Function and Biology Details
Reaction catalysed:
Release of an N-terminal D-amino acid from a peptide, Xaa-|-Yaa-, in which Xaa is preferably D-Ala, D-Ser or D-Thr. D-amino acid amides and methyl esters also are hydrolyzed, as is glycine amide.
Biochemical function:
Biological process:
- not assigned
Cellular component:
- not assigned
Sequence domains:
Structure domain:
Structure analysis Details
Assembly composition:
homo tetramer (preferred)
Assembly name:
D-aminopeptidase (preferred)
PDBe Complex ID:
PDB-CPX-176809 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
D-aminopeptidase
Molecule details ›
Chains: A, B, C, D, E, F
Length: 375 amino acids
Theoretical weight: 40.46 KDa
Source organism: Brucella anthropi
Expression system: Escherichia coli
UniProt:
Sequence domains: Peptidase family S58
Structure domains: L-amino peptidase D-ALA esterase/amidase
Length: 375 amino acids
Theoretical weight: 40.46 KDa
Source organism: Brucella anthropi
Expression system: Escherichia coli
UniProt:
- Canonical:
Q59632 (Residues: 1-375; Coverage: 100%)
Sequence domains: Peptidase family S58
Structure domains: L-amino peptidase D-ALA esterase/amidase
Ligands and Environments
No bound ligands
No modified residues
Experiments and Validation Details
X-ray source:
LURE BEAMLINE DW32
Spacegroup:
P21212
Expression system: Escherichia coli
