3AKG

Crystal structure of exo-1,5-alpha-L-arabinofuranosidase complexed with alpha-1,5-L-arabinofuranobiose

External Resource: Annotation

Domain Annotation: ECOD Classification
Domain Annotation: CATH
Protein Family Annotation
Gene Ontology: Gene Product Annotation
InterPro: Protein Family Classification

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
A	Glyco_hydro_43	e3akgA2	A: beta duplicates or obligate multimers	X: beta-propeller-like	H: beta-propeller	T: 5-bladed	F: Glyco_hydro_43	ECOD (1.6)
A	AbfB	e3akgA1	A: beta duplicates or obligate multimers	X: beta-Trefoil (From Topology)	H: beta-Trefoil (From Topology)	T: beta-Trefoil	F: AbfB	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	2.115.10.20	Mainly Beta	5 Propeller	Tachylectin-2	Chain A	CATH (4.3.0)
A	2.80.10.50	Mainly Beta	Trefoil	Trefoil (Acidic Fibroblast Growth Factor, subunit A)		CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A	PF05270	Alpha-L-arabinofuranosidase B (ABFB) domain (AbfB)	Alpha-L-arabinofuranosidase B (ABFB) domain	This family consists of several fungal alpha-L-arabinofuranosidase B proteins. L-Arabinose is a constituent of plant-cell-wall poly-saccharides. It is found in a polymeric form in L-arabinan, in which the backbone is formed by 1,5-a- linked l-arabin ...	This family consists of several fungal alpha-L-arabinofuranosidase B proteins. L-Arabinose is a constituent of plant-cell-wall poly-saccharides. It is found in a polymeric form in L-arabinan, in which the backbone is formed by 1,5-a- linked l-arabinose residues that can be branched via 1,2-a- and 1,3-a-linked l-arabinofuranose side chains. AbfB hydrolyses 1,5-a, 1,3-a and 1,2-a linkages in both oligosaccharides and polysaccharides, which contain terminal non-reducing l-arabinofuranoses in side chains [1].	Domain
A	PF04616	Glycosyl hydrolases family 43 (Glyco_hydro_43)	Glycosyl hydrolases family 43	-	Repeat

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A	Putative secreted alpha L-arabinofuranosidase II	alpha-L-arabinofuranosidase activity hydrolase activity, acting on glycosyl bonds hydrolase activity, hydrolyzing O-glycosyl compounds hydrolase activity catalytic activity	carbohydrate metabolic process catabolic process carbohydrate catabolic process primary metabolic process macromolecule catabolic process arabinan metabolic process arabinan catabolic process polysaccharide metabolic process polysaccharide catabolic process metabolic process cellular process macromolecule metabolic process monosaccharide metabolic process arabinose metabolic process carbohydrate metabolic process catabolic process carbohydrate catabolic process primary metabolic process macromolecule catabolic process arabinan metabolic process arabinan catabolic process polysaccharide metabolic process polysaccharide catabolic process metabolic process cellular process macromolecule metabolic process monosaccharide metabolic process arabinose metabolic process small molecule metabolic process pentose metabolic process L-arabinose metabolic process	cellular anatomical structure extracellular region

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A	IPR007934	Alpha-L-arabinofuranosidase B, arabinose-binding domain	Domain
A	IPR023296	Glycosyl hydrolase, five-bladed beta-propeller domain superfamily	Homologous Superfamily
A	IPR036195	Alpha-L-arabinofuranosidase B, arabinose-binding domain superfamily	Homologous Superfamily
A	IPR006710	Glycoside hydrolase, family 43	Family

RCSB PDB Core Operations are funded by the U.S. National Science Foundation (DBI-2321666), the US Department of Energy (DE-SC0019749), and the National Cancer Institute, National Institute of Allergy and Infectious Diseases, and National Institute of General Medical Sciences of the National Institutes of Health under grant R01GM157729.