› 3s3f

X-ray diffraction
2.7Å resolution

Crystal Structure of the catalytic domain of PTP10D from Drosophila melanogaster with a small molecule inhibitor Vanadate

Released:
DOI: 10.2210/pdb3s3f/pdb
PDB entry 3s3f coloured by chain, front view.
PDB entry 3s3f coloured by chain, side view.
PDB entry 3s3f coloured by chain, top view.
Source organism: Drosophila melanogaster
Primary publication:
Conformational basis for substrate recruitment in protein tyrosine phosphatase 10D.
Madan LL, Gopal B
Biochemistry 50 10114-25 (2011)
PMID: 22007620

Function and Biology Details

Reaction catalysed: 
Protein tyrosine phosphate + H(2)O = protein tyrosine + phosphate
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-153096 (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

4 bound ligands:
Ligand 1BO 2 x 1BO
Ligand IPA 2 x IPA
Ligand VO4 1 x VO4
Ligand BU1 1 x BU1
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE BM14
Spacegroup: P3121
Unit cell:
a: 103.07Å b: 103.07Å c: 173.401Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.24 0.238 0.272
Expression system: Escherichia coli

Quick links

Citations

2 review citations

Protein Tyrosine Phosphatases: A new paradigm in an old signaling system?
Welsh et al. (2021)
1 more

2 mentions without citation

Conformational basis for substrate recruitment in protein tyrosine phosphatase 10D.
Madan et al. (2011)
1 more