PDBe 1zcl

X-ray diffraction
2.9Å resolution

prl-1 c104s mutant in complex with sulfate

Released:

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
Macromolecule:
Protein tyrosine phosphatase type IVA 1 Chains: A, B
Molecule details ›
Chains: A, B
Length: 180 amino acids
Theoretical weight: 20.53 KDa
Source organism: Rattus norvegicus
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: Q78EG7 (Residues: 1-160; Coverage: 93%)
Gene names: Prl1, Ptp4a1
Sequence domains: Dual specificity phosphatase, catalytic domain
Structure domains: Protein tyrosine phosphatase superfamily

Ligands and Environments

1 bound ligand:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: CHESS BEAMLINE F2
Spacegroup: I213
Unit cell:
a: 146.681Å b: 146.681Å c: 146.681Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.261 0.261 0.296
Expression system: Escherichia coli BL21