602 b:22.8 occ:1.00 O A:HOH711 2.0 27.1 1.0 O A:HOH925 2.0 39.3 1.0 O A:HOH727 2.0 35.8 1.0 O A:HOH699 2.1 34.7 1.0 O A:HOH805 2.2 32.6 1.0 OE1 A:GLU130 4.1 15.7 1.0 O A:HOH793 4.3 37.8 1.0 OE1 A:GLU129 4.3 17.3 1.0 OE2 A:GLU130 4.3 18.8 1.0 O A:HOH826 4.5 36.5 1.0 CD A:GLU130 4.6 16.6 1.0

S.R.Klopfenstein, A.G.Evdokimov, A.-O.Colson, N.T.Fairweather, J.J.Neuman, M.B.Maier, J.L.Gray, G.S.Gerwe, G.E.Stake, B.W.Howard, J.A.Farmer, M.E.Pokross, T.R.Downs, B.Kasibhatla, K.G.Peters. 1,2,3,4-Tetrahydroisoquinolinyl Sulfamic Acids As Phosphatase PTP1B Inhibitors Bioorg.Med.Chem.Lett. V. 16 1574 2006.
ISSN: ISSN 0960-894X
PubMed: 16386905
DOI: 10.1016/J.BMCL.2005.12.051