› 2h03

X-ray diffraction
1.65Å resolution

Structural studies of protein tyrosine phosphatase beta catalytic domain in complex with inhibitors

Released:
DOI: 10.2210/pdb2h03/pdb
PDB entry 2h03 coloured by chain, front view.
PDB entry 2h03 coloured by chain, side view.
PDB entry 2h03 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Design and synthesis of potent, non-peptidic inhibitors of HPTPbeta.
Amarasinghe KK, Evdokimov AG, Evidokimov AG, Xu K, Clark CM, Maier MB, Srivastava A, Colson AO, Gerwe GS, Stake GE, Howard BW, Pokross ME, Gray JL, Peters KG
Bioorg Med Chem Lett 16 4252-6 (2006)
PMID: 16759857

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

Assemblies composition:
monomeric (preferred)
homo dimer
Assembly name:
PDBe Complex ID:
PDB-CPX-149972 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Receptor-type tyrosine-protein phosphatase beta Chain: A
Molecule details ›
Chain: A
Length: 291 amino acids
Theoretical weight: 33.78 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P23467 (Residues: 1676-1970; Coverage: 15%)
Gene names: PTPB, PTPRB
Sequence domains: Protein-tyrosine phosphatase
Structure domains: Protein tyrosine phosphatase superfamily

Ligands and Environments

3 bound ligands:
Ligand CL 2 x CL
Ligand MG 2 x MG
Ligand 3UN 1 x 3UN
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 22-ID
Spacegroup: C2
Unit cell:
a: 112.316Å b: 38.934Å c: 66.062Å
α: 90° β: 103.91° γ: 90°
R-values:
R R work R free
0.182 0.18 0.217
Expression system: Escherichia coli

Quick links

Citations

2 review citations

Small molecule tools for functional interrogation of protein tyrosine phosphatases.
He et al. (2013)
1 more

3 mentions without citation

A bioinformatic and mechanistic study elicits the antifibrotic effect of ursolic acid through the attenuation of oxidative stress with the involvement of ERK, PI3K/Akt, and p38 MAPK signaling pathways in human hepatic stellate cells and rat liver.
He et al. (2015)
2 more