› 9gaf

X-ray diffraction
1.9Å resolution

PRECURSOR OF THE W11F MUTANT GLYCOSYLASPARAGINASE FROM FLAVOBACTERIUM MENINGOSEPTICUM

Released:
DOI: 10.2210/pdb9gaf/pdb
PDB entry 9gaf coloured by chain, front view.
PDB entry 9gaf coloured by chain, side view.
PDB entry 9gaf coloured by chain, top view.
Source organism: Elizabethkingia meningoseptica
Primary publication:
Structural insights into the mechanism of intramolecular proteolysis.
Xu Q, Buckley D, Guan C, Guo HC
Cell 98 651-61 (1999)
PMID: 10490104

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-175277 (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: 32.14 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 X4A
Spacegroup: P1
Unit cell:
a: 46.3Å b: 52.8Å c: 62.4Å
α: 80.8° β: 90.5° γ: 105.1°
R-values:
R R work R free
0.196 0.196 0.239
Expression system: Escherichia coli

Quick links

Citations

10 review citations

Protein splicing and related forms of protein autoprocessing.
Paulus H. (2000)
9 more

4 mentions without citation

Structures of apo and product-bound human L-asparaginase: insights into the mechanism of autoproteolysis and substrate hydrolysis.
Nomme et al. (2012)
3 more