1GQJ

Structure of Pseudomonas cellulosa alpha-D-glucuronidase complexed with xylobiose

External Resource: Annotation

Domain Annotation: SCOP/SCOPe Classification
Domain Annotation: SCOP2 Classification
Domain Annotation: ECOD Classification
Domain Annotation: CATH
Protein Family Annotation
Gene Ontology: Gene Product Annotation
InterPro: Protein Family Classification

Domain Annotation: SCOP/SCOPe Classification SCOP-e Database Homepage

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
A	d1gqja1	Alpha and beta proteins (a/b)	TIM beta/alpha-barrel	(Trans)glycosidases	alpha-D-glucuronidase/Hyaluronidase catalytic domain	alpha-D-glucuronidase catalytic domain	(Cellvibrio japonicus ) [TaxId: 155077 ],	SCOPe (2.08)
A	d1gqja2	Alpha and beta proteins (a+b)	Zincin-like	beta-N-acetylhexosaminidase-like domain	alpha-D-glucuronidase, N-terminal domain	alpha-D-glucuronidase, N-terminal domain	(Cellvibrio japonicus ) [TaxId: 155077 ],	SCOPe (2.08)
B	d1gqjb1	Alpha and beta proteins (a/b)	TIM beta/alpha-barrel	(Trans)glycosidases	alpha-D-glucuronidase/Hyaluronidase catalytic domain	alpha-D-glucuronidase catalytic domain	(Cellvibrio japonicus ) [TaxId: 155077 ],	SCOPe (2.08)
B	d1gqjb2	Alpha and beta proteins (a+b)	Zincin-like	beta-N-acetylhexosaminidase-like domain	alpha-D-glucuronidase, N-terminal domain	alpha-D-glucuronidase, N-terminal domain	(Cellvibrio japonicus ) [TaxId: 155077 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2B Superfamily	beta-N-acetylhexosaminidase-like domain	8042248	3000192	SCOP2B (2022-06-29)
A	SCOP2B Superfamily	(Trans)glycosidases	8042247	3000313	SCOP2B (2022-06-29)
B	SCOP2B Superfamily	beta-N-acetylhexosaminidase-like domain	8042248	3000192	SCOP2B (2022-06-29)
B	SCOP2B Superfamily	(Trans)glycosidases	8042247	3000313	SCOP2B (2022-06-29)

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
A	Glyco_hydro_67M	e1gqjA1	A: a/b barrels	X: TIM beta/alpha-barrel	H: TIM barrels (From Topology)	T: TIM barrels	F: Glyco_hydro_67M	ECOD (1.6)
A	Glyco_hydro_67N	e1gqjA2	A: mixed a+b and a/b	X: Zincin-like	H: beta-N-acetylhexosaminidase-like domain (From Topology)	T: beta-N-acetylhexosaminidase-like domain	F: Glyco_hydro_67N	ECOD (1.6)
B	Glyco_hydro_67M	e1gqjB1	A: a/b barrels	X: TIM beta/alpha-barrel	H: TIM barrels (From Topology)	T: TIM barrels	F: Glyco_hydro_67M	ECOD (1.6)
B	Glyco_hydro_67N	e1gqjB2	A: mixed a+b and a/b	X: Zincin-like	H: beta-N-acetylhexosaminidase-like domain (From Topology)	T: beta-N-acetylhexosaminidase-like domain	F: Glyco_hydro_67N	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	3.30.379.10	Alpha Beta	2-Layer Sandwich	Chitobiase	domain 2	CATH (4.3.0)
A	3.20.20.80	Alpha Beta	Alpha-Beta Barrel	TIM Barrel	Glycosidases	CATH (4.3.0)
A	3.90.1330.10	Alpha Beta	Alpha-Beta Complex	Alpha-d-glucuronidase, C-terminal Domain	Alpha-glucuronidase, C-terminal domain	CATH (4.3.0)
B	3.30.379.10	Alpha Beta	2-Layer Sandwich	Chitobiase	domain 2	CATH (4.3.0)
B	3.20.20.80	Alpha Beta	Alpha-Beta Barrel	TIM Barrel	Glycosidases	CATH (4.3.0)
B	3.90.1330.10	Alpha Beta	Alpha-Beta Complex	Alpha-d-glucuronidase, C-terminal Domain	Alpha-glucuronidase, C-terminal domain	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B	PF03648	Glycosyl hydrolase family 67 N-terminus (Glyco_hydro_67N)	Glycosyl hydrolase family 67 N-terminus	Alpha-glucuronidases, components of an ensemble of enzymes central to the recycling of photosynthetic biomass, remove the alpha-1,2 linked 4-O-methyl glucuronic acid from xylans. This family represents the N-terminal region of alpha-glucuronidase. Th ...	Alpha-glucuronidases, components of an ensemble of enzymes central to the recycling of photosynthetic biomass, remove the alpha-1,2 linked 4-O-methyl glucuronic acid from xylans. This family represents the N-terminal region of alpha-glucuronidase. The N-terminal domain forms a two-layer sandwich, each layer being formed by a beta sheet of five strands. A further two helices form part of the interface with the central, catalytic, module (Pfam:PF07488) [1].	Domain
A, B	PF07477	Glycosyl hydrolase family 67 C-terminus (Glyco_hydro_67C)	Glycosyl hydrolase family 67 C-terminus	Alpha-glucuronidases, components of an ensemble of enzymes central to the recycling of photosynthetic biomass, remove the alpha-1,2 linked 4-O-methyl glucuronic acid from xylans. This family represents the C terminal region of alpha-glucuronidase whi ...	Alpha-glucuronidases, components of an ensemble of enzymes central to the recycling of photosynthetic biomass, remove the alpha-1,2 linked 4-O-methyl glucuronic acid from xylans. This family represents the C terminal region of alpha-glucuronidase which is mainly alpha-helical. It wraps around the catalytic domain (Pfam:PF07488), making additional interactions both with the N-terminal domain (Pfam:PF03648) of its parent monomer and also forming the majority of the dimer-surface with the equivalent C-terminal domain of the other monomer of the dimer [1].	Domain
A, B	PF07488	Glycosyl hydrolase family 67 middle domain (Glyco_hydro_67M)	Glycosyl hydrolase family 67 middle domain	Alpha-glucuronidases, components of an ensemble of enzymes central to the recycling of photosynthetic biomass, remove the alpha-1,2 linked 4-O-methyl glucuronic acid from xylans. This family represents the central catalytic domain of alpha-glucuroni ...	Alpha-glucuronidases, components of an ensemble of enzymes central to the recycling of photosynthetic biomass, remove the alpha-1,2 linked 4-O-methyl glucuronic acid from xylans. This family represents the central catalytic domain of alpha-glucuronidase [1].	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B	ALPHA-D-GLUCURONIDASE	hydrolase activity, acting on glycosyl bonds alpha-glucuronidase activity hydrolase activity, hydrolyzing O-glycosyl compounds hydrolase activity catalytic activity xylan alpha-1,2-glucuronosidase activity	carbohydrate metabolic process xylan catabolic process catabolic process glucuronoxylan metabolic process hemicellulose metabolic process cell wall organization or biogenesis carbohydrate catabolic process hemicellulose catabolic process primary metabolic process macromolecule catabolic process cell wall macromolecule catabolic process xylan metabolic process polysaccharide metabolic process polysaccharide catabolic process carbohydrate metabolic process xylan catabolic process catabolic process glucuronoxylan metabolic process hemicellulose metabolic process cell wall organization or biogenesis carbohydrate catabolic process hemicellulose catabolic process primary metabolic process macromolecule catabolic process cell wall macromolecule catabolic process xylan metabolic process polysaccharide metabolic process polysaccharide catabolic process metabolic process cellular process macromolecule metabolic process glucuronoxylan catabolic process cell wall polysaccharide metabolic process cell wall macromolecule metabolic process cell wall polysaccharide catabolic process	extracellular region cellular anatomical entity cell periphery cell outer membrane external encapsulating structure membrane cell envelope outer membrane

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B	IPR011099	Glycosyl hydrolase family 67, C-terminal	Domain
A, B	IPR037054	Alpha-glucuronidase, C-terminal domain superfamily	Homologous Superfamily
A, B	IPR011100	Glycosyl hydrolase family 67, catalytic domain	Domain
A, B	IPR017853	Glycoside hydrolase superfamily	Homologous Superfamily
A, B	IPR029018	Beta-hexosaminidase-like, domain 2	Homologous Superfamily
A, B	IPR011395	Alpha glucuronidase	Family
A, B	IPR005154	Alpha glucuronidase, N-terminal	Domain

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.