› 1p4v

X-ray diffraction
1.9Å resolution

CRYSTAL STRUCTURE OF THE GLYCOSYLASPARAGINASE PRECURSOR D151N MUTANT WITH GLYCINE

Released:
DOI: 10.2210/pdb1p4v/pdb
PDB entry 1p4v coloured by chain, front view.
PDB entry 1p4v coloured by chain, side view.
PDB entry 1p4v coloured by chain, top view.
Source organism: Elizabethkingia meningoseptica
Primary publication:
A dual role for an aspartic acid in glycosylasparaginase autoproteolysis.
Qian X, Guan C, Guo HC
Structure 11 997-1003 (2003)
PMID: 12906830

Function and Biology Details

Reaction catalysed: 
N(4)-(beta-N-acetyl-D-glucosaminyl)-L-asparagine + H(2)O = N-acetyl-beta-D-glucosaminylamine + L-aspartate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-559586 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
N(4)-(Beta-N-acetylglucosaminyl)-L-asparaginase Chains: A, C
Molecule details ›
Chains: A, C
Length: 295 amino acids
Theoretical weight: 32.18 KDa
Source organism: Elizabethkingia meningoseptica
Expression system: Escherichia coli
UniProt:
  • Canonical: Q47898 (Residues: 46-340; Coverage: 100%)
Sequence domains: Asparaginase

Ligands and Environments

1 bound ligand:
Ligand GLY 2 x GLY
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X12C
Spacegroup: P1
Unit cell:
a: 45.877Å b: 52.369Å c: 61.741Å
α: 80.92° β: 90.41° γ: 105.1°
R-values:
R R work R free
0.193 0.193 0.225
Expression system: Escherichia coli

Quick links

Citations

19 citation in other articles

CARD8 and NLRP1 undergo autoproteolytic processing through a ZU5-like domain.
D'Osualdo et al. (2011)
18 more

1 mention without citation

Biochemical characterization and comparison of aspartylglucosaminidases secreted in venom of the parasitoid wasps Asobara tabida and Leptopilina heterotoma.
Coulette et al. (2017)