2VMH

The structure of CBM51 from Clostridium perfringens GH95

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	d2vmha_	All beta proteins	Galactose-binding domain-like	Galactose-binding domain-like	NPCBM-like	automated matches	(Clostridium perfringens ) [TaxId: 1502 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2 Family	NPCMB-like	8003770	4000220	SCOP2 (2022-06-29)
A	SCOP2 Superfamily	galactose-binding domain-like	8003771	3000087	SCOP2 (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	NPCBM	e2vmhA1	A: beta sandwiches	X: jelly-roll	H: Concanavalin A-like	T: Galactose-binding domain-like	F: NPCBM	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	2.60.120.1060	Mainly Beta	Sandwich	Jelly Rolls	NPCBM/NEW2 domain	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A	PF08305	NPCBM/NEW2 domain (NPCBM)	NPCBM/NEW2 domain	This novel putative carbohydrate binding module (NPCBM) domain is found at the N-terminus of glycosyl hydrolase family 98 proteins [1]. This domain has also been called the NEW2 domain [2]. NPCBM domains found in bacterial conflict systems are predi ...	This novel putative carbohydrate binding module (NPCBM) domain is found at the N-terminus of glycosyl hydrolase family 98 proteins [1]. This domain has also been called the NEW2 domain [2]. NPCBM domains found in bacterial conflict systems are predicted to interact with invasive molecules and recruit downstream effectors [3].	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A	FIBRONECTIN TYPE III DOMAIN PROTEIN	fucosidase activity hydrolase activity, acting on glycosyl bonds hydrolase activity, hydrolyzing O-glycosyl compounds alpha-L-fucosidase activity hydrolase activity catalytic activity cation binding ion binding binding metal ion binding small molecule binding	carbohydrate metabolic process polysaccharide metabolic process catabolic process polysaccharide catabolic process carbohydrate catabolic process metabolic process cellular process primary metabolic process macromolecule metabolic process macromolecule catabolic process	-

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A	IPR002105	Dockerin type I repeat	Repeat
A	IPR018247	EF-Hand 1, calcium-binding site	Binding Site
A	IPR008928	Six-hairpin glycosidase superfamily	Homologous Superfamily
A	IPR027414	Glycosyl hydrolase family 95, N-terminal domain	Domain
A	IPR003961	Fibronectin type III	Domain
A	IPR008979	Galactose-binding-like domain superfamily	Homologous Superfamily
A	IPR012341	Six-hairpin glycosidase-like superfamily	Homologous Superfamily
A	IPR049053	Alpha fucosidase A-like, C-terminal domain	Domain
A	IPR013320	Concanavalin A-like lectin/glucanase domain superfamily	Homologous Superfamily
A	IPR013222	Glycosyl hydrolase family 98, putative carbohydrate-binding module	Domain
A	IPR013783	Immunoglobulin-like fold	Homologous Superfamily
A	IPR038637	NPCBM domain superfamily	Homologous Superfamily
A	IPR036439	Dockerin domain superfamily	Homologous Superfamily
A	IPR054363	Glycosyl hydrolase family 95, catalytic domain	Domain
A	IPR036116	Fibronectin type III 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.