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X-ray diffraction
2.2Å resolution

CRYSTAL STRUCTURE OF PEPTIDE-N(4)-(N-ACETYL-BETA-D-GLUCOSAMINYL) ASPARAGINE AMIDASE AT 2.2 ANGSTROMS RESOLUTION

Released:

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)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Peptide-N(4)-(N-acetyl-beta-D-glucosaminyl)asparagine amidase F Chain: A
Molecule details ›
Chain: A
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%)
Gene names: ngl, png
Sequence domains:
Structure domains: Jelly Rolls

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: C2221
Unit cell:
a: 87.16Å b: 125.1Å c: 79.33Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.183 0.183 not available
Expression system: Not provided