› 3sme

X-ray diffraction
1.7Å resolution

Structure of PTP1B inactivated by H2O2/bicarbonate

Released:
DOI: 10.2210/pdb3sme/pdb
PDB entry 3sme coloured by chain, front view.
PDB entry 3sme coloured by chain, side view.
PDB entry 3sme coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
The biological buffer bicarbonate/CO2 potentiates H2O2-mediated inactivation of protein tyrosine phosphatases.
Zhou H, Singh H, Parsons ZD, Lewis SM, Bhattacharya S, Seiner DR, LaButti JN, Reilly TJ, Tanner JJ, Gates KS
J Am Chem Soc 133 15803-5 (2011)
PMID: 21913686

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: 300 amino acids
Theoretical weight: 34.92 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P18031 (Residues: 1-298; Coverage: 69%)
Gene names: PTP1B, PTPN1
Sequence domains: Protein-tyrosine phosphatase
Structure domains: Protein tyrosine phosphatase superfamily

Ligands and Environments

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

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 4.2.2
Spacegroup: P3121
Unit cell:
a: 88Å b: 88Å c: 104Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.198 0.197 0.21
Expression system: Escherichia coli

Quick links

Citations

11 review citations

The molecular mechanisms and physiological consequences of oxidative stress: lessons from a model bacterium.
Imlay JA. (2013)
10 more

9 mentions without citation

Advanced Bioinformatics Tools in the Pharmacokinetic Profiles of Natural and Synthetic Compounds with Anti-Diabetic Activity.
Udrea et al. (2021)
8 more