› 4z6b

X-ray diffraction
1.2Å resolution

YopH W354H Yersinia enterocolitica PTPase in the apo form

Released:
DOI: 10.2210/pdb4z6b/pdb
PDB entry 4z6b coloured by chain, front view.
PDB entry 4z6b coloured by chain, side view.
PDB entry 4z6b coloured by chain, top view.
Source organism: Yersinia enterocolitica
Primary publication:
Conservative tryptophan mutants of the protein tyrosine phosphatase YopH exhibit impaired WPD-loop function and crystallize with divanadate esters in their active sites.
Moise G, Gallup NM, Alexandrova AN, Hengge AC, Johnson SJ
Biochemistry 54 6490-500 (2015)
PMID: 26445170

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: 33.51 KDa
Source organism: Yersinia enterocolitica
Expression system: Escherichia coli
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 GOL 1 x GOL
Ligand ACT 1 x ACT
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
0.141 0.14 0.159
Expression system: Escherichia coli

Quick links

Citations

2 review citations

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

1 mention 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)