Magnesium in PDB 2hc2: Engineered Protein Tyrosine Phosphatase Beta Catalytic Domain

All present enzymatic activity of Engineered Protein Tyrosine Phosphatase Beta Catalytic Domain:
3.1.3.48;

The structure of Engineered Protein Tyrosine Phosphatase Beta Catalytic Domain, PDB code: 2hc2 was solved by A.G.Evdokimov, M.Pokross, R.Walter, M.Mekel, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	33.67 / 1.40
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	38.314, 70.775, 49.846, 90.00, 92.52, 90.00
R / Rfree (%)	14.4 / 17.9

The structure of Engineered Protein Tyrosine Phosphatase Beta Catalytic Domain also contains other interesting chemical elements:

Sodium

(Na)

2 atoms

The binding sites of Magnesium atom in the Engineered Protein Tyrosine Phosphatase Beta Catalytic Domain (pdb code 2hc2). 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 Engineered Protein Tyrosine Phosphatase Beta Catalytic Domain, PDB code: 2hc2:

Magnesium binding site 1 out of 1 in the Engineered Protein Tyrosine Phosphatase Beta Catalytic Domain


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Engineered Protein Tyrosine Phosphatase Beta Catalytic Domain within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg401 b:16.7 occ:1.00 O A:HOH2 2.0 18.4 1.0 O A:HOH5 2.0 18.1 1.0 O A:HOH3 2.1 21.9 1.0 O A:HOH6 2.1 21.4 1.0 O A:HOH1 2.2 15.9 1.0 O A:HOH4 2.2 14.9 1.0 OD2 A:ASP1821 4.2 15.3 1.0 O A:HOH84 4.2 27.2 1.0 O A:HOH29 4.4 15.9 1.0 OD2 A:ASP1819 4.4 19.0 1.0 CB A:ASP1821 4.7 12.0 1.0 CG A:ASP1821 4.9 12.0 1.0

A.G.Evdokimov, M.Pokross, R.Walter, M.Mekel, B.Cox, C.Li, R.Bechard, F.Genbauffe, R.Andrews, C.Diven, B.Howard, V.Rastogi, J.Gray, M.Maier, K.G.Peters. Engineering the Catalytic Domain of Human Protein Tyrosine Phosphatase Beta For Structure-Based Drug Discovery. Acta Crystallogr.,Sect.D V. 62 1435 2006.
ISSN: ISSN 0907-4449
PubMed: 17139078
DOI: 10.1107/S0907444906037784