Chlorine in PDB 5j8c: Human Mof C316S, E350Q Crystal Structure

All present enzymatic activity of Human Mof C316S, E350Q Crystal Structure:
2.3.1.48;

The structure of Human Mof C316S, E350Q Crystal Structure, PDB code: 5j8c was solved by C.E.Mccullough, R.Marmorstein, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	27.84 / 2.17
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	46.148, 55.676, 122.311, 90.00, 90.00, 90.00
R / Rfree (%)	19.1 / 23.4

The structure of Human Mof C316S, E350Q Crystal Structure also contains other interesting chemical elements:

Zinc	(Zn)	1 atom
Sodium	(Na)	2 atoms

The binding sites of Chlorine atom in the Human Mof C316S, E350Q Crystal Structure (pdb code 5j8c). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 2 binding sites of Chlorine where determined in the Human Mof C316S, E350Q Crystal Structure, PDB code: 5j8c:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in the Human Mof C316S, E350Q Crystal Structure


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Human Mof C316S, E350Q Crystal Structure within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl502 b:34.6 occ:1.00 O A:HOH621 3.0 28.6 1.0 O A:HOH635 3.0 30.6 1.0 N A:ASP190 3.4 29.4 1.0 CA A:ILE189 3.8 32.3 1.0 OD2 A:ASP190 4.0 35.5 1.0 C A:ILE189 4.1 34.1 1.0 O A:GLU188 4.2 32.1 1.0 CG2 A:ILE189 4.2 30.0 1.0 CG A:ASP190 4.2 35.6 1.0 CB A:ASP190 4.2 32.9 1.0 CA A:ASP190 4.4 32.6 1.0 O A:HOH636 4.5 43.0 1.0 CB A:ILE189 4.6 33.1 1.0 O A:ASP190 4.8 27.5 1.0 N A:ILE189 4.8 30.4 1.0 O A:HOH601 4.9 35.7 1.0 C A:GLU188 4.9 34.6 1.0 OD1 A:ASP190 4.9 35.4 1.0

Chlorine binding site 2 out of 2 in the Human Mof C316S, E350Q Crystal Structure


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Human Mof C316S, E350Q Crystal Structure within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl503 b:52.2 occ:1.00 N A:LYS330 3.3 33.2 1.0 O A:HOH665 3.4 31.1 1.0 N A:GLY327 3.4 37.8 1.0 N A:GLY329 3.4 33.8 1.0 CA A:GLY327 3.4 38.4 1.0 C A:GLY327 3.6 38.2 1.0 CG A:LYS330 3.7 47.5 1.0 CA A:GLY329 3.7 33.5 1.0 O A:HOH616 3.9 35.8 1.0 C A:GLY329 3.9 37.9 1.0 N A:TYR328 4.0 35.3 1.0 CB A:LYS330 4.1 37.6 1.0 O A:GLY327 4.1 39.8 1.0 CA A:LYS330 4.3 37.7 1.0 CE A:LYS330 4.4 56.1 1.0 CD A:LYS330 4.4 52.4 1.0 C A:TYR328 4.5 34.4 1.0 N A:ARG326 4.6 43.4 1.0 CA A:ARG325 4.7 44.2 1.0 C A:ARG326 4.7 42.9 1.0 N A:ARG325 4.8 41.7 1.0 CA A:TYR328 4.9 36.3 1.0 C A:ARG325 4.9 45.2 1.0 OG A:SER360 4.9 40.1 1.0

C.E.Mccullough, S.Song, M.H.Shin, F.B.Johnson, R.Marmorstein. Structural and Functional Role of Acetyltransferase Hmof K274 Autoacetylation. J.Biol.Chem. V. 291 18190 2016.
ISSN: ESSN 1083-351X
PubMed: 27382063
DOI: 10.1074/JBC.M116.736264