EBI Databases InterPro	Search Open in usermanual InterPro:
Jump to: InterProScan Databases Documentation FTP site Help Click on the icon for context sensitive help from the user manual. Advanced search

InterPro: IPR004866 Carbohydrate-binding, chitobiase/hexosaminidase-type, N-terminal

Protein matches Help

UniProtKB

Matches:

168 proteins

Overview:	sorted by AC,	sorted by name,	of known structure,	proteins with splice variants
Detailed:	sorted by AC,	sorted by name,	of known structure	proteins with splice variants
Table:	For all matching proteins,	of known structure
Architectures
Accession List
Matches in BioMart

Accession

IPR004866 CB_bd_Hex_N

Type

Domain

Signatures Help

Database	ID	Name	Proteins
Pfam	PF03173	CHB_HEX	168
Signatures in BioMart

InterPro Relationships Help

Parent

IPR012291 Cellulose-binding family II/chitobiase, carbohydrate-binding domain

GO Term annotation Help

Function

GO:0030246 carbohydrate binding

InterPro annotation

Entry Details in BioMart

Abstract

This domain represents the N-terminal domain in chitobiases and beta-hexosaminidases EC:3.2.1.52. Chitobiases degrade chitin, which forms the exoskeleton in insects and crustaceans, and which is one of the most abundant polysaccharides on earth [1]. Beta-hexosaminidases are composed of either a HexA/HexB heterodimer or a HexB homodimer, and can hydrolyse diverse substrates, including GM(2)-gangliosides; mutations in this enzyme are associated with Tay-Sachs disease [2]. HexB is structurally similar to chitobiase, consisting of a beta sandwich structure; this structure is similar to that found in the cellulose-binding domain of cellulase from Cellulomonas fimi (IPR001919), suggesting that it may function as a carbohydrate-binding domain.

Structural links Help

PDB - click here

SCOP: b.2.2.3

CATH: 2.60.40.290

Database links Help

Enzyme: EC:3.2.1.52

PANDIT: PF03173

Blocks: IPB004866

Pfam Clan: CL0203.8

Taxonomic coverage Help

Overlapping InterPro entries Help

IPR004866

Numbers of overlapping proteins

Average numbers of overlapping amino acids

Example proteins Help

Q54468 Chitobiase

More proteins

Example Proteins Key

InterPro entry accession number/name and structure databases		Colour code
IPR013781	Glycoside hydrolase, subgroup, catalytic core
IPR013812	Glycoside hydrolase, family 2/20, immunoglobulin-like beta-sandwich domain
IPR012291	Cellulose-binding family II/chitobiase, carbohydrate-binding domain
IPR004867	Glycoside hydrolase, family 20, C-terminal
IPR014756	Immunoglobulin E-set
IPR015883	Glycoside hydrolase, family 20, catalytic core
IPR008965	Carbohydrate-binding
IPR015882	Beta-N-acetylhexosaminidase-like
IPR004866	Carbohydrate-binding, chitobiase/hexosaminidase-type, N-terminal
IPR017853	Glycoside hydrolase, catalytic core
IPR001540	Glycoside hydrolase, family 20
	PDB Chain
	ModBase
	CATH Domain
	SCOP Domain

Publications Open in usermanual
1.	Tews I, Perrakis A, Oppenheim A, Dauter Z, Wilson KS, Vorgias CE. Bacterial chitobiase structure provides insight into catalytic mechanism and the basis of Tay-Sachs disease. Nat. Struct. Biol. 3 638-48 1996 [PubMed: 8673609] http://dx.doi.org/10.1038/nsb0796-638
2.	Mark BL, Mahuran DJ, Cherney MM, Zhao D, Knapp S, James MN. Crystal structure of human beta-hexosaminidase B: understanding the molecular basis of Sandhoff and Tay-Sachs disease. J. Mol. Biol. 327 1093-109 2003 [PubMed: 12662933] http://dx.doi.org/10.1016/S0022-2836(03)00216-X

Additional Reading Open in usermanual
	Prag G, Papanikolau Y, Tavlas G, Vorgias CE, Petratos K, Oppenheim AB. Structures of chitobiase mutants complexed with the substrate Di-N-acetyl-d-glucosamine: the catalytic role of the conserved acidic pair, aspartate 539 and glutamate 540. J. Mol. Biol. 300 2000 611-7 [PubMed: 10884356] http://dx.doi.org/10.1006/jmbi.2000.3906

InterPro 23.1