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Magnesium in PDB 5m12: Structure of GH36 Alpha-Galactosidase From Thermotoga Maritima in Complex with Intact Cyclopropyl-Carbasugar.

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

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

Protein crystallography data

The structure of Structure of GH36 Alpha-Galactosidase From Thermotoga Maritima in Complex with Intact Cyclopropyl-Carbasugar., PDB code: 5m12 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) 43.69 / 1.53
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 68.150, 96.040, 98.120, 90.00, 90.00, 90.00
R / Rfree (%) 19.3 / 22.2

Other elements in 5m12:

The structure of Structure of GH36 Alpha-Galactosidase From Thermotoga Maritima in Complex with Intact Cyclopropyl-Carbasugar. also contains other interesting chemical elements:

Fluorine (F) 2 atoms

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Structure of GH36 Alpha-Galactosidase From Thermotoga Maritima in Complex with Intact Cyclopropyl-Carbasugar. (pdb code 5m12). 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 Intact Cyclopropyl-Carbasugar., PDB code: 5m12:

Magnesium binding site 1 out of 1 in 5m12

Go back to Magnesium Binding Sites List in 5m12
Magnesium binding site 1 out of 1 in the Structure of GH36 Alpha-Galactosidase From Thermotoga Maritima in Complex with Intact 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 Intact Cyclopropyl-Carbasugar. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg603

b:20.8
occ:1.00
 O A:HOH993 2.0 20.9 1.0
O A:HOH760 2.0 18.5 1.0
O A:HOH951 2.1 26.5 1.0
OD2 A:ASP419 2.1 20.5 1.0
O A:HOH916 2.1 22.4 1.0
OD2 A:ASP454 2.1 18.7 1.0
CG A:ASP419 3.1 21.0 1.0
CG A:ASP454 3.2 21.2 1.0
OD1 A:ASP419 3.4 21.6 1.0
OD1 A:ASP454 3.6 19.3 1.0
NE2 A:HIS418 4.0 16.7 1.0
O A:HOH877 4.0 22.0 1.0
O A:HOH756 4.2 23.4 1.0
O A:HOH793 4.3 28.9 1.0
O A:HOH1060 4.4 36.4 1.0
O A:GLY483 4.4 20.9 1.0
CB A:ASP454 4.5 18.1 1.0
CB A:ASP419 4.5 17.2 1.0
O A:HOH939 4.7 48.0 1.0
CD2 A:HIS418 4.8 16.3 1.0
CE1 A:HIS418 4.8 17.2 1.0
O A:ASP454 5.0 19.0 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: Mon Dec 14 20:49:58 2020

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