Function and Biology Details
Reaction catalysed:
Hydrolysis of an N(4)-(acetyl-beta-D-glucosaminyl)asparagine residue in which the glucosamine residue may be further glycosylated, to yield a (substituted) N-acetyl-beta-D-glucosaminylamine and a peptide containing an aspartate residue
Biochemical function:
Biological process:
- not assigned
Cellular component:
- not assigned
Structure analysis Details
Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-149116 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Peptide-N(4)-(N-acetyl-beta-D-glucosaminyl)asparagine amidase F
Molecule details ›
Chain: A
Length: 314 amino acids
Theoretical weight: 34.82 KDa
Source organism: Elizabethkingia meningoseptica
Expression system: Not provided
UniProt:
Sequence domains: Peptide-N-glycosidase F, C terminal
Structure domains: Jelly Rolls
Length: 314 amino acids
Theoretical weight: 34.82 KDa
Source organism: Elizabethkingia meningoseptica
Expression system: Not provided
UniProt:
- Canonical:
P21163 (Residues: 41-354; Coverage: 100%)
Sequence domains: Peptide-N-glycosidase F, C terminal
Structure domains: Jelly Rolls
Ligands and Environments
No bound ligands
No modified residues
Experiments and Validation Details
Spacegroup:
C2221
Expression system: Not provided
