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Magnesium in PDB 6fnr: Ergothioneine-Biosynthetic Methyltransferase Egtd in Complex with Chlorohistidine

Enzymatic activity of Ergothioneine-Biosynthetic Methyltransferase Egtd in Complex with Chlorohistidine

All present enzymatic activity of Ergothioneine-Biosynthetic Methyltransferase Egtd in Complex with Chlorohistidine:
2.1.1.44;

Protein crystallography data

The structure of Ergothioneine-Biosynthetic Methyltransferase Egtd in Complex with Chlorohistidine, PDB code: 6fnr was solved by A.Vit, W.Blankenfeldt, F.P.Seebeck, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 41.81 / 1.83
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 71.153, 79.211, 136.316, 90.00, 90.00, 90.00
R / Rfree (%) 15.7 / 18.3

Other elements in 6fnr:

The structure of Ergothioneine-Biosynthetic Methyltransferase Egtd in Complex with Chlorohistidine also contains other interesting chemical elements:

Chlorine (Cl) 2 atoms

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Ergothioneine-Biosynthetic Methyltransferase Egtd in Complex with Chlorohistidine (pdb code 6fnr). 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 Ergothioneine-Biosynthetic Methyltransferase Egtd in Complex with Chlorohistidine, PDB code: 6fnr:

Magnesium binding site 1 out of 1 in 6fnr

Go back to Magnesium Binding Sites List in 6fnr
Magnesium binding site 1 out of 1 in the Ergothioneine-Biosynthetic Methyltransferase Egtd in Complex with Chlorohistidine


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Ergothioneine-Biosynthetic Methyltransferase Egtd in Complex with Chlorohistidine within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg401

b:20.4
occ:1.00
 OD1 A:ASP268 2.1 24.9 1.0
O A:HOH619 2.1 21.9 1.0
CG A:ASP268 3.2 25.4 1.0
HA A:ASP268 3.2 27.3 1.0
HB3 A:ASP268 3.4 28.1 1.0
CB A:ASP268 3.6 23.4 1.0
CA A:ASP268 3.9 22.7 1.0
O A:HOH736 4.1 48.0 1.0
O A:HOH653 4.1 35.5 1.0
OD2 A:ASP268 4.2 27.9 1.0
O A:ALA265 4.4 21.9 1.0
HH21 A:ARG263 4.5 43.4 1.0
HB2 A:ASP268 4.6 28.1 1.0
O A:HOH770 4.7 53.7 1.0
H A:ASP268 4.7 26.8 1.0
N A:ASP268 4.8 22.4 1.0
HH22 A:ARG263 4.8 43.4 1.0
HA A:ALA265 4.9 26.7 1.0
C A:ASP268 4.9 22.5 1.0

Reference:

L.Misson, R.Burn, A.Vit, J.Hildesheim, M.A.Beliaeva, W.Blankenfeldt, F.P.Seebeck. Inhibition and Regulation of the Ergothioneine Biosynthetic Methyltransferase Egtd. Acs Chem. Biol. V. 13 1333 2018.
ISSN: ESSN 1554-8937
PubMed: 29658702
DOI: 10.1021/ACSCHEMBIO.8B00127
Page generated: Tue Oct 1 00:34:35 2024

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