Sodium in PDB 8cqy: Crystal Structure of the PTPN3 Pdz Domain Bound to the Pbm Tace C- Terminal Peptide

All present enzymatic activity of Crystal Structure of the PTPN3 Pdz Domain Bound to the Pbm Tace C- Terminal Peptide:
3.1.3.48; 3.4.24.86;

The structure of Crystal Structure of the PTPN3 Pdz Domain Bound to the Pbm Tace C- Terminal Peptide, PDB code: 8cqy was solved by M.Genera, B.Colcombet-Cazenave, A.Croitoru, B.Raynal, A.Mechaly, J.Caillet, A.Haouz, N.Wolff, C.Caillet-Saguy, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	66.58 / 1.70
Space group	P 32 2 1
Cell size a, b, c (Å), α, β, γ (°)	76.878, 76.878, 46.253, 90, 90, 120
R / Rfree (%)	16.8 / 20.3

The binding sites of Sodium atom in the Crystal Structure of the PTPN3 Pdz Domain Bound to the Pbm Tace C- Terminal Peptide (pdb code 8cqy). This binding sites where shown within 5.0 Angstroms radius around Sodium atom.
In total 2 binding sites of Sodium where determined in the Crystal Structure of the PTPN3 Pdz Domain Bound to the Pbm Tace C- Terminal Peptide, PDB code: 8cqy:
Jump to Sodium binding site number: 1; 2;

Sodium binding site 1 out of 2 in the Crystal Structure of the PTPN3 Pdz Domain Bound to the Pbm Tace C- Terminal Peptide


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 1 of Crystal Structure of the PTPN3 Pdz Domain Bound to the Pbm Tace C- Terminal Peptide within 5.0Å range: probe atom residue distance (Å) B Occ A:Na101 b:42.7 occ:1.00 O A:HOH217 3.3 43.6 1.0 N A:LYS52 3.7 31.7 1.0 CB A:PRO51 3.8 37.2 1.0 CA A:PRO51 3.9 34.9 1.0 C A:PRO51 4.3 35.7 1.0 CG A:LYS52 4.3 32.0 1.0 CB A:LYS52 4.7 32.6 1.0 CA A:LYS52 4.7 32.3 1.0 O A:LYS52 4.8 32.4 1.0 CE A:LYS52 4.8 33.5 1.0 NH1 A:ARG96 4.8 34.2 1.0 CD A:LYS52 4.8 34.7 1.0

Sodium binding site 2 out of 2 in the Crystal Structure of the PTPN3 Pdz Domain Bound to the Pbm Tace C- Terminal Peptide


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 2 of Crystal Structure of the PTPN3 Pdz Domain Bound to the Pbm Tace C- Terminal Peptide within 5.0Å range: probe atom residue distance (Å) B Occ A:Na102 b:41.5 occ:1.00 N A:GLY64 3.0 35.6 1.0 O A:ALA91 3.1 36.0 1.0 N A:ASN63 3.5 32.1 1.0 C A:ALA91 3.6 36.6 1.0 CA A:ASN63 3.8 33.4 1.0 CG2 A:VAL93 3.8 34.2 1.0 C A:ASN63 3.8 35.6 1.0 CA A:GLY64 3.9 37.2 1.0 N A:VAL93 3.9 33.1 1.0 CB A:LEU61 3.9 31.1 1.0 CB A:ALA91 3.9 35.9 1.0 O A:LEU61 4.1 30.6 1.0 C A:ILE62 4.2 33.1 1.0 N A:LEU92 4.2 35.4 1.0 C A:LEU92 4.2 34.8 1.0 C A:LEU61 4.2 34.9 1.0 CA A:LEU92 4.3 32.0 1.0 CA A:ALA91 4.3 33.9 1.0 CD1 A:LEU10 4.4 49.5 1.0 N A:ILE62 4.4 29.4 1.0 CA A:ILE62 4.5 30.8 1.0 CB A:VAL93 4.6 29.4 1.0 CD1 A:LEU61 4.7 35.3 1.0 CA A:LEU61 4.7 31.1 1.0 CA A:VAL93 4.8 29.1 1.0 CG A:LEU61 4.9 34.0 1.0 O A:LEU92 4.9 36.4 1.0 O A:ASN63 4.9 34.6 1.0

M.Genera, B.Colcombet-Cazenave, A.Croitoru, B.Raynal, A.Mechaly, J.Caillet, A.Haouz, N.Wolff, C.Caillet-Saguy. Interactions of the Protein Tyrosine Phosphatase PTPN3 with Viral and Cellular Partners Through Its Pdz Domain: Insights Into Structural Determinants and Phosphatase Activity Front Mol Biosci V. 10 2023.
ISSN: ESSN 2296-889X