Chlorine in PDB 4nm0: Crystal Structure of Peptide Inhibitor-Free Gsk-3/Axin Complex

All present enzymatic activity of Crystal Structure of Peptide Inhibitor-Free Gsk-3/Axin Complex:
2.7.11.1; 2.7.11.26;

The structure of Crystal Structure of Peptide Inhibitor-Free Gsk-3/Axin Complex, PDB code: 4nm0 was solved by M.L.-H.Chu, J.L.Stamos, M.D.Enos, N.Shah, W.I.Weis, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	39.05 / 2.50
Space group	P 61 2 2
Cell size a, b, c (Å), α, β, γ (°)	81.303, 81.303, 280.829, 90.00, 90.00, 120.00
R / Rfree (%)	19.1 / 23.9

The structure of Crystal Structure of Peptide Inhibitor-Free Gsk-3/Axin Complex also contains other interesting chemical elements:

Magnesium

(Mg)

2 atoms

The binding sites of Chlorine atom in the Crystal Structure of Peptide Inhibitor-Free Gsk-3/Axin Complex (pdb code 4nm0). 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 Crystal Structure of Peptide Inhibitor-Free Gsk-3/Axin Complex, PDB code: 4nm0:

Chlorine binding site 1 out of 1 in the Crystal Structure of Peptide Inhibitor-Free Gsk-3/Axin Complex


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Crystal Structure of Peptide Inhibitor-Free Gsk-3/Axin Complex within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl410 b:77.1 occ:1.00 N A:LYS297 3.5 40.9 1.0 CG2 A:ILE296 3.8 39.9 1.0 CA A:ILE296 3.9 42.7 1.0 N B:ARG401 3.9 92.7 1.0 CD1 A:ILE296 3.9 43.1 1.0 C A:ILE296 4.2 42.2 1.0 CB A:LYS297 4.3 44.5 1.0 CB B:ARG401 4.3 97.3 1.0 CB A:ILE296 4.3 40.0 1.0 CA A:LYS297 4.4 43.0 1.0 CA B:GLN400 4.5 78.5 1.0 O A:GLN295 4.5 49.8 1.0 CG B:GLN400 4.5 74.8 1.0 O B:VAL399 4.7 67.3 1.0 CA B:ARG401 4.7 96.5 1.0 C B:GLN400 4.7 88.5 1.0 CG1 A:ILE296 4.8 41.3 1.0 O A:LYS297 4.8 49.6 1.0

J.L.Stamos, M.L.Chu, M.D.Enos, N.Shah, W.I.Weis. Structural Basis of Gsk-3 Inhibition By N-Terminal Phosphorylation and By the Wnt Receptor LRP6. Elife V. 3 01998 2014.
ISSN: ESSN 2050-084X
PubMed: 24642411