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Magnesium in PDB 3sme: Structure of PTP1B Inactivated By H2O2/Bicarbonate

Enzymatic activity of Structure of PTP1B Inactivated By H2O2/Bicarbonate

All present enzymatic activity of Structure of PTP1B Inactivated By H2O2/Bicarbonate:
3.1.3.48;

Protein crystallography data

The structure of Structure of PTP1B Inactivated By H2O2/Bicarbonate, PDB code: 3sme was solved by J.J.Tanner, H.Singh, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 44.00 / 1.70
Space group P 31 2 1
Cell size a, b, c (Å), α, β, γ (°) 88.000, 88.000, 104.000, 90.00, 90.00, 120.00
R / Rfree (%) 19.7 / 21

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Structure of PTP1B Inactivated By H2O2/Bicarbonate (pdb code 3sme). 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 Structure of PTP1B Inactivated By H2O2/Bicarbonate, PDB code: 3sme:

Magnesium binding site 1 out of 1 in 3sme

Go back to Magnesium Binding Sites List in 3sme
Magnesium binding site 1 out of 1 in the Structure of PTP1B Inactivated By H2O2/Bicarbonate


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Structure of PTP1B Inactivated By H2O2/Bicarbonate within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg299

b:35.0
occ:1.00
O A:HOH370 2.2 30.0 1.0
O A:HOH372 2.2 37.8 1.0
O A:HOH371 2.2 32.4 1.0
O A:HOH373 2.3 34.2 1.0
O A:HOH409 2.3 42.4 1.0
O A:HOH374 2.4 42.9 1.0
OE2 A:GLU130 4.1 28.9 1.0
OE2 A:GLU129 4.2 26.1 1.0
OE1 A:GLU130 4.3 29.8 1.0
O A:HOH440 4.3 45.4 1.0
O A:HOH456 4.6 39.8 1.0
O A:HOH436 4.6 51.1 1.0
CD A:GLU130 4.6 29.3 1.0

Reference:

H.Zhou, H.Singh, Z.D.Parsons, S.M.Lewis, S.Bhattacharya, D.R.Seiner, J.N.Labutti, T.J.Reilly, J.J.Tanner, K.S.Gates. The Biological Buffer Bicarbonate/Co(2) Potentiates H(2)O(2)-Mediated Inactivation of Protein Tyrosine Phosphatases. J.Am.Chem.Soc. V. 133 15803 2011.
ISSN: ISSN 0002-7863
PubMed: 21913686
DOI: 10.1021/JA2077137
Page generated: Mon Dec 14 08:51:23 2020

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