Function and Biology Details
Reaction catalysed:
Exolytic cleavage of the (1->4)-beta-glycosidic linkage between N-acetylmuramic acid (MurNAc) and N-acetylglucosamine (GlcNAc) residues in peptidoglycan, from either the reducing or the non-reducing ends of the peptidoglycan chains, with concomitant formation of a 1,6-anhydrobond in the MurNAc residue.
Biochemical function:
- not assigned
Biological process:
- not assigned
Cellular component:
- not assigned
Sequence domains:
Structure domain:
Structure analysis Details
Assembly composition:
monomeric (preferred)
Assembly name:
Membrane-bound lytic murein transglycosylase D (preferred)
PDBe Complex ID:
PDB-CPX-142681 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Membrane-bound lytic murein transglycosylase D
Molecule details ›
Chain: A
Length: 48 amino acids
Theoretical weight: 5.44 KDa
Source organism: Escherichia coli
Expression system: Not provided
UniProt:
Sequence domains: LysM domain
Structure domains: LysM domain
Length: 48 amino acids
Theoretical weight: 5.44 KDa
Source organism: Escherichia coli
Expression system: Not provided
UniProt:
- Canonical:
P0AEZ7 (Residues: 398-445; Coverage: 11%)
Sequence domains: LysM domain
Structure domains: LysM domain
Ligands and Environments
No bound ligands
No modified residues
Experiments and Validation Details
Refinement method:
SA
Expression system: Not provided
