Function and Biology Details
Reaction catalysed:
L-asparagine + H(2)O = L-aspartate + NH(3)
Biochemical function:
- not assigned
Biological process:
- not assigned
Cellular component:
- not assigned
Sequence domains:
Structure analysis Details
Assembly composition:
hetero dimer (preferred)
Assembly name:
L-asparaginase (preferred)
PDBe Complex ID:
PDB-CPX-186319 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
L-asparaginase
Molecule details ›
Chain: A
Length: 204 amino acids
Theoretical weight: 22.27 KDa
Source organism: Pyrococcus furiosus DSM 3638
Expression system: Escherichia coli
UniProt:
Sequence domains: Asparaginase, N-terminal
Structure domains: L-asparaginase, N-terminal domain
Length: 204 amino acids
Theoretical weight: 22.27 KDa
Source organism: Pyrococcus furiosus DSM 3638
Expression system: Escherichia coli
UniProt:
- Canonical:
Q8TZE8 (Residues: 1-182; Coverage: 56%)
Sequence domains: Asparaginase, N-terminal
Structure domains: L-asparaginase, N-terminal domain
L-asparaginase
Molecule details ›
Chain: B
Length: 147 amino acids
Theoretical weight: 16.08 KDa
Source organism: Pyrococcus furiosus DSM 3638
Expression system: Escherichia coli
UniProt:
Sequence domains: Glutaminase/Asparaginase C-terminal domain
Structure domains: Rossmann fold
Length: 147 amino acids
Theoretical weight: 16.08 KDa
Source organism: Pyrococcus furiosus DSM 3638
Expression system: Escherichia coli
UniProt:
- Canonical: Q8TZE8 (Residues: 202-326; Coverage: 38%)
Sequence domains: Glutaminase/Asparaginase C-terminal domain
Structure domains: Rossmann fold
