8qyn

Electron Microscopy
2.88Å resolution

Human 20S proteasome assembly intermediate structure 5

Released:
Source organism: Homo sapiens
Related structures: EMD-18759

Function and Biology Details

Reaction catalysed:
Cleavage of peptide bonds with very broad specificity.
Biochemical function:
Cellular component:

Structure analysis Details

Assembly composition:
hetero heptadecamer (preferred)
PDBe Complex ID:
PDB-CPX-271556 (preferred)
Entry contents:
17 distinct polypeptide molecules
Macromolecules (17 distinct):
Proteasome subunit alpha type-2 Chain: A
Molecule details ›
Chain: A
Length: 234 amino acids
Theoretical weight: 25.93 KDa
Source organism: Homo sapiens
Expression system: Trichoplusia ni
UniProt:
  • Canonical: P25787 (Residues: 1-234; Coverage: 100%)
Gene names: HC3, PSC3, PSMA2
Sequence domains:
Proteasome subunit alpha type-4 Chain: B
Molecule details ›
Chain: B
Length: 261 amino acids
Theoretical weight: 29.53 KDa
Source organism: Homo sapiens
Expression system: Trichoplusia ni
UniProt:
  • Canonical: P25789 (Residues: 1-261; Coverage: 100%)
Gene names: HC9, PSC9, PSMA4
Sequence domains:
Proteasome subunit alpha type-7 Chain: C
Proteasome subunit alpha type-5 Chain: D
Proteasome subunit alpha type-1 Chain: E
Proteasome subunit alpha type-3 Chain: F
Proteasome subunit alpha type-6 Chain: G
Proteasome maturation protein Chain: H
Proteasome assembly chaperone 1 Chain: I
Proteasome assembly chaperone 2 Chain: J
Proteasome subunit beta type-7 Chain: K
Proteasome subunit beta type-3 Chain: L
Proteasome subunit beta type-2 Chain: M
Proteasome subunit beta type-5 Chain: N
Proteasome subunit beta type-1 Chain: O
Proteasome subunit beta type-4 Chain: P
Proteasome subunit beta type-6 Chain: Q

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Resolution: 2.88Å
Relevant EMDB volumes: EMD-18759
Expression system: Trichoplusia ni