Chlorine in PDB 4mov: 1.45 A Resolution Crystal Structure of Protein Phosphatase 1

All present enzymatic activity of 1.45 A Resolution Crystal Structure of Protein Phosphatase 1:
3.1.3.16;

The structure of 1.45 A Resolution Crystal Structure of Protein Phosphatase 1, PDB code: 4mov was solved by M.S.Choy, W.Peti, R.Page, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	46.93 / 1.45
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	65.724, 77.600, 133.035, 90.00, 90.00, 90.00
R / Rfree (%)	15 / 16.7

The structure of 1.45 A Resolution Crystal Structure of Protein Phosphatase 1 also contains other interesting chemical elements:

Manganese

(Mn)

4 atoms

The binding sites of Chlorine atom in the 1.45 A Resolution Crystal Structure of Protein Phosphatase 1 (pdb code 4mov). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 2 binding sites of Chlorine where determined in the 1.45 A Resolution Crystal Structure of Protein Phosphatase 1, PDB code: 4mov:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in the 1.45 A Resolution Crystal Structure of Protein Phosphatase 1


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of 1.45 A Resolution Crystal Structure of Protein Phosphatase 1 within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl404 b:15.1 occ:1.00 NZ A:LYS113 3.1 11.9 1.0 O A:HOH760 3.3 39.4 1.0 CE A:LYS113 3.7 12.9 1.0 CD A:LYS113 3.8 15.2 1.0 OD2 A:ASP10 4.6 21.1 1.0 CD1 A:LEU9 5.0 17.7 1.0

Chlorine binding site 2 out of 2 in the 1.45 A Resolution Crystal Structure of Protein Phosphatase 1


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of 1.45 A Resolution Crystal Structure of Protein Phosphatase 1 within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl405 b:27.1 occ:1.00 N A:GLY215 3.0 22.8 1.0 N A:GLU230 3.2 18.7 1.0 C A:GLY228 3.4 17.3 1.0 N A:VAL231 3.5 19.0 1.0 CA A:GLY228 3.5 17.7 1.0 CB A:GLU230 3.5 23.1 1.0 N A:ALA229 3.7 16.2 1.0 CA A:GLU230 3.7 18.1 1.0 CA A:GLY215 3.8 27.2 1.0 O A:GLY228 3.8 18.6 1.0 CG2 A:VAL231 3.9 23.2 1.0 N A:GLY228 3.9 19.4 1.0 O A:VAL213 4.0 32.4 1.0 C A:GLN214 4.0 46.7 1.0 CA A:GLN214 4.0 40.8 1.0 C A:GLU230 4.0 18.0 1.0 C A:ALA229 4.2 20.1 1.0 O A:GLY215 4.3 24.2 1.0 CG A:GLU230 4.5 45.0 1.0 CB A:VAL231 4.5 18.0 1.0 CA A:ALA229 4.5 19.9 1.0 CA A:VAL231 4.5 19.9 1.0 C A:GLY215 4.5 32.0 1.0 C A:VAL213 4.8 32.6 1.0 O A:HOH611 4.9 23.8 1.0 N A:GLN214 4.9 34.5 1.0 CB A:GLN214 5.0 41.6 1.0

M.S.Choy, M.Hieke, G.S.Kumar, G.R.Lewis, K.R.Gonzalez-Dewhitt, R.P.Kessler, B.J.Stein, M.Hessenberger, A.C.Nairn, W.Peti, R.Page. Understanding the Antagonism of Retinoblastoma Protein Dephosphorylation By Pnuts Provides Insights Into the PP1 Regulatory Code. Proc.Natl.Acad.Sci.Usa V. 111 4097 2014.
ISSN: ISSN 0027-8424
PubMed: 24591642
DOI: 10.1073/PNAS.1317395111