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Magnesium in PDB 4rih: Chimeric Glycosyltransferase LANGT2S8AC, Carbasugar Substrate Complex

Protein crystallography data

The structure of Chimeric Glycosyltransferase LANGT2S8AC, Carbasugar Substrate Complex, PDB code: 4rih was solved by H.K.Tam, S.Gerhardt, B.Breit, A.Bechthold, O.Einsle, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 38.52 / 2.22
Space group P 1
Cell size a, b, c (Å), α, β, γ (°) 52.870, 59.030, 64.280, 80.08, 69.08, 86.45
R / Rfree (%) 17.5 / 21.2

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Chimeric Glycosyltransferase LANGT2S8AC, Carbasugar Substrate Complex (pdb code 4rih). 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 Chimeric Glycosyltransferase LANGT2S8AC, Carbasugar Substrate Complex, PDB code: 4rih:

Magnesium binding site 1 out of 1 in 4rih

Go back to Magnesium Binding Sites List in 4rih
Magnesium binding site 1 out of 1 in the Chimeric Glycosyltransferase LANGT2S8AC, Carbasugar Substrate Complex


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Chimeric Glycosyltransferase LANGT2S8AC, Carbasugar Substrate Complex within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mg402

b:47.7
occ:1.00
OD2 B:ASP150 2.3 40.5 1.0
O B:HOH626 2.3 22.7 1.0
O B:HOH609 2.6 37.3 1.0
CG B:ASP150 3.3 34.2 1.0
OD1 B:ASP150 3.7 35.8 1.0
O B:ASP150 4.0 27.0 1.0
O B:HOH564 4.2 33.6 1.0
CE1 B:HIS86 4.3 31.8 1.0
C B:ASP150 4.4 25.7 1.0
CB B:ASP150 4.6 22.9 1.0
N B:GLU151 4.8 22.2 1.0
CA B:GLU151 4.9 22.7 1.0

Reference:

H.K.Tam, J.Harle, S.Gerhardt, J.Rohr, G.Wang, J.S.Thorson, A.Bigot, M.Lutterbeck, W.Seiche, B.Breit, A.Bechthold, O.Einsle. Structural Characterization of O- and C-Glycosylating Variants of the Landomycin Glycosyltransferase LANGT2. Angew.Chem.Int.Ed.Engl. 2015.
ISSN: ESSN 1521-3773
PubMed: 25581707
DOI: 10.1002/ANIE.201409792
Page generated: Tue Aug 20 03:08:08 2024

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