1o9k

X-ray diffraction
2.6Å resolution

Crystal structure of the retinoblastoma tumour suppressor protein bound to E2F peptide

Released:

Function and Biology Details

Structure analysis Details

Assembly composition:
hetero trimer (preferred)
PDBe Complex ID:
PDB-CPX-139026 (preferred)
Entry contents:
3 distinct polypeptide molecules
Macromolecules (3 distinct):
Retinoblastoma-associated protein Chains: A, C, E, G
Molecule details ›
Chains: A, C, E, G
Length: 218 amino acids
Theoretical weight: 25.1 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P06400 (Residues: 372-589; Coverage: 24%)
Gene name: RB1
Sequence domains: Retinoblastoma-associated protein A domain
Structure domains: Cyclin-like
Retinoblastoma-associated protein Chains: B, D, F, H
Molecule details ›
Chains: B, D, F, H
Length: 152 amino acids
Theoretical weight: 18.27 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P06400 (Residues: 636-787; Coverage: 16%)
Gene name: RB1
Sequence domains: Retinoblastoma-associated protein B domain
Structure domains: Cyclin-like
Transcription factor E2F1 Chains: P, Q, R, S
Molecule details ›
Chains: P, Q, R, S
Length: 18 amino acids
Theoretical weight: 2.13 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: Q01094 (Residues: 409-426; Coverage: 4%)
Gene names: E2F1, RBBP3

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID13
Spacegroup: C2
Unit cell:
a: 101.996Å b: 158.548Å c: 110.617Å
α: 90° β: 93.7° γ: 90°
R-values:
R R work R free
0.232 0.229 0.285
Expression systems:
  • Escherichia coli
  • Not provided