5FQG

The details of glycolipid glycan hydrolysis by the structural analysis of a family 123 glycoside hydrolase from Clostridium perfringens


Domain Annotation: ECOD Classification ECOD Database Homepage

ChainsFamily NameDomain Identifier ArchitecturePossible HomologyHomologyTopologyFamilyProvenance Source (Version)
AGlyco_hydro_123_Ne5fqgA2 A: beta sandwichesX: Immunoglobulin-like beta-sandwichH: Immunoglobulin-relatedT: Immunoglobulin/Fibronectin type III/E set domains/PapD-likeF: Glyco_hydro_123_NECOD (1.6)
ADUF4091,Glyco_hydro_123_Ne5fqgA1 A: a/b barrelsX: TIM beta/alpha-barrelH: TIM barrels (From Topology)T: TIM barrelsF: DUF4091,Glyco_hydro_123_NECOD (1.6)

Protein Family Annotation Pfam Database Homepage

ChainsAccessionNameDescriptionCommentsSource
PF22680Glycoside hydrolase 123 N-terminal domain (Glyco_hydro_123_N_2)Glycoside hydrolase 123 N-terminal domainThis entry represents the N-terminal domain of a group of glycoside hydrolases 123, from bacteria [1,2].Domain
PF13320Glycoside hydrolase 123, catalytic domain (GH123_cat)Glycoside hydrolase 123, catalytic domainThis domain is found at the C terminus of protein members of the glycoside hydrolase family 123, including N-acetylgalactosaminidase from Clostridium perfringens. This enzyme removes specific terminal N-D-acetylgalactosamine from glycosphingolipids. ...This domain is found at the C terminus of protein members of the glycoside hydrolase family 123, including N-acetylgalactosaminidase from Clostridium perfringens. This enzyme removes specific terminal N-D-acetylgalactosamine from glycosphingolipids. This catalytic domain adopts an alpha/beta barrel configuration with a two-stranded beta sheet and a pair of alpha-helices at the C-terminal end [1,2].
Domain