3s3h

X-ray diffraction
2.8Å resolution

Crystal structure of the catalytic domain of PTP10D from Drosophila melanogaster with a phosphopeptide substrate GP4

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

Assemblies composition:
monomeric (preferred)
hetero dimer
PDBe Complex ID:
PDB-CPX-153096 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
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
phosphopeptide GP4 Chain: C
Molecule details ›
Chain: C
Length: 11 amino acids
Theoretical weight: 1.42 KDa
Source organism: Drosophila melanogaster
Expression system: Not provided

Ligands and Environments

2 bound ligands:
1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE BM14
Spacegroup: P3121
Unit cell:
a: 102.7Å b: 102.7Å c: 173.22Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.252 0.25 0.289
Expression systems:
  • Escherichia coli
  • Not provided