› 6d4d

X-ray diffraction
1.76Å resolution

Crystal structure of the PTP epsilon D1 domain

Released:
DOI: 10.2210/pdb6d4d/pdb
PDB entry 6d4d coloured by chain, front view.
PDB entry 6d4d coloured by chain, side view.
PDB entry 6d4d 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: 292 amino acids
Theoretical weight: 33.92 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P23469 (Residues: 107-398; Coverage: 43%)
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: C2
Unit cell:
a: 154.055Å b: 35.998Å c: 115.023Å
α: 90° β: 115.73° γ: 90°
R-values:
R R work R free
0.18 0.178 0.222
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)