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Magnesium in PDB 5m0x: Structure of Apo Structure of GH36 Alpha-Galactosidase From Thermotoga Maritima

Enzymatic activity of Structure of Apo Structure of GH36 Alpha-Galactosidase From Thermotoga Maritima

All present enzymatic activity of Structure of Apo Structure of GH36 Alpha-Galactosidase From Thermotoga Maritima:
3.2.1.22;

Protein crystallography data

The structure of Structure of Apo Structure of GH36 Alpha-Galactosidase From Thermotoga Maritima, PDB code: 5m0x 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) 32.09 / 1.80
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 67.960, 95.780, 97.540, 90.00, 90.00, 90.00
R / Rfree (%) 18.6 / 23.1

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Structure of Apo Structure of GH36 Alpha-Galactosidase From Thermotoga Maritima (pdb code 5m0x). 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 Apo Structure of GH36 Alpha-Galactosidase From Thermotoga Maritima, PDB code: 5m0x:

Magnesium binding site 1 out of 1 in 5m0x

Go back to Magnesium Binding Sites List in 5m0x
Magnesium binding site 1 out of 1 in the Structure of Apo Structure of GH36 Alpha-Galactosidase From Thermotoga Maritima


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Structure of Apo Structure of GH36 Alpha-Galactosidase From Thermotoga Maritima within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg601

b:23.6
occ:1.00
O A:HOH857 2.0 23.5 1.0
O A:HOH873 2.0 22.9 1.0
OD2 A:ASP419 2.0 23.2 1.0
O A:HOH752 2.1 22.4 1.0
OD2 A:ASP454 2.1 22.0 1.0
O A:HOH871 2.1 22.8 1.0
CG A:ASP419 3.1 23.7 1.0
CG A:ASP454 3.2 23.1 1.0
OD1 A:ASP419 3.3 22.1 1.0
OD1 A:ASP454 3.7 24.2 1.0
O A:HOH783 3.9 23.7 1.0
NE2 A:HIS418 3.9 22.1 1.0
O A:HOH979 4.2 46.2 1.0
O A:HOH761 4.3 28.4 1.0
O A:HOH848 4.3 33.5 1.0
O A:GLY483 4.3 25.7 1.0
O A:HOH1000 4.4 37.7 1.0
CB A:ASP454 4.4 22.2 1.0
CB A:ASP419 4.5 22.5 1.0
CD2 A:HIS418 4.7 19.2 1.0
O A:HOH788 4.8 44.9 1.0
CE1 A:HIS418 4.8 22.4 1.0
O A:HOH866 4.9 40.5 1.0
O A:ASP454 4.9 20.7 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 21:07:47 2024

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