› 4r4y

X-ray diffraction
2.1Å resolution

Structural basis of a point mutation that causes the genetic disease Aspartylglucosaminuria

Released:
DOI: 10.2210/pdb4r4y/pdb
PDB entry 4r4y coloured by chain, front view.
PDB entry 4r4y coloured by chain, side view.
PDB entry 4r4y coloured by chain, top view.
Source organism: Elizabethkingia miricola
Primary publication:
Structural basis of a point mutation that causes the genetic disease aspartylglucosaminuria.
Sui L, Lakshminarasimhan D, Pande S, Guo HC
Structure 22 1855-1861 (2014)
PMID: 25456816

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 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, B
Molecule details ›
Chains: A, B
Length: 295 amino acids
Theoretical weight: 32.24 KDa
Source organism: Elizabethkingia miricola
Expression system: Escherichia coli
UniProt:
  • Canonical: Q47898 (Residues: 46-340; Coverage: 100%)
Sequence domains: Asparaginase

Ligands and Environments

1 bound ligand:
Ligand SD4 1 x SD4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X29A
Spacegroup: P1
Unit cell:
a: 45.81Å b: 50.62Å c: 61.23Å
α: 86.28° β: 91.04° γ: 107.75°
R-values:
R R work R free
0.194 0.19 0.252
Expression system: Escherichia coli

Quick links

Citations

2 review citations

Aspartylglycosaminuria: a review.
Arvio et al. (2016)
1 more

2 mentions without citation

Structural basis of a point mutation that causes the genetic disease aspartylglucosaminuria.
Sui et al. (2014)
1 more