Function and Biology Details
Reaction catalysed:
L-asparagine + H(2)O = L-aspartate + NH(3)
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
- Asparaginase/glutaminase-like
- Asparaginase/glutaminase, C-terminal
- L-asparaginase, C-terminal
- Asparaginase/glutaminase, active site 2
- Asparaginase/glutaminase, active site 1
- L-asparaginase, N-terminal
- L-asparaginase, N-terminal domain superfamily
- Asparaginase/glutaminase-like superfamily
1 more domain
Structure domain:
Structure analysis Details
Assembly composition:
homo tetramer (preferred)
Assembly name:
Glutaminase-asparaginase (preferred)
PDBe Complex ID:
PDB-CPX-145197 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Glutaminase-asparaginase
Molecule details ›
Chains: 1, 2, 3, 4
Length: 337 amino acids
Theoretical weight: 35.98 KDa
Source organism: Pseudomonas sp. 7A
Expression system: Not provided
UniProt:
Sequence domains:
Structure domains:
Length: 337 amino acids
Theoretical weight: 35.98 KDa
Source organism: Pseudomonas sp. 7A
Expression system: Not provided
UniProt:
- Canonical:
P10182 (Residues: 8-337; Coverage: 98%)
Sequence domains:
Structure domains:
Ligands and Environments
No bound ligands
No modified residues
Experiments and Validation Details
Spacegroup:
P212121
Expression system: Not provided
