_EC Endo-alpha-N-acetylgalactosaminidase. 2 PDB entries  
EC 3.-.-.- Hydrolases. [22,330 PDB entries]
EC 3.2.-.- Glycosylases. [4,329 PDB entries]
EC 3.2.1.- Glycosidases, i.e. enzymes hydrolyzing O- and S-glycosyl compound [3,782 PDB entries]
EC Endo-alpha-N-acetylgalactosaminidase. [2 PDB entries]    

Reaction: 3-O-beta-D-galactosyl-N-acetyl-alpha-D-galactosaminyl-L-serine-[protein] + H(2)O = 3-O-beta-D-galactosyl-N-acetyl-alpha-D-galactosamine + L-serine-[protein].
Other name(s): D-galactosyl-3-(N-acetyl-alpha-D-galactosaminyl)-L-serine mucinaminohydrolase. D-galactosyl-N-acetyl-alpha-D-galactosamine D-galactosyl-N-acetyl- galactosaminohydrolase. Endo-alpha-acetylgalactosaminidase. Endo-alpha-GalNAc-ase. Endo-alpha-N-acetyl-D-galactosaminidase. Glycopeptide alpha-N-acetylgalactosaminidase. Mucinaminylserine mucinaminidase.
Comments: The enzyme catalyzes the liberation of Gal-(1->3)-beta-GalNAc alpha- linked to serine or threonine residues of mucin-type glycoproteins. EngBF from Bifidobacterium longum specifically acts on core 1-type O-glycan to release the disaccharide Gal-(1->3)-beta-GalNAc. The enzymes from Clostridium perfringens, Enterococcus faecalis, Propionibacterium acnes and Alcaligenes faecalis show broader specificity (e.g. release of the core 2 trisaccharide Gal-(1->3)- beta-(GlcNAc-(1->6)-beta)-GalNAc or the core 3 disaccharide GlcNAc- (1->3)-beta-GalNAc). The enzyme may play an important role in the degradation and
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There are 2 PDB entries in enzyme class E.C.

  PDB code Protein
Crystal structure of endo-alpha-n-acetylgalactosaminidase from bifidobacterium longum (engbf)
Source: Bifidobacterium longum. Organism_taxid: 216816. Strain: jcm1217. Gene: engbf. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chain: A (1178 residues) CATH domains: 1.20.1270.70
Endo-alpha-n-acetylgalactosaminidase from streptococcus pneu semet structure
Source: Streptococcus pneumoniae. Organism_taxid: 171101. Strain: r6. Gene: spr0328. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chains: A, B (1336 residues) CATH domains: Unassigned