Function and Biology Details
Reaction catalysed:
Cleavage of peptide bonds with very broad specificity.
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
- Peptidase T1A, proteasome beta-subunit
- Nucleophile aminohydrolases, N-terminal
- Peptidase T1A, proteasome beta-subunit, archaeal
- Proteasome alpha subunit, archaeal
- Proteasome B-type subunit
- Proteasome, subunit alpha/beta
- Proteasome beta-type subunit, conserved site
- Proteasome alpha-type subunit
1 more domain
Structure analysis Details
Assembly composition:
hetero 28-mer (preferred)
Assembly name:
Proteasome core complex (preferred)
PDBe Complex ID:
PDB-CPX-150391 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Proteasome subunit alpha
Molecule details ›
Chains: 0, A, C, E, G, I, K, M, O, Q, S, U, W, Y
Length: 233 amino acids
Theoretical weight: 25.83 KDa
Source organism: Thermoplasma acidophilum
Expression system: Escherichia coli
UniProt:
Sequence domains:
Structure domains: Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1
Length: 233 amino acids
Theoretical weight: 25.83 KDa
Source organism: Thermoplasma acidophilum
Expression system: Escherichia coli
UniProt:
- Canonical:
P25156 (Residues: 1-233; Coverage: 100%)
Sequence domains:
Structure domains: Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1
Proteasome subunit beta
Molecule details ›
Chains: 1, B, D, F, H, J, L, N, P, R, T, V, X, Z
Length: 211 amino acids
Theoretical weight: 23.17 KDa
Source organism: Thermoplasma acidophilum
Expression system: Escherichia coli
UniProt:
Sequence domains: Proteasome subunit
Structure domains: Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1
Length: 211 amino acids
Theoretical weight: 23.17 KDa
Source organism: Thermoplasma acidophilum
Expression system: Escherichia coli
UniProt:
- Canonical: P28061 (Residues: 1-211; Coverage: 100%)
Sequence domains: Proteasome subunit
Structure domains: Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1
