› 1r6h

Solution NMR

Solution Structure of human PRL-3

Released:
DOI: 10.2210/pdb1r6h/pdb
PDB entry 1r6h coloured by chain, ensemble of 20 models, front view.
PDB entry 1r6h coloured by chain, ensemble of 20 models, side view.
PDB entry 1r6h coloured by chain, ensemble of 20 models, top view.
Source organism: Homo sapiens
Primary publication:
Structural insights into molecular function of the metastasis-associated phosphatase PRL-3.
Kozlov G, Cheng J, Ziomek E, Banville D, Gehring K, Ekiel I
J Biol Chem 279 11882-9 (2004)
PMID: 14704153

Function and Biology Details

Reaction catalysed: 
Protein tyrosine phosphate + H(2)O = protein tyrosine + phosphate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-130912 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Protein tyrosine phosphatase type IVA 3 Chain: A
Molecule details ›
Chain: A
Length: 172 amino acids
Theoretical weight: 19.41 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: O75365 (Residues: 1-169; Coverage: 98%)
Gene names: PRL3, PTP4A3
Sequence domains: Protein-tyrosine phosphatase
Structure domains: Protein tyrosine phosphatase superfamily

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

16 review citations

PRL PTPs: mediators and markers of cancer progression.
Bessette et al. (2008)
15 more

3 mentions without citation

Targeting phosphatases of regenerating liver (PRLs) in cancer.
Wei et al. (2018)
2 more