PDBe 2ixp

X-ray diffraction
2.8Å resolution

CRYSTAL STRUCTURE OF THE PP2A PHOSPHATASE ACTIVATOR Ypa1 PTPA1 in complex with model substrate

Released:

Function and Biology Details

Reaction catalysed:
Peptidylproline (omega=180) = peptidylproline (omega=0). 
Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
hetero tetramer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
SIN-ALA-ALA-PRO-LYS-NIT Chains: F, G, H, I
Molecule details ›
Chains: F, G, H, I
Length: 6 amino acids
Theoretical weight: 607 Da
Source organism: synthetic construct
Expression system: Not provided
Serine/threonine-protein phosphatase 2A activator 1 Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 323 amino acids
Theoretical weight: 37.46 KDa
Source organism: Saccharomyces cerevisiae
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P40454 (Residues: 1-317; Coverage: 81%)
Gene names: NCS1, RRD1, YIL153W, YPA1
Sequence domains: Phosphotyrosyl phosphate activator (PTPA) protein

Ligands and Environments

2 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-3
Spacegroup: P65
Unit cell:
a: 86.886Å b: 86.886Å c: 410.626Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.233 0.229 0.302
Expression systems:
  • Not provided
  • Escherichia coli BL21(DE3)