› 1yts

X-ray diffraction
2.5Å resolution

A LIGAND-INDUCED CONFORMATIONAL CHANGE IN THE YERSINIA PROTEIN TYROSINE PHOSPHATASE

Released:
DOI: 10.2210/pdb1yts/pdb
PDB entry 1yts coloured by chain, front view.
PDB entry 1yts coloured by chain, side view.
PDB entry 1yts coloured by chain, top view.
Source organism: Yersinia enterocolitica
Primary publication:
A ligand-induced conformational change in the Yersinia protein tyrosine phosphatase.
Schubert HL, Fauman EB, Stuckey JA, Dixon JE, Saper MA
Protein Sci 4 1904-13 (1995)
PMID: 8528087

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-147287 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Tyrosine-protein phosphatase YopH Chain: A
Molecule details ›
Chain: A
Length: 278 amino acids
Theoretical weight: 30.63 KDa
Source organism: Yersinia enterocolitica
Expression system: Escherichia coli
UniProt:
  • Canonical: P15273 (Residues: 191-468; Coverage: 59%)
Gene names: yop51, yopH
Sequence domains: Protein-tyrosine phosphatase
Structure domains: Protein tyrosine phosphatase superfamily

Ligands and Environments

1 bound ligand:
Ligand SO4 2 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P212121
Unit cell:
a: 56.4Å b: 49.8Å c: 100.4Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.174 0.174 not available
Expression system: Escherichia coli

Quick links

Citations

17 review citations

Structural and evolutionary relationships among protein tyrosine phosphatase domains.
Andersen et al. (2001)
16 more

5 mentions without citation

Normal-modes-based prediction of protein conformational changes guided by distance constraints.
Zheng et al. (2005)
4 more