› 4yaa

X-ray diffraction
1.05Å resolution

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-147287 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Tyrosine-protein phosphatase YopH Chain: A
Molecule details ›
Chain: A
Length: 306 amino acids
Theoretical weight: 33.53 KDa
Source organism: Yersinia enterocolitica
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: P15273 (Residues: 164-468; Coverage: 65%)
Gene names: yop51, yopH
Sequence domains: Protein-tyrosine phosphatase
Structure domains: Protein tyrosine phosphatase superfamily

Ligands and Environments

2 bound ligands:
Ligand ACT 1 x ACT
Ligand SO4 1 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL9-3
Spacegroup: P212121
Unit cell:
a: 52.888Å b: 60.512Å c: 89.358Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.129 0.128 0.14
Expression system: Escherichia coli BL21

Quick links

Citations

2 review citations

The metal face of protein tyrosine phosphatase 1B.
Bellomo et al. (2016)
1 more

2 mentions without citation

Conservative tryptophan mutants of the protein tyrosine phosphatase YopH exhibit impaired WPD-loop function and crystallize with divanadate esters in their active sites.
Moise et al. (2015)
1 more