› 1p8a

Solution NMR

Solution structure of the low molecular weight protein tyrosine phosphatase from Tritrichomonas foetus

Released:
DOI: 10.2210/pdb1p8a/pdb
PDB entry 1p8a coloured by chain, ensemble of 21 models, front view.
PDB entry 1p8a coloured by chain, ensemble of 21 models, side view.
PDB entry 1p8a coloured by chain, ensemble of 21 models, top view.
Source organism: Tritrichomonas suis
Primary publication:
Solution structure of the low-molecular-weight protein tyrosine phosphatase from Tritrichomonas foetus reveals a flexible phosphate binding loop.
Gustafson CL, Stauffacher CV, Hallenga K, Van Etten RL
Protein Sci 14 2515-25 (2005)
PMID: 16195543

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-126394 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Phosphotyrosine protein phosphatase I domain-containing protein Chain: A
Molecule details ›
Chain: A
Length: 146 amino acids
Theoretical weight: 15.84 KDa
Source organism: Tritrichomonas suis
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: O00810 (Residues: 2-147; Coverage: 99%)
Sequence domains: Low molecular weight phosphotyrosine protein phosphatase
Structure domains: Rossmann fold

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Refinement method: simulated annealing
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

6 citation in other articles

Ligand binding reduces conformational flexibility in the active site of tyrosine phosphatase related to biofilm formation A (TpbA) from Pseudomonasaeruginosa.
Koveal et al. (2013)
5 more

2 mentions without citation

The structure of the nucleoside triphosphate diphosphohydrolases (NTPDases) as revealed by mutagenic and computational modeling analyses.
Kirley et al. (2006)
1 more