7AX7

Crystal structure of the Xyl-CE4 domain of a multidomain xylanase from the hindgut metagenome of Trinervitermes trinervoides

External Resource: Annotation

Domain Annotation: SCOP/SCOPe Classification
Domain Annotation: SCOP2 Classification
Domain Annotation: ECOD Classification
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	d7ax7a_	Alpha and beta proteins (a/b)	7-stranded beta/alpha barrel	Glycoside hydrolase/deacetylase	automated matches	automated matches	(uncultured bacterium ) [TaxId: 77133 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2 Family	NodB-like	8101222	4000448	SCOP2 (2022-06-29)
A	SCOP2 Superfamily	Glycoside hydrolase/deacetylase	8101223	3001025	SCOP2 (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	PF01522	e7ax7A1	A: a/b barrels	X: TIM beta/alpha-barrel	H: Glycoside hydrolase/deacetylase (From Topology)	T: Glycoside hydrolase/deacetylase	F: PF01522	ECOD (1.6)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A	PF01522	Polysaccharide deacetylase (Polysacc_deac_1)	Polysaccharide deacetylase	-	Family

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A	Endo-1,4-beta-xylanase	binding carbohydrate binding hydrolase activity catalytic activity hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds xylanase activity hydrolase activity, acting on glycosyl bonds endo-1,4-beta-xylanase activity hydrolase activity, hydrolyzing O-glycosyl compounds	carbohydrate metabolic process xylan catabolic process 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 xylan metabolic process polysaccharide metabolic process organic substance metabolic process polysaccharide catabolic process carbohydrate metabolic process xylan catabolic process 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 xylan metabolic process polysaccharide metabolic process organic substance metabolic process polysaccharide catabolic process metabolic process cellular process macromolecule metabolic process cell wall polysaccharide metabolic process organic substance catabolic process cell wall macromolecule metabolic process cell wall polysaccharide catabolic process	-

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A	IPR018208	Glycoside hydrolase family 11, active site 1	Active Site
A	IPR013319	Glycoside hydrolase family 11/12	Homologous Superfamily
A	IPR008979	Galactose-binding-like domain superfamily	Homologous Superfamily
A	IPR002509	NodB homology domain	Domain
A	IPR033119	Glycoside hydrolase family 11, active site 2	Active Site
A	IPR011330	Glycoside hydrolase/deacetylase, beta/alpha-barrel	Homologous Superfamily
A	IPR001137	Glycoside hydrolase family 11	Family
A	IPR013320	Concanavalin A-like lectin/glucanase domain superfamily	Homologous Superfamily
A	IPR005084	Carbohydrate binding module family 6	Domain
A	IPR033123	Glycosyl hydrolases family 11 (GH11) domain	Domain

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.