Domain Annotation: ECOD Classification ECOD Database Homepage

ChainsFamily NameDomain Identifier ArchitecturePossible HomologyHomologyTopologyFamilyProvenance Source (Version)
BGcnA_Ce2epoB3 A: alpha bundlesX: Hyaluronidase domain-likeH: Hyaluronidase post-catalytic domain-like (From Topology)T: Hyaluronidase post-catalytic domain-likeF: GcnA_CECOD (1.6)
BGlyco_hydro_20e2epoB1 A: a/b barrelsX: TIM beta/alpha-barrelH: TIM barrels (From Topology)T: TIM barrelsF: Glyco_hydro_20ECOD (1.6)
BGcnA_Ne2epoB2 A: mixed a+b and a/bX: Zincin-likeH: beta-N-acetylhexosaminidase-like domain (From Topology)T: beta-N-acetylhexosaminidase-like domainF: GcnA_NECOD (1.6)
AGcnA_Ce2epoA3 A: alpha bundlesX: Hyaluronidase domain-likeH: Hyaluronidase post-catalytic domain-like (From Topology)T: Hyaluronidase post-catalytic domain-likeF: GcnA_CECOD (1.6)
AGlyco_hydro_20e2epoA2 A: a/b barrelsX: TIM beta/alpha-barrelH: TIM barrels (From Topology)T: TIM barrelsF: Glyco_hydro_20ECOD (1.6)
AGcnA_Ne2epoA1 A: mixed a+b and a/bX: Zincin-likeH: beta-N-acetylhexosaminidase-like domain (From Topology)T: beta-N-acetylhexosaminidase-like domainF: GcnA_NECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Protein Family Annotation Pfam Database Homepage

ChainsAccessionNameDescriptionCommentsSource
A, B
PF18088Glycoside Hydrolase 20C C-terminal domain (Glyco_H_20C_C)Glycoside Hydrolase 20C C-terminal domainThis is the C-terminal domain of Glycoside hydrolase 20 C (GH20C) present in S. pneumoniae. GH20C possesses the ability to hydrolyze the beta-linkages joining either N-acetylglucosamine or N-acetylgalactosamine to a wide variety of aglycon residues. ...This is the C-terminal domain of Glycoside hydrolase 20 C (GH20C) present in S. pneumoniae. GH20C possesses the ability to hydrolyze the beta-linkages joining either N-acetylglucosamine or N-acetylgalactosamine to a wide variety of aglycon residues. The C-terminal domain is commonly known as Domain III is important in dimerization as it forms the primary interface of the dimer. However, there is presently no evidence supporting dimerization as being necessary for catalysis. Domain III is unusual among structurally characterized GH20 enzymes but in GH20 enzymes possessing domain III, dimerization seems to be a conserved feature [1].
Domain
A, B
PF18229N-acetyl-beta-D-glucosaminidase N-terminal domain (GcnA_N)N-acetyl-beta-D-glucosaminidase N-terminal domainThis is the N-terminal domain found in N-acetyl-beta-D-glucosaminidase (GcnA) present in Streptococcus gordonii. GcnA is a family 20 glycosidase that cleaves N-acetyl-beta-D-glucosamine and N-acetyl-beta-D-galactosamine from 4-methylumbelliferylated ...This is the N-terminal domain found in N-acetyl-beta-D-glucosaminidase (GcnA) present in Streptococcus gordonii. GcnA is a family 20 glycosidase that cleaves N-acetyl-beta-D-glucosamine and N-acetyl-beta-D-galactosamine from 4-methylumbelliferylated substrates. Similar N-terminal domains have been observed in all family 20 glycosidases although the number of beta-sheet strands may vary from five [1].
Domain