X-ray diffraction
3.2Å resolution

Crystal structure of an Rb C-terminal peptide bound to the catalytic subunit of PP1


Function and Biology Details

Structure analysis Details

Assemblies composition:
Non-polymer only trimer
Non-polymer only dimer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Serine/threonine-protein phosphatase PP1-alpha catalytic subunit Chains: A, B
Molecule details ›
Chains: A, B
Length: 300 amino acids
Theoretical weight: 34.37 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
  • Canonical: P62136 (Residues: 1-300; Coverage: 91%)
Gene names: PPP1A, PPP1CA
Sequence domains:
Structure domains: Purple Acid Phosphatase; chain A, domain 2
Retinoblastoma-associated protein Chain: C
Molecule details ›
Chain: C
Length: 13 amino acids
Theoretical weight: 1.53 KDa
Source organism: Homo sapiens
Expression system: Not provided
  • Canonical: P06400 (Residues: 870-882; Coverage: 1%)
Gene name: RB1

Ligands and Environments

2 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 5.0.1
Spacegroup: P41212
Unit cell:
a: 92.946Å b: 92.946Å c: 192.381Å
α: 90° β: 90° γ: 90°
R R work R free
0.225 0.221 0.261
Expression systems:
  • Escherichia coli BL21(DE3)
  • Not provided