› 2zmm

X-ray diffraction
2.1Å 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 Chain: A
Molecule details ›
Chain: A
Length: 299 amino acids
Theoretical weight: 34.83 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P18031 (Residues: 1-299; Coverage: 69%)
Gene names: PTP1B, PTPN1
Sequence domains: Protein-tyrosine phosphatase
Structure domains: Protein tyrosine phosphatase superfamily

Ligands and Environments

3 bound ligands:
Ligand MG 1 x MG
Ligand CL 6 x CL
Ligand 35B 1 x 35B
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: P3121
Unit cell:
a: 88.02Å b: 88.02Å c: 103.676Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.184 0.183 0.214
Expression system: Escherichia coli

Quick links

Citations

3 review citations

Bidentate inhibitors of protein tyrosine phosphatases.
Low et al. (2014)
2 more

5 mentions without citation

CSAR benchmark exercise of 2010: selection of the protein-ligand complexes.
Dunbar et al. (2011)
4 more