Function and Biology Details
Reaction catalysed:
Hydrolyzes the link between N-acetylmuramoyl residues and L-amino acid residues in certain cell-wall glycopeptides
Biochemical function:
Biological process:
Cellular component:
Structure analysis Details
Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-160659 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
1,6-anhydro-N-acetylmuramyl-L-alanine amidase AmpD
Molecule details ›
Chains: A, B, C
Length: 187 amino acids
Theoretical weight: 20.87 KDa
Source organism: Citrobacter freundii
Expression system: Escherichia coli
UniProt:
Sequence domains: N-acetylmuramoyl-L-alanine amidase
Structure domains: Peptidoglycan recognition protein-like
Length: 187 amino acids
Theoretical weight: 20.87 KDa
Source organism: Citrobacter freundii
Expression system: Escherichia coli
UniProt:
- Canonical:
P82974 (Residues: 1-187; Coverage: 100%)
Sequence domains: N-acetylmuramoyl-L-alanine amidase
Structure domains: Peptidoglycan recognition protein-like
Ligands and Environments
No bound ligands
No modified residues
Experiments and Validation Details
X-ray source:
ESRF BEAMLINE ID29
Spacegroup:
P32
Expression system: Escherichia coli
