Chlorine in PDB 6sjz: HSNMT1 in Complex with Both Myrcoa and Acetylated-Gncfskpr Substrates

All present enzymatic activity of HSNMT1 in Complex with Both Myrcoa and Acetylated-Gncfskpr Substrates:
2.3.1.97;

The structure of HSNMT1 in Complex with Both Myrcoa and Acetylated-Gncfskpr Substrates, PDB code: 6sjz 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)	48.89 / 2.00
Space group	P 21 21 2
Cell size a, b, c (Å), α, β, γ (°)	79.908, 178.900, 58.379, 90.00, 90.00, 90.00
R / Rfree (%)	17.2 / 20.2

The binding sites of Chlorine atom in the HSNMT1 in Complex with Both Myrcoa and Acetylated-Gncfskpr Substrates (pdb code 6sjz). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 2 binding sites of Chlorine where determined in the HSNMT1 in Complex with Both Myrcoa and Acetylated-Gncfskpr Substrates, PDB code: 6sjz:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in the HSNMT1 in Complex with Both Myrcoa and Acetylated-Gncfskpr Substrates


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of HSNMT1 in Complex with Both Myrcoa and Acetylated-Gncfskpr Substrates within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl502 b:39.8 occ:1.00 O A:HOH861 3.0 49.1 1.0 O A:HOH859 3.2 41.9 1.0 N A:VAL132 3.3 30.6 1.0 N A:SER485 3.3 17.3 1.0 NZ A:LYS289 3.4 40.7 1.0 OG A:SER485 3.5 28.1 1.0 O A:VAL132 3.7 28.1 1.0 CA A:PRO484 3.8 18.5 1.0 CB A:SER485 4.0 25.1 1.0 CB A:VAL132 4.0 25.0 1.0 CA A:VAL132 4.0 26.7 1.0 C A:PRO484 4.1 16.8 1.0 CA A:VAL131 4.1 40.9 1.0 C A:VAL131 4.2 35.8 1.0 CE A:LYS289 4.2 32.9 1.0 CA A:SER485 4.2 19.6 1.0 CG1 A:VAL131 4.3 39.4 1.0 C A:VAL132 4.4 28.9 1.0 CB A:PRO484 4.5 20.1 1.0 CG2 A:VAL132 4.6 29.6 1.0 O A:GLU130 4.6 44.4 1.0 O A:CYS483 4.7 17.2 1.0 CB A:VAL131 4.8 43.6 1.0 O A:HOH831 4.9 46.5 1.0

Chlorine binding site 2 out of 2 in the HSNMT1 in Complex with Both Myrcoa and Acetylated-Gncfskpr Substrates


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of HSNMT1 in Complex with Both Myrcoa and Acetylated-Gncfskpr Substrates within 5.0Å range: probe atom residue distance (Å) B Occ B:Cl504 b:39.5 occ:1.00 N B:LEU163 3.1 25.4 1.0 ND1 B:HIS211 3.2 17.3 1.0 CZ3 B:TRP206 3.2 23.6 1.0 NH2 B:ARG202 3.2 27.4 1.0 NE B:ARG202 3.3 29.9 1.0 CE1 B:HIS211 3.4 17.9 1.0 O B:LEU161 3.5 23.6 1.0 CH2 B:TRP206 3.6 25.9 1.0 CZ B:ARG202 3.7 27.8 1.0 CB B:LEU163 3.7 21.1 1.0 CG B:LEU163 3.9 25.2 1.0 CA B:ASP162 3.9 27.8 1.0 CA B:LEU163 3.9 26.7 1.0 C B:ASP162 3.9 26.9 1.0 CE3 B:TRP206 3.9 19.9 1.0 OD1 B:ASP162 4.1 26.7 1.0 N B:GLY164 4.4 27.5 1.0 CD B:ARG202 4.5 26.8 1.0 CG B:HIS211 4.5 18.1 1.0 C B:LEU161 4.5 26.6 1.0 CD1 B:LEU163 4.5 26.6 1.0 CG B:ARG202 4.6 20.0 1.0 C B:LEU163 4.6 27.2 1.0 CZ2 B:TRP206 4.6 26.6 1.0 N B:ASP162 4.7 25.1 1.0 NE2 B:HIS211 4.7 20.9 1.0 CA B:PRO208 4.8 20.3 1.0 CD2 B:TRP206 4.9 18.0 1.0 CB B:ASP162 4.9 26.4 1.0 CG B:ASP162 5.0 33.1 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