4mbb

X-ray diffraction
1.85Å resolution

Cubic crystal form of PIR1 dual specificity phosphatase core

Released:
Source organism: Homo sapiens
Primary publication:
Structure of human PIR1, an atypical dual-specificity phosphatase.
Biochemistry 53 862-71 (2014)
PMID: 24447265

Function and Biology Details

Structure analysis Details

Assemblies composition:
monomeric (preferred)
homo trimer
PDBe Complex ID:
PDB-CPX-130893 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
RNA/RNP complex-1-interacting phosphatase Chain: A
Molecule details ›
Chain: A
Length: 184 amino acids
Theoretical weight: 21.48 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: O75319 (Residues: 29-207; Coverage: 54%)
Gene names: DUSP11, PIR1
Sequence domains: Dual specificity phosphatase, catalytic domain
Structure domains: Protein tyrosine phosphatase superfamily

Ligands and Environments

2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X6A
Spacegroup: P213
Unit cell:
a: 92.74Å b: 92.74Å c: 92.74Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.169 0.168 0.188
Expression system: Escherichia coli BL21(DE3)