PDBe 3s3e

X-ray diffraction
2.4Å resolution

Crystal structure of the catalytic domain of PTP10D from Drosophila melanogaster

Released:
Source organism: Drosophila melanogaster
Primary publication:
Conformational basis for substrate recruitment in protein tyrosine phosphatase 10D.
Biochemistry 50 10114-25 (2011)
PMID: 22007620

Function and Biology Details

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Tyrosine-protein phosphatase 10D Chains: A, B
Molecule details ›
Chains: A, B
Length: 307 amino acids
Theoretical weight: 35.95 KDa
Source organism: Drosophila melanogaster
Expression system: Escherichia coli
UniProt:
  • Canonical: P35992 (Residues: 1250-1533; Coverage: 15%)
Gene names: CG1817, Ptp10D
Sequence domains: Protein-tyrosine phosphatase
Structure domains: Protein tyrosine phosphatase superfamily

Ligands and Environments

3 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE BM14
Spacegroup: P3121
Unit cell:
a: 102.46Å b: 102.46Å c: 171.842Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.206 0.205 0.227
Expression system: Escherichia coli