Function and Biology Details
Reaction catalysed:
Cleavage of a beta-linked Asp residue from the N-terminus of a polypeptide.
Biochemical function:
Biological process:
- not assigned
Cellular component:
- not assigned
Sequence domains:
Structure domain:
Structure analysis Details
Assembly composition:
hetero tetramer (preferred)
Assembly name:
Isoaspartyl peptidase subunit beta (preferred)
PDBe Complex ID:
PDB-CPX-153446 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Isoaspartyl peptidase subunit alpha
Molecule details ›
Chains: A, C
Length: 177 amino acids
Theoretical weight: 18.96 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
Sequence domains: Asparaginase
Length: 177 amino acids
Theoretical weight: 18.96 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
- Canonical:
P37595 (Residues: 2-178; Coverage: 55%)
Sequence domains: Asparaginase
Isoaspartyl peptidase subunit beta
Molecule details ›
Chains: B, D
Length: 143 amino acids
Theoretical weight: 14.43 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
Sequence domains: Asparaginase
Structure domains: (Glycosyl)asparaginase
Length: 143 amino acids
Theoretical weight: 14.43 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
- Canonical: P37595 (Residues: 179-321; Coverage: 45%)
Sequence domains: Asparaginase
Structure domains: (Glycosyl)asparaginase
