› 6d3f

X-ray diffraction
2.27Å resolution

Crystal Structure of the PTP epsilon D2 domain

Released:
DOI: 10.2210/pdb6d3f/pdb
PDB entry 6d3f coloured by chain, front view.
PDB entry 6d3f coloured by chain, side view.
PDB entry 6d3f coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
High-resolution crystal structures of the D1 and D2 domains of protein tyrosine phosphatase epsilon for structure-based drug design.
Lountos GT, Raran-Kurussi S, Zhao BM, Dyas BK, Burke TR, Ulrich RG, Waugh DS
Acta Crystallogr D Struct Biol 74 1015-1026 (2018)
PMID: 30289412

Function and Biology Details

Reaction catalysed: 
Protein tyrosine phosphate + H(2)O = protein tyrosine + phosphate
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-149979 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Receptor-type tyrosine-protein phosphatase epsilon Chains: A, B
Molecule details ›
Chains: A, B
Length: 279 amino acids
Theoretical weight: 32.33 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P23469 (Residues: 425-700; Coverage: 41%)
Gene name: PTPRE
Sequence domains: Protein-tyrosine phosphatase

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 22-ID
Spacegroup: P21
Unit cell:
a: 56.337Å b: 74.3Å c: 75.725Å
α: 90° β: 91.98° γ: 90°
R-values:
R R work R free
0.177 0.173 0.236
Expression system: Escherichia coli

Quick links

Citations

1 citations in other articles

A novel binding pocket in the D2 domain of protein tyrosine phosphatase mu (PTPmu) guides AI screen to identify small molecules that modulate tumour cell adhesion, growth and migration.
Molyneaux et al. (2023)

2 mentions without citation

The homophilic receptor PTPRK selectively dephosphorylates multiple junctional regulators to promote cell-cell adhesion.
Fearnley et al. (2019)
1 more