Magnesium in PDB 6pau: Structure of Human NMT2 with Myristoyl-Lysine Peptide and Coa Products

All present enzymatic activity of Structure of Human NMT2 with Myristoyl-Lysine Peptide and Coa Products:
2.3.1.97;

The structure of Structure of Human NMT2 with Myristoyl-Lysine Peptide and Coa Products, PDB code: 6pau was solved by I.R.Price, H.Lin, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	67.83 / 1.93
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	63.162, 46.350, 74.395, 90.00, 114.25, 90.00
R / Rfree (%)	19.7 / 21.8

The binding sites of Magnesium atom in the Structure of Human NMT2 with Myristoyl-Lysine Peptide and Coa Products (pdb code 6pau). 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 Structure of Human NMT2 with Myristoyl-Lysine Peptide and Coa Products, PDB code: 6pau:

Magnesium binding site 1 out of 1 in the Structure of Human NMT2 with Myristoyl-Lysine Peptide and Coa Products


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Structure of Human NMT2 with Myristoyl-Lysine Peptide and Coa Products within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg501 b:70.8 occ:1.00 H A:LYS257 1.9 58.0 1.0 H A:VAL259 2.3 53.6 1.0 O25 A:4PS511 2.6 52.5 1.0 N A:LYS257 2.6 48.3 1.0 HG23 A:VAL259 2.6 48.3 1.0 HB2 A:LYS257 2.6 57.6 1.0 HA A:ARG255 2.8 50.6 1.0 H A:ARG258 2.9 60.7 1.0 O A:LEU254 3.0 44.9 1.0 HB A:VAL259 3.0 46.0 1.0 N A:ARG258 3.1 50.6 1.0 N A:VAL259 3.1 44.7 1.0 CA A:LYS257 3.1 51.0 1.0 C A:LYS257 3.2 50.0 1.0 H A:SER256 3.2 54.3 1.0 N A:SER256 3.3 45.2 1.0 CB A:LYS257 3.3 48.0 1.0 CG2 A:VAL259 3.4 40.3 1.0 O21 A:4PS511 3.5 58.9 1.0 C A:ARG255 3.5 46.0 1.0 O26 A:4PS511 3.5 56.5 1.0 HG11 A:VAL250 3.5 42.5 1.0 CA A:ARG255 3.5 42.2 1.0 CB A:VAL259 3.5 38.3 1.0 P24 A:4PS511 3.5 58.1 1.0 HG21 A:VAL259 3.7 48.3 1.0 C A:SER256 3.7 50.5 1.0 H A:ALA260 3.9 44.9 1.0 CA A:VAL259 3.9 40.8 1.0 HB3 A:LYS257 3.9 57.6 1.0 C A:LEU254 3.9 45.7 1.0 O A:LYS257 4.0 47.9 1.0 CA A:SER256 4.0 50.0 1.0 CA A:ARG258 4.0 54.9 1.0 C A:ARG258 4.0 49.3 1.0 HA A:LYS257 4.1 61.1 1.0 HA A:ARG258 4.2 65.9 1.0 HG22 A:VAL259 4.2 48.3 1.0 HA A:SER256 4.2 60.0 1.0 HG3 A:LYS257 4.2 62.8 1.0 N A:ARG255 4.2 42.8 1.0 O A:ARG255 4.2 46.5 1.0 CG A:LYS257 4.4 52.3 1.0 O23 A:4PS511 4.4 59.3 1.0 CG1 A:VAL250 4.4 35.4 1.0 P20 A:4PS511 4.5 63.6 1.0 HG12 A:VAL250 4.5 42.5 1.0 N A:ALA260 4.6 37.4 1.0 HG21 A:VAL250 4.6 41.0 1.0 HA A:VAL259 4.6 49.0 1.0 CB A:ARG255 4.7 41.1 1.0 HG2 A:ARG255 4.8 48.2 1.0 HB3 A:ARG255 4.8 49.3 1.0 O A:SER256 4.8 51.6 1.0 C A:VAL259 4.8 37.5 1.0 O27 A:4PS511 4.9 53.1 1.0 HG13 A:VAL250 4.9 42.5 1.0 HD2 A:LYS257 4.9 63.2 1.0 CG1 A:VAL259 4.9 36.4 1.0

T.Kosciuk, I.R.Price, X.Zhang, C.Zhu, K.N.Johnson, S.Zhang, S.L.Halaby, G.P.Komaniecki, M.Yang, C.J.Dehart, P.M.Thomas, N.L.Kelleher, J.Christopher Fromme, H.Lin. NMT1 and NMT2 Are Lysine Myristoyltransferases Regulating the ARF6 Gtpase Cycle. Nat Commun V. 11 1067 2020.
ISSN: ESSN 2041-1723
PubMed: 32103017
DOI: 10.1038/S41467-020-14893-X