PDBe 3igu

X-ray diffraction
2.15Å resolution

Crystal structure of human alpha-N-acetylgalactosaminidase, covalent intermediate

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:
hetero dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
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


No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X6A
Spacegroup: C2
Unit cell:
a: 151.612Å b: 113.649Å c: 68.415Å
α: 90° β: 96.14° γ: 90°
R-values:
R R work R free
0.166 0.164 0.199
Expression system: Trichoplusia ni