› 6d4f

X-ray diffraction
1.91Å resolution

Crystal structure of PTP epsilon D2 domain (A455N/V457Y/E597D)

Released:
DOI: 10.2210/pdb6d4f/pdb
PDB entry 6d4f coloured by chain, front view.
PDB entry 6d4f coloured by chain, side view.
PDB entry 6d4f 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 Chain: A
Molecule details ›
Chain: A
Length: 279 amino acids
Theoretical weight: 32.43 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

1 bound ligand:
Ligand 1PE 1 x 1PE
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU MICROMAX-007 HF
Spacegroup: P212121
Unit cell:
a: 61.47Å b: 73.489Å c: 75.656Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.193 0.19 0.225
Expression system: Escherichia coli

Quick links

Citations

2 citation in other articles

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

1 mention without citation

High-resolution crystal structures of the D1 and D2 domains of protein tyrosine phosphatase epsilon for structure-based drug design.
Lountos et al. (2018)