PDBe 2kyl

Solution NMR

Solution structure of MAST2-PDZ complexed with the C-terminus of PTEN

Released:
Source organism: Homo sapiens
Entry authors: Terrien E, Wolff N, Cordier F, Simenel C, Lafon M, Delepierre M

Function and Biology Details

Reactions catalysed:
ATP + a protein = ADP + a phosphoprotein
[a protein]-serine/threonine phosphate + H(2)O = [a protein]-serine/threonine + phosphate
Protein tyrosine phosphate + H(2)O = protein tyrosine + phosphate
Phosphatidylinositol 3,4,5-trisphosphate + H(2)O = phosphatidylinositol 4,5-bisphosphate + phosphate
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Microtubule-associated serine/threonine-protein kinase 2 Chain: A
Molecule details ›
Chain: A
Length: 96 amino acids
Theoretical weight: 10.45 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q6P0Q8 (Residues: 1099-1193; Coverage: 5%)
Gene names: KIAA0807, MAST2, MAST205
Sequence domains: PDZ domain
Structure domains: Pdz3 Domain
Phosphatidylinositol 3,4,5-trisphosphate 3-phosphatase and dual-specificity protein phosphatase PTEN Chain: B
Molecule details ›
Chain: B
Length: 13 amino acids
Theoretical weight: 1.56 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: P60484 (Residues: 391-403; Coverage: 3%)
Gene names: MMAC1, PTEN, TEP1

Ligands and Environments

No bound ligands

No modified residues

Experiments and Validation Details

Entry percentile scores
Chemical shift assignment: 86%
Refinement method: torsion angle dynamics
Chemical shifts: BMR16967  
Expression systems:
  • Escherichia coli
  • Not provided