8r1g

Electron Microscopy
3.99Å resolution

Dimeric ternary structure of E6AP-E6-p53

Released:

Function and Biology Details

Reaction catalysed:
(1a) S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [HECT-type E3 ubiquitin transferase]-L-cysteine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + S-ubiquitinyl-[HECT-type E3 ubiquitin transferase]-L-cysteine
Biochemical function:
Cellular component:

Structure analysis Details

Assembly composition:
hetero hexamer (preferred)
PDBe Complex ID:
PDB-CPX-236263 (preferred)
Entry contents:
3 distinct polypeptide molecules
Macromolecules (3 distinct):
Ubiquitin-protein ligase E3A Chains: A, D
Molecule details ›
Chains: A, D
Length: 899 amino acids
Theoretical weight: 103.6 KDa
Source organism: Homo sapiens
Expression system: Trichoplusia ni
UniProt:
  • Canonical: Q05086 (Residues: 1-875; Coverage: 100%)
Gene names: E6AP, EPVE6AP, HPVE6A, UBE3A
Sequence domains:
Protein E6; Ubiquitin-like protein SMT3 Chains: B, E
Molecule details ›
Chains: B, E
Length: 266 amino acids
Theoretical weight: 31.54 KDa
Source organisms: Expression system: Trichoplusia ni
UniProt:
  • Canonical: Q12306 (Residues: 1-98; Coverage: 97%)
  • Canonical: P03126 (Residues: 1-158; Coverage: 100%)
Gene names: D9719.15, E6, SMT3, YDR510W
Sequence domains:
Cellular tumor antigen p53 Chains: C, F
Molecule details ›
Chains: C, F
Length: 417 amino acids
Theoretical weight: 46.5 KDa
Source organism: Homo sapiens
Expression system: Trichoplusia ni
UniProt:
  • Canonical: P04637 (Residues: 1-393; Coverage: 100%)
Gene names: P53, TP53
Sequence domains:

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
Resolution: 3.99Å
Relevant EMDB volumes: EMD-18810
Expression system: Trichoplusia ni