Structure analysis

STRUCTURE OF AN E6AP-UBCH7 COMPLEX: INSIGHTS INTO THE UBIQUITINATION PATHWAY

X-ray diffraction
2.6Å resolution
Source organism: Homo sapiens
Assembly composition:
hetero tetramer (preferred)
Entry contents: 2 distinct polypeptide molecules

Assemblies

Assembly 1 (preferred)
Download    3D Visualisation
Multimeric state: hetero tetramer
Accessible surface area: 56493.7 Å2
Buried surface area: 8487.92 Å2
Dissociation area: 4,243.96 Å2
Dissociation energy (ΔGdiss): -3.37 kcal/mol
Dissociation entropy (TΔSdiss): 41.6 kcal/mol
Symmetry number: 1
PDBe Complex ID: PDB-CPX-159272

Macromolecules

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
Pfam: HECT-domain (ubiquitin-transferase)
InterPro:
CATH:
SCOP: Hect, E3 ligase catalytic domain
PDBe-KB: UniProt Coverage View: Q05086  
135850100150200250300350
 
100200300
UniProt
Q05086
Chains
Domains
Secondary structure
Flexibility predictions
Early folding residue predictions
Interaction interfaces
Sequence conservation
Variants

Search similar proteins

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
Pfam: Ubiquitin-conjugating enzyme
InterPro:
CATH: Ubiquitin Conjugating Enzyme
SCOP: UBC-related
PDBe-KB: UniProt Coverage View: P68036  
115420406080100120140
 
50100150
UniProt
P68036
Chains
Domains
Secondary structure
Flexibility predictions
Early folding residue predictions
Interaction interfaces
Sequence conservation
Variants

Search similar proteins