2CN3

Crystal Structures of Clostridium thermocellum Xyloglucanase

External Resource: Annotation

Domain Annotation: SCOP/SCOPe Classification
Domain Annotation: ECOD Classification
Domain Annotation: CATH
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)
B	d2cn3b1	All beta proteins	7-bladed beta-propeller	Oligoxyloglucan reducing end-specific cellobiohydrolase	automated matches	automated matches	(Acetivibrio thermocellus ) [TaxId: 1515 ],	SCOPe (2.08)
A	d2cn3a1	All beta proteins	7-bladed beta-propeller	Oligoxyloglucan reducing end-specific cellobiohydrolase	automated matches	automated matches	(Acetivibrio thermocellus ) [TaxId: 1515 ],	SCOPe (2.08)

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
B	PSII_BNR	e2cn3B1	A: beta duplicates or obligate multimers	X: beta-propeller-like	H: beta-propeller	T: 7-bladed	F: PSII_BNR	ECOD (1.6)
B	PSII_BNR_1	e2cn3B2	A: beta duplicates or obligate multimers	X: beta-propeller-like	H: beta-propeller	T: 7-bladed	F: PSII_BNR_1	ECOD (1.6)
A	PSII_BNR	e2cn3A1	A: beta duplicates or obligate multimers	X: beta-propeller-like	H: beta-propeller	T: 7-bladed	F: PSII_BNR	ECOD (1.6)
A	PSII_BNR_1	e2cn3A2	A: beta duplicates or obligate multimers	X: beta-propeller-like	H: beta-propeller	T: 7-bladed	F: PSII_BNR_1	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
B	2.130.10.10	Mainly Beta	7 Propeller	Methylamine Dehydrogenase	Chain H	CATH (4.3.0)
A	2.130.10.10	Mainly Beta	7 Propeller	Methylamine Dehydrogenase	Chain H	CATH (4.3.0)

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B	BETA-1,4-XYLOGLUCAN HYDROLASE	hydrolase activity, acting on glycosyl bonds beta-glucanase activity xyloglucan-specific endo-beta-1,4-glucanase activity hydrolase activity, hydrolyzing O-glycosyl compounds hydrolase activity catalytic activity	carbohydrate metabolic process catabolic process glucan catabolic 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 xyloglucan catabolic process polysaccharide metabolic process glucan metabolic process polysaccharide catabolic process carbohydrate metabolic process catabolic process glucan catabolic 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 xyloglucan catabolic process polysaccharide metabolic process glucan metabolic process polysaccharide catabolic process xyloglucan metabolic process metabolic process cellular process macromolecule metabolic process cell wall polysaccharide metabolic process cell wall polysaccharide catabolic process cell wall macromolecule metabolic process beta-glucan metabolic process beta-glucan catabolic process cellulose catabolic process cellulose metabolic process	cellulosome cellular anatomical structure extracellular organelle extracellular region organelle membraneless organelle extracellular membraneless organelle

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B	IPR002105	Dockerin type I repeat	Repeat
A, B	IPR016134	Dockerin domain	Domain
A, B	IPR018247	EF-Hand 1, calcium-binding site	Binding Site
A, B	IPR052025	Xyloglucan-specific glycosyl hydrolase	Family
A, B	IPR036439	Dockerin domain superfamily	Homologous Superfamily
A, B	IPR015943	WD40/YVTN repeat-like-containing 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.