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Magnesium in PDB 6fnq: Ergothioneine-Biosynthetic Methyltransferase Egtd in Complex with N,N, N-Trimethylhistidine (Hercynine)

Enzymatic activity of Ergothioneine-Biosynthetic Methyltransferase Egtd in Complex with N,N, N-Trimethylhistidine (Hercynine)

All present enzymatic activity of Ergothioneine-Biosynthetic Methyltransferase Egtd in Complex with N,N, N-Trimethylhistidine (Hercynine):
2.1.1.44;

Protein crystallography data

The structure of Ergothioneine-Biosynthetic Methyltransferase Egtd in Complex with N,N, N-Trimethylhistidine (Hercynine), PDB code: 6fnq 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) 49.33 / 1.75
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 71.040, 79.377, 136.045, 90.00, 90.00, 90.00
R / Rfree (%) 15.2 / 17.9

Magnesium Binding Sites:

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

Magnesium binding site 1 out of 1 in 6fnq

Go back to Magnesium Binding Sites List in 6fnq
Magnesium binding site 1 out of 1 in the Ergothioneine-Biosynthetic Methyltransferase Egtd in Complex with N,N, N-Trimethylhistidine (Hercynine)


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 N,N, N-Trimethylhistidine (Hercynine) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg402

b:11.6
occ:1.00
 O A:HOH614 2.0 18.2 1.0
OD1 A:ASP268 2.0 23.2 1.0
CG A:ASP268 3.2 21.5 1.0
HA A:ASP268 3.2 21.8 1.0
HB3 A:ASP268 3.5 22.8 1.0
CB A:ASP268 3.7 19.1 1.0
CA A:ASP268 3.9 18.2 1.0
O A:HOH682 4.0 34.5 1.0
O A:HOH809 4.1 35.2 1.0
OD2 A:ASP268 4.2 24.4 1.0
O A:ALA265 4.4 17.2 1.0
HH21 A:ARG263 4.5 39.8 0.6
HB2 A:ASP268 4.6 22.8 1.0
HH11 A:ARG263 4.6 39.8 0.4
H A:ASP268 4.7 20.9 1.0
N A:ASP268 4.8 17.5 1.0
HH22 A:ARG263 4.9 39.8 0.6
HH12 A:ARG263 4.9 39.8 0.4
HA A:ALA265 5.0 20.8 1.0
C A:ASP268 5.0 18.2 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: Wed Aug 13 06:09:31 2025

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