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Magnesium in PDB 5m16: Structure of GH36 Alpha-Galactosidase From Thermotoga Maritima in Complex with A Hydrolysed Cyclopropyl Carbasugar.

Enzymatic activity of Structure of GH36 Alpha-Galactosidase From Thermotoga Maritima in Complex with A Hydrolysed Cyclopropyl Carbasugar.

All present enzymatic activity of Structure of GH36 Alpha-Galactosidase From Thermotoga Maritima in Complex with A Hydrolysed Cyclopropyl Carbasugar.:
3.2.1.22;

Protein crystallography data

The structure of Structure of GH36 Alpha-Galactosidase From Thermotoga Maritima in Complex with A Hydrolysed Cyclopropyl Carbasugar., PDB code: 5m16 was solved by R.Pengelly, T.Gloster, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 55.66 / 1.62
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 68.300, 96.020, 98.050, 90.00, 90.00, 90.00
R / Rfree (%) 17.2 / 19.8

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Structure of GH36 Alpha-Galactosidase From Thermotoga Maritima in Complex with A Hydrolysed Cyclopropyl Carbasugar. (pdb code 5m16). 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 GH36 Alpha-Galactosidase From Thermotoga Maritima in Complex with A Hydrolysed Cyclopropyl Carbasugar., PDB code: 5m16:

Magnesium binding site 1 out of 1 in 5m16

Go back to Magnesium Binding Sites List in 5m16
Magnesium binding site 1 out of 1 in the Structure of GH36 Alpha-Galactosidase From Thermotoga Maritima in Complex with A Hydrolysed Cyclopropyl Carbasugar.


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Structure of GH36 Alpha-Galactosidase From Thermotoga Maritima in Complex with A Hydrolysed Cyclopropyl Carbasugar. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg603

b:18.9
occ:1.00
 O A:HOH723 2.0 16.9 1.0
O A:HOH955 2.1 19.7 1.0
O A:HOH953 2.1 22.2 1.0
OD2 A:ASP454 2.1 17.3 1.0
OD2 A:ASP419 2.1 18.8 1.0
O A:HOH909 2.2 19.1 1.0
CG A:ASP419 3.1 19.9 1.0
CG A:ASP454 3.2 17.9 1.0
OD1 A:ASP419 3.4 18.7 1.0
OD1 A:ASP454 3.6 17.9 1.0
O A:HOH830 3.9 21.0 1.0
NE2 A:HIS418 4.0 14.3 1.0
O A:HOH749 4.2 22.0 1.0
O A:HOH1002 4.3 44.6 1.0
O A:HOH834 4.3 29.7 1.0
CB A:ASP454 4.4 16.6 1.0
O A:GLY483 4.5 19.6 1.0
CB A:ASP419 4.5 16.4 1.0
O A:HOH1020 4.6 37.5 1.0
O A:HOH823 4.7 45.7 1.0
CD2 A:HIS418 4.8 15.4 1.0
CE1 A:HIS418 4.8 17.0 1.0
O A:ASP454 4.9 17.2 1.0

Reference:

C.Adamson, R.J.Pengelly, S.Shamsi Kazem Abadi, S.Chakladar, J.Draper, R.Britton, T.M.Gloster, A.J.Bennet. Structural Snapshots For Mechanism-Based Inactivation of A Glycoside Hydrolase By Cyclopropyl Carbasugars. Angew.Chem.Int.Ed.Engl. V. 55 14978 2016.
ISSN: ESSN 1521-3773
PubMed: 27783466
DOI: 10.1002/ANIE.201607431
Page generated: Sun Sep 29 21:08:09 2024

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