1ANU | pdb_00001anu

COHESIN-2 DOMAIN OF THE CELLULOSOME FROM CLOSTRIDIUM THERMOCELLUM

External Resource: Annotation

Domain Annotation: SCOP/SCOPe 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	d1anua_	All beta proteins	Common fold of diphtheria toxin/transcription factors/cytochrome f	Carbohydrate-binding domain	Cellulose-binding domain family III	Cohesin domain	(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)
A	Cohesin	e1anuA1	A: beta sandwiches	X: Immunoglobulin-like beta-sandwich	H: Immunoglobulin-related	T: Common fold of diphtheria toxin/transcription factors/cytochrome f	F: Cohesin	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	2.60.40.680	Mainly Beta	Sandwich	Immunoglobulin-like		CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A	PF00963	Cohesin domain (Cohesin)	Cohesin domain	Cohesin domains interact with a complementary domain, termed the dockerin domain. The cohesin-dockerin interaction is the crucial interaction for complex formation in the cellulosome [1].	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A	COHESIN-2	binding polysaccharide binding cellulose binding carbohydrate binding hydrolase activity, acting on glycosyl bonds hydrolase activity, hydrolyzing O-glycosyl compounds hydrolase activity catalytic activity	cellular component organization cell wall organization or biogenesis cell wall organization cellular process cellular component organization or biogenesis external encapsulating structure organization carbohydrate metabolic process catabolic process glucan catabolic process beta-glucan metabolic process carbohydrate catabolic process primary metabolic process macromolecule catabolic process polysaccharide metabolic process cellular component organization cell wall organization or biogenesis cell wall organization cellular process cellular component organization or biogenesis external encapsulating structure organization carbohydrate metabolic process catabolic process glucan catabolic process beta-glucan metabolic process carbohydrate catabolic process primary metabolic process macromolecule catabolic process polysaccharide metabolic process glucan metabolic process beta-glucan catabolic process polysaccharide catabolic process metabolic process cellulose catabolic process macromolecule metabolic process cellulose metabolic process	cellular anatomical structure extracellular region

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A	IPR002105	Dockerin type I repeat	Repeat
A	IPR036966	Carbohydrate-binding module 3 superfamily	Homologous Superfamily
A	IPR016134	Dockerin domain	Domain
A	IPR001956	Carbohydrate-binding module 3	Domain
A	IPR018247	EF-Hand 1, calcium-binding site	Binding Site
A	IPR008965	CBM2/CBM3, carbohydrate-binding domain superfamily	Homologous Superfamily
A	IPR008969	Carboxypeptidase-like, regulatory domain superfamily	Homologous Superfamily
A	IPR002102	Cellulosome anchoring protein, cohesin domain	Domain
A	IPR036439	Dockerin 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.