3h53

X-ray diffraction
2.01Å resolution

Crystal Structure of human alpha-N-acetylgalactosaminidase

Released:

Function and Biology Details

Reaction catalysed:
Cleavage of non-reducing alpha-(1->3)-N-acetylgalactosamine residues from human blood group A and AB mucin glycoproteins, Forssman hapten and blood group A lacto series glycolipids
Biochemical function:
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
PDBe Complex ID:
PDB-CPX-147860 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (4 distinct):
Alpha-N-acetylgalactosaminidase Chains: A, B
Molecule details ›
Chains: A, B
Length: 400 amino acids
Theoretical weight: 45.58 KDa
Source organism: Homo sapiens
Expression system: Trichoplusia ni
UniProt:
  • Canonical: P17050 (Residues: 18-411; Coverage: 100%)
Gene name: NAGA
Sequence domains:
Structure domains:

Ligands and Environments

Carbohydrate polymer : NEW Components: NAG, BMA, FUC
Carbohydrate polymer : NEW Components: NAG, BMA, MAN
Carbohydrate polymer : NEW Components: NAG, FUC
2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RUH3R
Spacegroup: C2
Unit cell:
a: 153.532Å b: 114.26Å c: 68.408Å
α: 90° β: 96.11° γ: 90°
R-values:
R R work R free
0.163 0.161 0.194
Expression system: Trichoplusia ni