2W1W

Native structure of a family 35 carbohydrate binding module from Clostridium thermocellum

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)
A	SCOP2 Family	CBM35-like	8085808	4005087	SCOP2 (2022-06-29)
A	SCOP2 Superfamily	galactose-binding domain-like	8061827	3000087	SCOP2 (2022-06-29)
B	SCOP2B Superfamily	galactose-binding domain-like	8061827	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)
A	PF03422	e2w1wA1	A: beta sandwiches	X: jelly-roll	H: Galactose-binding domain-like (From Topology)	T: Galactose-binding domain-like	F: PF03422	ECOD (1.6)
B	PF03422	e2w1wB1	A: beta sandwiches	X: jelly-roll	H: Galactose-binding domain-like (From Topology)	T: Galactose-binding domain-like	F: PF03422	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	2.60.120.260	Mainly Beta	Sandwich	Jelly Rolls	Galactose-binding domain-like	CATH (4.3.0)
B	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	PF18099	Carbohydrate binding module (family 35) (CBM_35_2)	Carbohydrate binding module (family 35)	This is a delta4,5-anhydrogalacturonic acid-specific carbohydrate-binding module family 35, which is found in several prokaryotic proteins. Its crystal structure shows a jelly roll/beta-sandwich fold with 2 antiparallel sheets made of 4 and 5 antipar ...	This is a delta4,5-anhydrogalacturonic acid-specific carbohydrate-binding module family 35, which is found in several prokaryotic proteins. Its crystal structure shows a jelly roll/beta-sandwich fold with 2 antiparallel sheets made of 4 and 5 antiparallel beta-strands [1]. It is also found at the end of a family of putative glycosyl hydrolases.	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B	LIPOLYTIC ENZYME, G-D-S-L	binding carbohydrate binding hydrolase activity, acting on glycosyl bonds hydrolase activity, hydrolyzing O-glycosyl compounds hydrolase activity catalytic activity hydrolase activity, acting on ester bonds cation binding ion binding metal ion binding small molecule binding	carbohydrate metabolic process catabolic process carbohydrate catabolic process primary metabolic process macromolecule catabolic process polysaccharide metabolic process organic substance metabolic process polysaccharide catabolic process metabolic process macromolecule metabolic process organic substance catabolic process	-

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B	IPR002105	Dockerin type I repeat	Repeat
A, B	IPR001087	GDSL lipase/esterase	Family
A, B	IPR016134	Dockerin domain	Domain
A, B	IPR041342	Carbohydrate binding module family 35	Domain
A, B	IPR018247	EF-Hand 1, calcium-binding site	Binding Site
A, B	IPR036514	SGNH hydrolase superfamily	Homologous Superfamily
A, B	IPR008979	Galactose-binding-like domain superfamily	Homologous Superfamily
A, B	IPR013830	SGNH hydrolase-type esterase domain	Domain
A, B	IPR005084	Carbohydrate binding module family 6	Domain
A, B	IPR049033	Beta-agarase/YXIM esterase-like, galactose-binding domain-like	Domain
A, B	IPR036439	Dockerin domain superfamily	Homologous Superfamily
A, B	IPR037459	Rhamnogalacturonan acetylesterase RhgT-like	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 R01GM133198.