Chlorine in PDB 5zs8: Acetylation of Lysine 100 of Phosphoglycerate Mutase 1 Complexed with KH_OL

All present enzymatic activity of Acetylation of Lysine 100 of Phosphoglycerate Mutase 1 Complexed with KH_OL:
5.4.2.11; 5.4.2.4;

The structure of Acetylation of Lysine 100 of Phosphoglycerate Mutase 1 Complexed with KH_OL, PDB code: 5zs8 was solved by L.L.Jiang, L.Zhou, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	49.67 / 2.20
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	78.743, 83.101, 100.368, 90.00, 90.00, 90.00
R / Rfree (%)	17.9 / 22

The binding sites of Chlorine atom in the Acetylation of Lysine 100 of Phosphoglycerate Mutase 1 Complexed with KH_OL (pdb code 5zs8). 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 Acetylation of Lysine 100 of Phosphoglycerate Mutase 1 Complexed with KH_OL, PDB code: 5zs8:

Chlorine binding site 1 out of 1 in the Acetylation of Lysine 100 of Phosphoglycerate Mutase 1 Complexed with KH_OL


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Acetylation of Lysine 100 of Phosphoglycerate Mutase 1 Complexed with KH_OL within 5.0Å range: probe atom residue distance (Å) B Occ B:Cl301 b:30.8 occ:1.00 NH2 C:ARG83 3.3 27.2 1.0 NE1 C:TRP68 3.3 27.4 1.0 NH1 C:ARG83 3.3 24.9 1.0 NE1 B:TRP68 3.3 28.2 1.0 NH1 B:ARG83 3.3 23.6 1.0 NH2 B:ARG83 3.3 25.7 1.0 CZ C:ARG83 3.7 29.1 1.0 CZ B:ARG83 3.8 28.7 1.0 CG2 C:VAL81 4.0 24.8 1.0 CB C:VAL81 4.0 25.1 1.0 CG2 B:VAL81 4.1 24.4 1.0 CB B:VAL81 4.1 27.8 1.0 CG1 C:VAL81 4.1 21.8 1.0 CE2 B:TRP68 4.1 26.5 1.0 CE2 C:TRP68 4.2 29.1 1.0 CD1 C:TRP68 4.2 26.0 1.0 CD1 B:TRP68 4.2 25.2 1.0 CG1 B:VAL81 4.4 28.4 1.0 CZ2 B:TRP68 4.4 28.7 1.0 CZ2 C:TRP68 4.5 24.9 1.0

L.L.Jiang, L.Zhou. Acetylation of Lysine 100 of Phosphoglycerate Mutase 1 Complexed with KH_OL To Be Published.