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Electron Microscopy
3.41Å resolution

Cryo-EM structure of human proteasome assembly intermediate preholo-1

Released:
Source organism: Homo sapiens
Related structures: EMD-39333

Function and Biology Details

Reaction catalysed:
Cleavage of peptide bonds with very broad specificity.
Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
hetero 34-mer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-271561 (preferred)
Entry contents:
17 distinct polypeptide molecules
Macromolecules (17 distinct):
Proteasome subunit alpha type-2 Chains: A, O
Molecule details ›
Chains: A, O
Length: 234 amino acids
Theoretical weight: 25.93 KDa
Source organism: Homo sapiens
UniProt:
  • Canonical: P25787 (Residues: 1-234; Coverage: 100%)
Gene names: HC3, PSC3, PSMA2
Sequence domains:
Proteasome subunit alpha type-4 Chains: B, P
Molecule details ›
Chains: B, P
Length: 261 amino acids
Theoretical weight: 29.53 KDa
Source organism: Homo sapiens
UniProt:
  • Canonical: P25789 (Residues: 1-261; Coverage: 100%)
Gene names: HC9, PSC9, PSMA4
Sequence domains:
Proteasome subunit alpha type-7 Chains: C, Q
Proteasome subunit alpha type-5 Chains: D, R
Proteasome subunit alpha type-1 Chains: E, S
Proteasome subunit alpha type-3 Chains: F, T
Proteasome subunit alpha type-6 Chains: G, U
Proteasome subunit beta type-7 Chains: H, V
Proteasome subunit beta type-3 Chains: I, W
Proteasome subunit beta type-2 Chains: J, X
Proteasome subunit beta type-5 Chains: K, Y
Proteasome subunit beta type-1 Chains: L, Z
Proteasome subunit beta type-4 Chains: M, a
Proteasome subunit beta type-6 Chains: N, b
Proteasome assembly chaperone 1 Chains: c, f
Proteasome assembly chaperone 2 Chains: d, g
Proteasome maturation protein Chains: e, h

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Resolution: 3.41Å
Relevant EMDB volumes: EMD-39333