› 2h04

X-ray diffraction
2.3Å resolution

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

Released:
DOI: 10.2210/pdb2h04/pdb
PDB entry 2h04 coloured by chain, front view.
PDB entry 2h04 coloured by chain, side view.
PDB entry 2h04 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

Assembly composition:
monomeric (preferred)
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: 313 amino acids
Theoretical weight: 36.29 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P23467 (Residues: 1662-1973; Coverage: 16%)
Gene names: PTPB, PTPRB
Sequence domains: Protein-tyrosine phosphatase
Structure domains: Protein tyrosine phosphatase superfamily

Ligands and Environments

1 bound ligand:
Ligand 4UN 1 x 4UN
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 17-ID
Spacegroup: P212121
Unit cell:
a: 44.803Å b: 70.12Å c: 90.722Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.172 0.169 0.238
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

6 mentions without citation

Potent Molecular Feature-based Neutralizing Monoclonal Antibodies as Promising Therapeutics Against SARS-CoV-2 Infection.
Kombe Kombe et al. (2021)
5 more