› 4bpc

X-ray diffraction
2.1Å resolution

Structure of the Catalytic Domain of Protein Tyrosine Phosphatase Sigma in the Sulfenic Acid Form

Released:
DOI: 10.2210/pdb4bpc/pdb
PDB entry 4bpc coloured by chain, front view.
PDB entry 4bpc coloured by chain, side view.
PDB entry 4bpc coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structure of the catalytic domain of protein tyrosine phosphatase sigma in the sulfenic acid form.
Jeon TJ, Chien PN, Chun HJ, Ryu SE
Mol Cells 36 55-61 (2013)
PMID: 23820885

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-171644 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Receptor-type tyrosine-protein phosphatase S Chain: A
Molecule details ›
Chain: A
Length: 582 amino acids
Theoretical weight: 66.93 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q13332 (Residues: 1367-1948; Coverage: 30%)
Gene name: PTPRS
Sequence domains: Protein-tyrosine phosphatase
Structure domains: Protein tyrosine phosphatase superfamily

Ligands and Environments

No bound ligands
1 modified residue:
Ligand CSO 1 x CSO

Experiments and Validation Details

Entry percentile scores
X-ray source: PAL/PLS BEAMLINE 7A (6B, 6C1)
Spacegroup: P61
Unit cell:
a: 94.672Å b: 94.672Å c: 123.423Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.18 0.178 0.222
Expression system: Escherichia coli

Quick links

Citations

2 review citations

Biological chemistry and functionality of protein sulfenic acids and related thiol modifications.
Devarie-Baez et al. (2016)
1 more

2 mentions without citation

RPTPĪ± phosphatase activity is allosterically regulated by the membrane-distal catalytic domain.
Wen et al. (2020)
1 more