X-ray diffraction
2.55Å resolution

Crystal structure of full-length human papillomavirus oncoprotein E6 in complex with LXXLL peptide of ubiquitin ligase E6AP at 2.55 A resolution


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:
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (3 distinct):
Maltose/maltodextrin-binding periplasmic protein; Ubiquitin-protein ligase E3A Chains: A, B
Molecule details ›
Chains: A, B
Length: 382 amino acids
Theoretical weight: 41.67 KDa
Source organisms: Expression system: Escherichia coli
  • Canonical: P0AEX9 (Residues: 27-392; Coverage: 99%)
  • Canonical: Q05086 (Residues: 400-417; Coverage: 2%)
Gene names: E6AP, EPVE6AP, HPVE6A, JW3994, UBE3A, b4034, malE
Sequence domains: Bacterial extracellular solute-binding protein
Structure domains: Periplasmic binding protein-like II
Protein E6 Chains: C, D
Molecule details ›
Chains: C, D
Length: 142 amino acids
Theoretical weight: 17.14 KDa
Source organism: Human papillomavirus type 16
Expression system: Escherichia coli
  • Canonical: P03126 (Residues: 9-150; Coverage: 90%)
Gene name: E6
Sequence domains: Early Protein (E6)
Structure domains: E6 early regulatory protein

Ligands and Environments

Carbohydrate polymer : NEW Components: GLC
1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-4
Spacegroup: P212121
Unit cell:
a: 106.279Å b: 134.936Å c: 138.794Å
α: 90° β: 90° γ: 90°
R R work R free
0.168 0.166 0.196
Expression system: Escherichia coli