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Magnesium in PDB 2i4h: Structural Studies of Protein Tyrosine Phosphatase Beta Catalytic Domain Co-Crystallized with A Sulfamic Acid Inhibitor

Enzymatic activity of Structural Studies of Protein Tyrosine Phosphatase Beta Catalytic Domain Co-Crystallized with A Sulfamic Acid Inhibitor

All present enzymatic activity of Structural Studies of Protein Tyrosine Phosphatase Beta Catalytic Domain Co-Crystallized with A Sulfamic Acid Inhibitor:
3.1.3.48;

Protein crystallography data

The structure of Structural Studies of Protein Tyrosine Phosphatase Beta Catalytic Domain Co-Crystallized with A Sulfamic Acid Inhibitor, PDB code: 2i4h was solved by A.G.Evdokimov, M.E.Pokross, R.L.Walter, M.Mekel, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 27.37 / 2.15
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 113.313, 38.795, 66.983, 90.00, 104.94, 90.00
R / Rfree (%) 16.9 / 24.6

Other elements in 2i4h:

The structure of Structural Studies of Protein Tyrosine Phosphatase Beta Catalytic Domain Co-Crystallized with A Sulfamic Acid Inhibitor also contains other interesting chemical elements:

Chlorine (Cl) 1 atom

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Structural Studies of Protein Tyrosine Phosphatase Beta Catalytic Domain Co-Crystallized with A Sulfamic Acid Inhibitor (pdb code 2i4h). 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 Structural Studies of Protein Tyrosine Phosphatase Beta Catalytic Domain Co-Crystallized with A Sulfamic Acid Inhibitor, PDB code: 2i4h:

Magnesium binding site 1 out of 1 in 2i4h

Go back to Magnesium Binding Sites List in 2i4h
Magnesium binding site 1 out of 1 in the Structural Studies of Protein Tyrosine Phosphatase Beta Catalytic Domain Co-Crystallized with A Sulfamic Acid Inhibitor


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Structural Studies of Protein Tyrosine Phosphatase Beta Catalytic Domain Co-Crystallized with A Sulfamic Acid Inhibitor within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg202

b:28.5
occ:0.50
 O A:HOH61 2.0 15.7 0.5
O A:HOH58 2.0 25.1 1.0
O A:HOH59 2.0 15.7 1.0
O A:HOH60 2.0 16.4 0.5
OD2 A:ASP1784 4.0 10.1 1.0
O A:HOH195 4.2 12.3 1.0
N A:GLY1826 4.2 16.5 1.0
OD1 A:ASP1784 4.3 12.7 1.0
O A:HOH97 4.3 17.9 1.0
O A:TYR1824 4.4 13.6 1.0
CG A:ASP1784 4.6 12.5 1.0
CA A:GLY1826 4.9 18.9 1.0
CA A:TYR1825 5.0 13.9 1.0

Reference:

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
Page generated: Wed Aug 14 00:03:08 2024

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