Magnesium in PDB 6skj: DELTAC2 C-Terminal Truncation of HSNMT1 in Complex with Myrcoa and Gncfskpr Substrates

All present enzymatic activity of DELTAC2 C-Terminal Truncation of HSNMT1 in Complex with Myrcoa and Gncfskpr Substrates:
2.3.1.97;

The structure of DELTAC2 C-Terminal Truncation of HSNMT1 in Complex with Myrcoa and Gncfskpr Substrates, PDB code: 6skj was solved by C.Dian, F.B.Riviere, T.Asensio, C.Giglione, T.Meinnel, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	49.37 / 2.80
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	92.965, 58.270, 154.132, 90.00, 90.92, 90.00
R / Rfree (%)	18.9 / 21.9

The binding sites of Magnesium atom in the DELTAC2 C-Terminal Truncation of HSNMT1 in Complex with Myrcoa and Gncfskpr Substrates (pdb code 6skj). 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 DELTAC2 C-Terminal Truncation of HSNMT1 in Complex with Myrcoa and Gncfskpr Substrates, PDB code: 6skj:

Magnesium binding site 1 out of 1 in the DELTAC2 C-Terminal Truncation of HSNMT1 in Complex with Myrcoa and Gncfskpr Substrates


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of DELTAC2 C-Terminal Truncation of HSNMT1 in Complex with Myrcoa and Gncfskpr Substrates within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg504 b:24.8 occ:1.00 O B:HOH635 2.5 23.0 1.0 ND1 B:HIS426 3.3 22.8 1.0 O B:THR429 3.6 24.8 1.0 CE1 B:HIS426 4.0 22.1 1.0 C B:THR427 4.1 30.9 1.0 O B:THR427 4.1 34.3 1.0 C B:THR429 4.3 24.5 1.0 N B:GLN428 4.3 29.6 1.0 CG B:HIS426 4.4 20.5 1.0 C B:GLN428 4.4 27.1 1.0 CA B:GLN428 4.4 29.8 1.0 O B:GLN428 4.5 29.3 1.0 CA B:PRO430 4.5 25.4 1.0 CA B:THR427 4.5 25.3 1.0 N B:PRO430 4.6 21.7 1.0 CB B:HIS426 4.7 20.5 1.0 N B:THR427 4.7 25.6 1.0 C B:HIS426 4.7 26.1 1.0 O B:HIS426 4.8 26.3 1.0 N B:THR429 4.9 25.4 1.0

C.Dian, I.Perez-Dorado, F.Riviere, T.Asensio, P.Legrand, M.Ritzefeld, M.Shen, E.Cota, T.Meinnel, E.W.Tate, C.Giglione. High-Resolution Snapshots of Human N-Myristoyltransferase in Action Illuminate A Mechanism Promoting N-Terminal Lys and Gly Myristoylation. Nat Commun V. 11 1132 2020.
ISSN: ESSN 2041-1723
PubMed: 32111831
DOI: 10.1038/S41467-020-14847-3