2VZP

Atomic Resolution Structure of the C-terminal CBM35 from Amycolatopsis orientalis exo-chitosanase CsxA

External Resource: Annotation

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: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
B	SCOP2 Family	CBM35-like	8061828	4005087	SCOP2 (2022-06-29)
B	SCOP2 Superfamily	galactose-binding domain-like	8061829	3000087	SCOP2 (2022-06-29)
A	SCOP2B Superfamily	galactose-binding domain-like	8061829	3000087	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)
B	CBM_35	e2vzpB1	A: beta sandwiches	X: jelly-roll	H: Concanavalin A-like	T: Galactose-binding domain-like	F: CBM_35	ECOD (1.6)
A	CBM_35	e2vzpA1	A: beta sandwiches	X: jelly-roll	H: Concanavalin A-like	T: Galactose-binding domain-like	F: CBM_35	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
B	2.60.120.260	Mainly Beta	Sandwich	Jelly Rolls	Galactose-binding domain-like	CATH (4.3.0)
A	2.60.120.260	Mainly Beta	Sandwich	Jelly Rolls	Galactose-binding domain-like	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B	PF16990	Carbohydrate binding module (family 35) (CBM_35)	Carbohydrate binding module (family 35)	This is a mannan-specific carbohydrate binding domain, previously known as the X4 module [1]. Unlike other carbohydrate binding modules, binding to substrate causes a conformational change [2].	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B	EXO-BETA-D-GLUCOSAMINIDASE	binding carbohydrate binding hydrolase activity, acting on glycosyl bonds hydrolase activity, hydrolyzing O-glycosyl compounds hydrolase activity catalytic activity exo-1,4-beta-D-glucosaminidase activity	carbohydrate derivative catabolic process catabolic process carbohydrate derivative metabolic process chitin metabolic process aminoglycan catabolic process macromolecule catabolic process glucosamine-containing compound catabolic process amino sugar catabolic process aminoglycan metabolic process amino sugar metabolic process metabolic process cellular process macromolecule metabolic process chitin catabolic process carbohydrate derivative catabolic process catabolic process carbohydrate derivative metabolic process chitin metabolic process aminoglycan catabolic process macromolecule catabolic process glucosamine-containing compound catabolic process amino sugar catabolic process aminoglycan metabolic process amino sugar metabolic process metabolic process cellular process macromolecule metabolic process chitin catabolic process glucosamine-containing compound metabolic process carbohydrate metabolic process polysaccharide metabolic process polysaccharide catabolic process carbohydrate catabolic process primary metabolic process	cellular anatomical structure extracellular region

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B	IPR041351	Exo-beta-D-glucosaminidase, Ig-fold domain	Domain
A, B	IPR017853	Glycoside hydrolase superfamily	Homologous Superfamily
A, B	IPR008979	Galactose-binding-like domain superfamily	Homologous Superfamily
A, B	IPR006102	Glycoside hydrolase, family 2, immunoglobulin-like beta-sandwich	Domain
A, B	IPR036156	Beta-Galactosidase/glucuronidase domain superfamily	Homologous Superfamily
A, B	IPR005084	Carbohydrate binding module family 6	Domain
A, B	IPR043534	Exo-beta-D-glucosaminidase/Endo-beta-mannosidase	Family
A, B	IPR013783	Immunoglobulin-like fold	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.