› 1xm2

X-ray diffraction
2.7Å resolution

Crystal structure of Human PRL-1

Released:
DOI: 10.2210/pdb1xm2/pdb
PDB entry 1xm2 coloured by chain, front view.
PDB entry 1xm2 coloured by chain, side view.
PDB entry 1xm2 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Trimeric structure of PRL-1 phosphatase reveals an active enzyme conformation and regulation mechanisms.
Jeong DG, Kim SJ, Kim JH, Son JH, Park MR, Lim SM, Yoon TS, Ryu SE
J Mol Biol 345 401-13 (2005)
PMID: 15571731

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo trimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-187986 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Protein tyrosine phosphatase type IVA 1 Chains: A, B, C, D, E, F
Molecule details ›
Chains: A, B, C, D, E, F
Length: 173 amino acids
Theoretical weight: 20.06 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q93096 (Residues: 1-173; Coverage: 100%)
Gene names: PRL1, PTP4A1, PTPCAAX1
Sequence domains: Dual specificity phosphatase, catalytic domain
Structure domains: Protein tyrosine phosphatase superfamily

Ligands and Environments

1 bound ligand:
Ligand SO4 6 x SO4
1 modified residue:
Ligand MSE 30 x MSE

Experiments and Validation Details

Entry percentile scores
X-ray source: PAL/PLS BEAMLINE 6B
Spacegroup: P21
Unit cell:
a: 59.29Å b: 84.76Å c: 122.18Å
α: 90° β: 99.79° γ: 90°
R-values:
R R work R free
0.243 0.237 0.296
Expression system: Escherichia coli

Quick links

Citations

9 review citations

Targeting PTPs with small molecule inhibitors in cancer treatment.
Jiang et al. (2008)
8 more

13 mentions without citation

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