PDBe 1c4z

X-ray diffraction
2.6Å resolution

STRUCTURE OF E6AP: INSIGHTS INTO UBIQUITINATION PATHWAY

Released:

Function and Biology Details

Reactions catalysed:
S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)- ubiquitinyl-[acceptor protein]-L-lysine. 
S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + [E2 ubiquitin-conjugating enzyme]-L-cysteine = [E1 ubiquitin-activating enzyme]-L-cysteine + S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L- cysteine. 
Cellular component:

Structure analysis Details

Assembly composition:
hetero tetramer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
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:
Ubiquitin-conjugating enzyme E2 L3 Chain: D
Molecule details ›
Chain: D
Length: 154 amino acids
Theoretical weight: 17.89 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P68036 (Residues: 1-154; Coverage: 100%)
Gene names: UBCE7, UBCH7, UBE2L3
Sequence domains: Ubiquitin-conjugating enzyme
Structure domains: Ubiquitin Conjugating Enzyme

Ligands and Environments

No bound ligands

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 5.0.2
Spacegroup: P212121
Unit cell:
a: 103.4Å b: 112.7Å c: 123.8Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.262 0.237 0.29
Expression system: Escherichia coli