3WXP

Structure of hyperthermophilic family 12 endocellulase (E197A) from Pyrococcus furiosus in complex with cellobiose

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_12	e3wxpA1	A: beta sandwiches	X: jelly-roll	H: Concanavalin A-like	T: Concanavalin A-like lectins/glucanases	F: Glyco_hydro_12	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	2.60.120.180	Mainly Beta	Sandwich	Jelly Rolls	Glycoside hydrolase family 11/12, catalytic domain	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A	PF01670	Glycosyl hydrolase family 12 (Glyco_hydro_12)	Glycosyl hydrolase family 12	-	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A	Endoglucanase A	hydrolase activity, acting on glycosyl bonds cellulase activity hydrolase activity, hydrolyzing O-glycosyl compounds 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 primary metabolic process macromolecule metabolic process macromolecule catabolic process	-

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A	IPR013320	Concanavalin A-like lectin/glucanase domain superfamily	Homologous Superfamily
A	IPR013319	Glycoside hydrolase family 11/12	Homologous Superfamily
A	IPR002594	Glycoside hydrolase family 12	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.