› 2cmb

X-ray diffraction
1.7Å resolution

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

Released:
DOI: 10.2210/pdb2cmb/pdb
PDB entry 2cmb coloured by chain, front view.
PDB entry 2cmb coloured by chain, side view.
PDB entry 2cmb 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: 304 amino acids
Theoretical weight: 35.55 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P18031 (Residues: 2-298; Coverage: 68%)
Gene names: PTP1B, PTPN1
Sequence domains: Protein-tyrosine phosphatase
Structure domains: Protein tyrosine phosphatase superfamily

Ligands and Environments

2 bound ligands:
Ligand F17 1 x F17
Ligand BOG 1 x BOG
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU MICROMAX-007
Spacegroup: P212121
Unit cell:
a: 60.95Å b: 71.16Å c: 83.78Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.197 0.197 0.217
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

3 review citations

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

6 mentions without citation

Moving Beyond Active-Site Detection: MixMD Applied to Allosteric Systems.
Ghanakota et al. (2016)
5 more