Magnesium in PDB 6sk3: C-Terminal HSNMT1 DELTAC3 Truncation in Complex with Both Myrcoa and Gncfskpr Substrates

Enzymatic activity of C-Terminal HSNMT1 DELTAC3 Truncation in Complex with Both Myrcoa and Gncfskpr Substrates

All present enzymatic activity of C-Terminal HSNMT1 DELTAC3 Truncation in Complex with Both Myrcoa and Gncfskpr Substrates:
2.3.1.97;

Protein crystallography data

The structure of C-Terminal HSNMT1 DELTAC3 Truncation in Complex with Both Myrcoa and Gncfskpr Substrates, PDB code: 6sk3 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) 46.87 / 2.70
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 91.806, 58.074, 148.212, 90.00, 92.25, 90.00
R / Rfree (%) 24.6 / 26.9

Magnesium Binding Sites:

The binding sites of Magnesium atom in the C-Terminal HSNMT1 DELTAC3 Truncation in Complex with Both Myrcoa and Gncfskpr Substrates (pdb code 6sk3). 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 C-Terminal HSNMT1 DELTAC3 Truncation in Complex with Both Myrcoa and Gncfskpr Substrates, PDB code: 6sk3:

Magnesium binding site 1 out of 1 in 6sk3

Go back to Magnesium Binding Sites List in 6sk3
Magnesium binding site 1 out of 1 in the C-Terminal HSNMT1 DELTAC3 Truncation in Complex with Both 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 C-Terminal HSNMT1 DELTAC3 Truncation in Complex with Both Myrcoa and Gncfskpr Substrates within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mg503

b:41.4
occ:1.00
 O9A B:MYA502 3.0 43.7 1.0
O B:SER116 3.4 45.4 1.0
O8A B:MYA502 3.6 42.0 1.0
P3X B:MYA502 3.8 39.5 1.0
NH2 B:ARG258 4.3 74.1 1.0
N B:GLN118 4.4 43.5 1.0
C B:SER116 4.6 45.9 1.0
CB B:GLN118 4.8 43.5 1.0
CA B:TYR117 4.8 44.2 1.0
O7A B:MYA502 4.8 41.0 1.0
C3X B:MYA502 4.9 41.3 1.0
O3X B:MYA502 4.9 40.4 1.0

Reference:

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
Page generated: Tue Dec 15 00:04:46 2020

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