3s4o

X-ray diffraction
2.3Å resolution

Protein Tyrosine Phosphatase (putative) from Leishmania major

Released:
Source organism: Leishmania major
Entry authors: Merritt EA, Arakaki T, Medical Structural Genomics of Pathogenic Protozoa (MSGPP), Structural Genomics of Pathogenic Protozoa Consortium (SGPP)

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
PDBe Complex ID:
PDB-CPX-175706 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Protein tyrosine phosphatase PRL-1 Chains: A, B
Molecule details ›
Chains: A, B
Length: 167 amino acids
Theoretical weight: 18.51 KDa
Source organism: Leishmania major
Expression system: Escherichia coli
UniProt:
  • Canonical: Q4QEZ7 (Residues: 4-165; Coverage: 93%)
Gene names: LMJF_16_0230, PRL-1
Sequence domains: Protein-tyrosine phosphatase
Structure domains: Protein tyrosine phosphatase superfamily

Ligands and Environments

2 bound ligands:
1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 8.2.2
Spacegroup: P212121
Unit cell:
a: 42.518Å b: 69.42Å c: 118.931Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.209 0.206 0.248
Expression system: Escherichia coli