PDBe 1xm2

X-ray diffraction
2.7Å resolution

Crystal structure of Human PRL-1


Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo trimer (preferred)
Entry contents:
1 distinct polypeptide molecule
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
  • 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:

1 modified residue:

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 R work R free
0.243 0.237 0.296
Expression system: Escherichia coli