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Magnesium in PDB 5l6e: Crystal Structure of the Human METTL3-METTL14 Complex Bound to Sam

Enzymatic activity of Crystal Structure of the Human METTL3-METTL14 Complex Bound to Sam

All present enzymatic activity of Crystal Structure of the Human METTL3-METTL14 Complex Bound to Sam:
2.1.1.62;

Protein crystallography data

The structure of Crystal Structure of the Human METTL3-METTL14 Complex Bound to Sam, PDB code: 5l6e was solved by P.Sledz, M.Jinek, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 44.61 / 1.90
Space group P 32 2 1
Cell size a, b, c (Å), α, β, γ (°) 63.949, 63.949, 225.858, 90.00, 90.00, 120.00
R / Rfree (%) 15.7 / 18.3

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Crystal Structure of the Human METTL3-METTL14 Complex Bound to Sam (pdb code 5l6e). 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 Crystal Structure of the Human METTL3-METTL14 Complex Bound to Sam, PDB code: 5l6e:

Magnesium binding site 1 out of 1 in 5l6e

Go back to Magnesium Binding Sites List in 5l6e
Magnesium binding site 1 out of 1 in the Crystal Structure of the Human METTL3-METTL14 Complex Bound to Sam


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Crystal Structure of the Human METTL3-METTL14 Complex Bound to Sam within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg602

b:43.0
occ:1.00
OD2 A:ASP552 2.2 27.5 1.0
O A:HOH832 2.2 42.8 1.0
O A:HOH708 2.2 32.2 1.0
O A:HOH803 2.4 28.6 1.0
CG A:ASP552 3.0 38.5 1.0
OD1 A:ASP552 3.2 28.5 1.0
O A:HOH861 4.3 53.3 1.0
CB A:ASP552 4.4 26.8 1.0
O A:HOH793 4.6 43.4 1.0
HB3 A:ASP552 4.6 32.2 1.0
HB2 A:ASP552 4.7 32.2 1.0

Reference:

P.Sledz, M.Jinek. Structural Insights Into the Molecular Mechanism of the M(6)A Writer Complex. Elife V. 5 2016.
ISSN: ESSN 2050-084X
PubMed: 27627798
DOI: 10.7554/ELIFE.18434
Page generated: Mon Dec 14 20:45:20 2020

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