Chlorine in PDB 6sk8: DELTAC3 C-Terminal Truncation of HSNMT1 in Complex with Myrcoa and Gdcfskpr Substrates

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

The structure of DELTAC3 C-Terminal Truncation of HSNMT1 in Complex with Myrcoa and Gdcfskpr Substrates, PDB code: 6sk8 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)	49.31 / 1.87
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	92.622, 58.256, 154.789, 90.00, 91.26, 90.00
R / Rfree (%)	20.8 / 24.4

The binding sites of Chlorine atom in the DELTAC3 C-Terminal Truncation of HSNMT1 in Complex with Myrcoa and Gdcfskpr Substrates (pdb code 6sk8). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total only one binding site of Chlorine was determined in the DELTAC3 C-Terminal Truncation of HSNMT1 in Complex with Myrcoa and Gdcfskpr Substrates, PDB code: 6sk8:

Chlorine binding site 1 out of 1 in the DELTAC3 C-Terminal Truncation of HSNMT1 in Complex with Myrcoa and Gdcfskpr Substrates


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of DELTAC3 C-Terminal Truncation of HSNMT1 in Complex with Myrcoa and Gdcfskpr Substrates within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl505 b:39.8 occ:1.00 O A:HOH906 2.5 34.9 1.0 NH2 A:ARG202 2.9 29.4 1.0 ND1 A:HIS211 3.0 26.6 1.0 NE A:ARG202 3.0 28.7 1.0 N A:LEU163 3.2 26.0 1.0 CE1 A:HIS211 3.3 23.7 1.0 CZ3 A:TRP206 3.3 27.9 1.0 CZ A:ARG202 3.3 29.3 1.0 O A:LEU161 3.6 22.5 1.0 CH2 A:TRP206 3.8 31.8 1.0 CB A:LEU163 3.8 25.6 1.0 CG A:LEU163 3.8 24.4 1.0 O A:HOH642 3.9 31.6 1.0 CE3 A:TRP206 3.9 27.7 1.0 CA A:ASP162 4.0 28.9 1.0 CA A:LEU163 4.0 26.1 1.0 C A:ASP162 4.1 25.8 1.0 OD1 A:ASP162 4.1 29.6 1.0 CD A:ARG202 4.3 23.6 1.0 CG A:HIS211 4.3 24.2 1.0 N A:GLY164 4.4 29.3 1.0 CG A:ARG202 4.5 25.5 1.0 CD1 A:LEU163 4.5 28.6 1.0 C A:LEU161 4.6 27.3 1.0 CZ2 A:TRP206 4.6 28.0 1.0 NE2 A:HIS211 4.6 21.3 1.0 NH1 A:ARG202 4.7 32.5 1.0 C A:LEU163 4.7 30.9 1.0 CD2 A:TRP206 4.7 21.8 1.0 CA A:PRO208 4.8 27.7 1.0 N A:ASP162 4.8 27.6 1.0 CG A:ASP162 5.0 31.2 1.0 CB A:HIS211 5.0 21.5 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