3ZUC | pdb_00003zuc

Structure of CBM3b of major scaffoldin subunit ScaA from Acetivibrio cellulolyticus determined from the crystals grown in the presence of Nickel

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	d3zuca1	All beta proteins	Common fold of diphtheria toxin/transcription factors/cytochrome f	Carbohydrate-binding domain	automated matches	automated matches	(Acetivibrio cellulolyticus ) [TaxId: 35830 ],	SCOPe (2.08)
A	d3zuca2	Artifacts	Tags	Tags	Tags	N-terminal Tags	(Acetivibrio cellulolyticus ) [TaxId: 35830 ],	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	CBM_3	e3zucA1	A: beta sandwiches	X: Immunoglobulin-like beta-sandwich	H: Immunoglobulin-related	T: Common fold of diphtheria toxin/transcription factors/cytochrome f	F: CBM_3	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	2.60.40.710	Mainly Beta	Sandwich	Immunoglobulin-like	Endoglucanase-like	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A	PF00942	Cellulose binding domain (CBM_3)	Cellulose binding domain		Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A	CELLULOSOMAL SCAFFOLDIN	hydrolase activity, acting on glycosyl bonds cellulase activity hydrolase activity, hydrolyzing O-glycosyl compounds hydrolase activity catalytic activity binding polysaccharide binding cellulose binding carbohydrate binding cation binding ion binding metal ion binding small molecule binding	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 cellular process cellulose catabolic process 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 cellular 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	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	IPR008928	Six-hairpin glycosidase superfamily	Homologous Superfamily
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	IPR012341	Six-hairpin glycosidase-like superfamily	Homologous Superfamily
A	IPR033126	Glycosyl hydrolases family 9, Asp/Glu active sites	Active Site
A	IPR001701	Glycoside hydrolase family 9	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.