1V7V

Crystal structure of Vibrio proteolyticus chitobiose phosphorylase

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	d1v7va1	All alpha proteins	alpha/alpha toroid	Six-hairpin glycosidases	Glycosyltransferase family 36 C-terminal domain	Chitobiose phosphorylase ChbP	(Vibrio proteolyticus ) [TaxId: 671 ],	SCOPe (2.08)
A	d1v7va2	All beta proteins	Supersandwich	Galactose mutarotase-like	Glycosyltransferase family 36 N-terminal domain	Chitobiose phosphorylase ChbP	(Vibrio proteolyticus ) [TaxId: 671 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2B Superfamily	Six-hairpin glycosidases	8041195	3000970	SCOP2B (2022-06-29)
A	SCOP2B Superfamily	Galactose mutarotase-like	8041196	3000035	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_transf_36	e1v7vA1	A: beta sandwiches	X: Glycosyl hydrolase domain-like	H: supersandwich (From Topology)	T: supersandwich	F: Glyco_transf_36	ECOD (1.6)
A	Glyco_hydro_65C_1	e1v7vA3	A: beta sandwiches	X: Glycosyl hydrolase domain-like	H: Glycoside hydrolase family 127 middle domain-related (From Topology)	T: Glycoside hydrolase family 127 middle domain-related	F: Glyco_hydro_65C_1	ECOD (1.6)
A	Glyco_hydro_36	e1v7vA2	A: alpha superhelices	X: Repetitive alpha hairpins	H: alpha/alpha toroid (From Topology)	T: alpha/alpha toroid	F: Glyco_hydro_36	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	2.70.98.40	Mainly Beta	Distorted Sandwich	Beta-galactosidase	Chain A, domain 5	CATH (4.3.0)
A	2.60.420.10	Mainly Beta	Sandwich	Maltose phosphorylase, domain 3	Maltose phosphorylase, domain 3	CATH (4.3.0)
A	1.50.10.10	Mainly Alpha	Alpha/alpha barrel	Glycosyltransferase		CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A	PF17167	Glycosyl hydrolase 36 superfamily, catalytic domain (Glyco_hydro_36)	Glycosyl hydrolase 36 superfamily, catalytic domain	-	Repeat
A	PF06165	Glycosyltransferase family 36 (Glyco_transf_36)	Glycosyltransferase family 36	The glycosyltransferase family 36 includes cellobiose phosphorylase (EC:2.4.1.20), cellodextrin phosphorylase (EC:2.4.1.49), chitobiose phosphorylase (EC:2.4.1.-). Many members of this family contain two copies of this domain.	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A	chitobiose phosphorylase	binding carbohydrate binding glycosyltransferase activity transferase activity catalytic activity	carbohydrate metabolic process primary metabolic process metabolic process cellular process	-

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A	IPR012341	Six-hairpin glycosidase-like superfamily	Homologous Superfamily
A	IPR009342	Putative carbohydrate binding domain	Domain
A	IPR037018	Glycoside hydrolase family 65, N-terminal domain superfamily	Homologous Superfamily
A	IPR033432	Glycosyl hydrolase 36, catalytic domain	Domain
A	IPR052047	Glycosyl Hydrolase 94 Enzymes	Family
A	IPR008928	Six-hairpin glycosidase superfamily	Homologous Superfamily
A	IPR010383	Glycosyl hydrolase 94	Domain
A	IPR037828	N,N'-diacetylchitobiose phosphorylase, N-terminal	Domain
A	IPR011013	Galactose mutarotase-like domain superfamily	Homologous Superfamily

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.