› 8exk

X-ray diffraction
2.1Å resolution

Crystal structure of PTP1B D181A/Q262A phosphatase domain with JAK2 activation loop phosphopeptide

Released:
DOI: 10.2210/pdb8exk/pdb
PDB entry 8exk coloured by chain, front view.
PDB entry 8exk coloured by chain, side view.
PDB entry 8exk coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structure guided studies of the interaction between PTP1B and JAK.
Morris R, Keating N, Tan C, Chen H, Laktyushin A, Saiyed T, Liau NPD, Nicola NA, Tiganis T, Kershaw NJ, Babon JJ
Commun Biol 6 641 (2023)
PMID: 37316570

Function and Biology Details

Reactions catalysed: 
Protein tyrosine phosphate + H(2)O = protein tyrosine + phosphate
ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate
Biochemical function:
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-220462 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Tyrosine-protein phosphatase non-receptor type 1 Chain: A
Molecule details ›
Chain: A
Length: 297 amino acids
Theoretical weight: 34.47 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P18031 (Residues: 3-299; Coverage: 68%)
Gene names: PTP1B, PTPN1
Sequence domains: Protein-tyrosine phosphatase
Tyrosine-protein kinase JAK2 Chain: B
Molecule details ›
Chain: B
Length: 16 amino acids
Theoretical weight: 1.93 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: O60674 (Residues: 1000-1015; Coverage: 1%)
Gene name: JAK2

Ligands and Environments

1 bound ligand:
Ligand PO4 1 x PO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: AUSTRALIAN SYNCHROTRON BEAMLINE MX2
Spacegroup: P43212
Unit cell:
a: 88.493Å b: 88.493Å c: 130.411Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.219 0.216 0.25
Expression systems:
  • Escherichia coli
  • Not provided

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