Bromine in PDB 9c56: Crystal Structure of Human PTPN2 in Complex with Allosteric Inhibitor

All present enzymatic activity of Crystal Structure of Human PTPN2 in Complex with Allosteric Inhibitor:
3.1.3.48;

The structure of Crystal Structure of Human PTPN2 in Complex with Allosteric Inhibitor, PDB code: 9c56 was solved by S.M.Bester, R.Linwood, W.-I.Wu, T.-C.Mou, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	41.77 / 2.43
Space group	C 2 2 21
Cell size a, b, c (Å), α, β, γ (°)	83.549, 225.084, 36.602, 90, 90, 90
R / Rfree (%)	19.9 / 24.6

The binding sites of Bromine atom in the Crystal Structure of Human PTPN2 in Complex with Allosteric Inhibitor (pdb code 9c56). This binding sites where shown within 5.0 Angstroms radius around Bromine atom.
In total 2 binding sites of Bromine where determined in the Crystal Structure of Human PTPN2 in Complex with Allosteric Inhibitor, PDB code: 9c56:
Jump to Bromine binding site number: 1; 2;

Bromine binding site 1 out of 2 in the Crystal Structure of Human PTPN2 in Complex with Allosteric Inhibitor


Mono view


Stereo pair view

A full contact list of Bromine with other atoms in the Br binding site number 1 of Crystal Structure of Human PTPN2 in Complex with Allosteric Inhibitor within 5.0Å range: probe atom residue distance (Å) B Occ A:Br401 b:100.5 occ:0.71 BR26 A:FRJ401 0.0 100.5 0.7 C20 A:FRJ401 1.9 83.1 0.7 C19 A:FRJ401 2.8 77.1 0.7 C21 A:FRJ401 2.9 82.3 0.7 O25 A:FRJ401 3.0 83.0 0.7 O A:HOH626 3.6 65.8 1.0 C11 A:FRJ401 4.2 72.8 0.7 C22 A:FRJ401 4.2 85.5 0.7 O A:CYS278 4.3 98.7 1.0 SG A:CYS278 4.4 95.3 1.0 CD1 A:ILE279 4.5 88.8 1.0 C23 A:FRJ401 4.7 81.4 0.7 C14 A:FRJ401 4.9 67.1 0.7 C A:CYS278 5.0 92.7 1.0

Bromine binding site 2 out of 2 in the Crystal Structure of Human PTPN2 in Complex with Allosteric Inhibitor


Mono view


Stereo pair view

A full contact list of Bromine with other atoms in the Br binding site number 2 of Crystal Structure of Human PTPN2 in Complex with Allosteric Inhibitor within 5.0Å range: probe atom residue distance (Å) B Occ A:Br401 b:83.3 occ:0.71 BR24 A:FRJ401 0.0 83.3 0.7 C22 A:FRJ401 1.9 85.5 0.7 C23 A:FRJ401 2.8 81.4 0.7 C21 A:FRJ401 2.9 82.3 0.7 O25 A:FRJ401 3.1 83.0 0.7 OE1 A:GLU201 3.2 88.4 1.0 O A:PHE197 3.7 44.6 1.0 CB A:PHE197 4.0 53.5 1.0 C A:PHE197 4.0 48.0 1.0 CD A:LYS198 4.0 65.4 1.0 NZ A:LYS198 4.1 68.1 1.0 C11 A:FRJ401 4.2 72.8 0.7 C20 A:FRJ401 4.2 83.1 0.7 N A:LYS198 4.4 44.8 1.0 CE A:LYS198 4.4 72.6 1.0 CD A:GLU201 4.5 84.8 1.0 CA A:PHE197 4.6 53.7 1.0 C19 A:FRJ401 4.7 77.1 0.7 CB A:GLU201 4.7 53.2 1.0 CA A:LYS198 4.7 47.0 1.0 OD1 A:ASN194 4.8 62.7 1.0

S.M.Bester, R.Linwood, R.Kataoka, W.I.Wu, T.C.Mou. Enhancing the Apo Protein Tyrosine Phosphatase Non-Receptor Type 2 Crystal Soaking Strategy Through Inhibitor-Accessible Binding Sites. Acta Crystallogr.,Sect.F 2024.
ISSN: ESSN 2053-230X
PubMed: 39177701
DOI: 10.1107/S2053230X24007866