1d5f

X-ray diffraction
2.8Å resolution

STRUCTURE OF E6AP: INSIGHTS INTO UBIQUITINATION PATHWAY

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
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo trimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Ubiquitin-protein ligase E3A Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 358 amino acids
Theoretical weight: 41.54 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q05086 (Residues: 518-875; Coverage: 41%)
Gene names: E6AP, EPVE6AP, HPVE6A, UBE3A
Sequence domains: HECT-domain (ubiquitin-transferase)
Structure domains:

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200, NSLS BEAMLINE X4A
Spacegroup: P212121
Unit cell:
a: 101.5Å b: 113.7Å c: 125.2Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.251 0.23 0.283
Expression system: Escherichia coli