› 8g69

X-ray diffraction
1.53Å resolution

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-148259 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Tyrosine-protein phosphatase non-receptor type 1 Chains: A, B
Molecule details ›
Chains: A, B
Length: 298 amino acids
Theoretical weight: 34.72 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P18031 (Residues: 1-298; Coverage: 69%)
Gene names: PTP1B, PTPN1
Sequence domains: Protein-tyrosine phosphatase

Ligands and Environments

3 bound ligands:
Ligand YXN 2 x YXN
Ligand MG 1 x MG
Ligand MPD 1 x MPD
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I03
Spacegroup: P43212
Unit cell:
a: 88.07Å b: 88.07Å c: 162.36Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.171 0.169 0.198
Expression system: Escherichia coli

Quick links

Citations

2 citation in other articles

A Conserved Local Structural Motif Controls the Kinetics of PTP1B Catalysis.
Yeh et al. (2023)
1 more

4 mentions without citation

Discovery and Validation of the Binding Poses of Allosteric Fragment Hits to Protein Tyrosine Phosphatase 1b: From Molecular Dynamics Simulations to X-ray Crystallography.
Greisman et al. (2023)
3 more