Chlorine in PDB 2nz6: Crystal Structure of the Ptprj Inactivating Mutant C1239S

All present enzymatic activity of Crystal Structure of the Ptprj Inactivating Mutant C1239S:
3.1.3.48;

The structure of Crystal Structure of the Ptprj Inactivating Mutant C1239S, PDB code: 2nz6 was solved by E.Ugochukwu, A.Barr, P.Savitsky, A.C.W.Pike, G.Bunkoczi, M.Sundstrom, J.Weigelt, C.H.Arrowsmith, A.Edwards, F.Von Delft, S.Knapp, Structuralgenomics Consortium (Sgc), with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	46.98 / 2.30
Space group	H 3
Cell size a, b, c (Å), α, β, γ (°)	88.521, 88.521, 118.950, 90.00, 90.00, 120.00
R / Rfree (%)	18.2 / 22.8

The structure of Crystal Structure of the Ptprj Inactivating Mutant C1239S also contains other interesting chemical elements:

Nickel

(Ni)

5 atoms

The binding sites of Chlorine atom in the Crystal Structure of the Ptprj Inactivating Mutant C1239S (pdb code 2nz6). 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 the Ptprj Inactivating Mutant C1239S, PDB code: 2nz6:

Chlorine binding site 1 out of 1 in the Crystal Structure of the Ptprj Inactivating Mutant C1239S


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 the Ptprj Inactivating Mutant C1239S within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl208 b:41.3 occ:1.00 O A:HOH87 3.7 34.9 1.0 N A:LYS1140 3.9 32.4 1.0 NH2 A:ARG1245 4.0 26.6 1.0 NH1 A:ARG1245 4.0 26.7 1.0 O A:LYS1140 4.1 34.5 1.0 CB A:THR1139 4.2 31.1 1.0 CA A:THR1139 4.3 31.1 1.0 CZ A:ARG1245 4.4 26.7 1.0 C A:THR1139 4.6 31.9 1.0 CG2 A:THR1139 4.7 30.1 1.0 C A:LYS1140 4.7 33.5 1.0 CA A:LYS1140 4.8 33.0 1.0 CB A:SER1240 4.9 30.0 1.0

A.J.Barr, E.Ugochukwu, W.H.Lee, O.N.King, P.Filippakopoulos, I.Alfano, P.Savitsky, N.A.Burgess-Brown, S.Muller, S.Knapp. Large-Scale Structural Analysis of the Classical Human Protein Tyrosine Phosphatome. Cell(Cambridge,Mass.) V. 136 352 2009.
ISSN: ISSN 0092-8674
PubMed: 19167335
DOI: 10.1016/J.CELL.2008.11.038