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Electron Microscopy
3.4Å resolution

Cryo-EM structure of a double loaded human UBA7-UBE2L6-ISG15 thioester mimetic complex (Form 1)

Released:

Function and Biology Details

Reaction catalysed:
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
Biochemical function:
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
hetero tetramer (preferred)
PDBe Complex ID:
PDB-CPX-231664 (preferred)
Entry contents:
3 distinct polypeptide molecules
Macromolecules (3 distinct):
Ubiquitin-like modifier-activating enzyme 7 Chain: A
Molecule details ›
Chain: A
Length: 1012 amino acids
Theoretical weight: 111.82 KDa
Source organism: Homo sapiens
Expression system: Trichoplusia ni
UniProt:
  • Canonical: P41226 (Residues: 1-1012; Coverage: 100%)
Gene names: UBA7, UBE1L, UBE2
Sequence domains:
Ubiquitin-like protein ISG15 Chains: B, D
Molecule details ›
Chains: B, D
Length: 157 amino acids
Theoretical weight: 17.15 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P05161 (Residues: 1-157; Coverage: 95%)
Gene names: G1P2, ISG15, UCRP
Sequence domains: Ubiquitin family
Ubiquitin/ISG15-conjugating enzyme E2 L6 Chain: C

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

wwPDB Validation report is not available for this EM entry.
Resolution: 3.4Å
Relevant EMDB volumes: EMD-40408
Expression systems:
  • Trichoplusia ni
  • Escherichia coli