› 2cm7

X-ray diffraction
2.1Å resolution

Structural Basis for Inhibition of Protein Tyrosine Phosphatase 1B by Isothiazolidinone Heterocyclic Phosphonate Mimetics

Released:
DOI: 10.2210/pdb2cm7/pdb
PDB entry 2cm7 coloured by chain, front view.
PDB entry 2cm7 coloured by chain, side view.
PDB entry 2cm7 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structural basis for inhibition of protein-tyrosine phosphatase 1B by isothiazolidinone heterocyclic phosphonate mimetics.
Ala PJ, Gonneville L, Hillman MC, Becker-Pasha M, Wei M, Reid BG, Klabe R, Yue EW, Wayland B, Douty B, Polam P, Wasserman Z, Bower M, Combs AP, Burn TC, Hollis GF, Wynn R
J Biol Chem 281 32784-95 (2006)
PMID: 16916797

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 domain:

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: 321 amino acids
Theoretical weight: 37.37 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P18031 (Residues: 1-321; Coverage: 74%)
Gene names: PTP1B, PTPN1
Sequence domains: Protein-tyrosine phosphatase
Structure domains: Protein tyrosine phosphatase superfamily

Ligands and Environments

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

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU MICROMAX-007
Spacegroup: P21
Unit cell:
a: 43.88Å b: 88.38Å c: 49.84Å
α: 90° β: 96.84° γ: 90°
R-values:
R R work R free
0.199 0.199 0.254
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

3 review citations

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

8 mentions without citation

Survey of phosphorylation near drug binding sites in the Protein Data Bank (PDB) and their effects.
Smith et al. (2015)
7 more