4HKW

Crystal Structures of Mutant Endo-beta-1,4-xylanase II Complexed with Substrate and Products

External Resource: Annotation

Domain Annotation: SCOP/SCOPe Classification
Domain Annotation: SCOP2 Classification
Domain Annotation: ECOD Classification
Domain Annotation: CATH
Protein Family Annotation
Gene Ontology: Gene Product Annotation
InterPro: Protein Family Classification
Protein Modification Annotation

Domain Annotation: SCOP/SCOPe Classification SCOP-e Database Homepage

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
A	d4hkwa1	All beta proteins	Concanavalin A-like lectins/glucanases	Concanavalin A-like lectins/glucanases	Xylanase/endoglucanase 11/12	Xylanase II	(Trichoderma reesei ) [TaxId: 51453 ],	SCOPe (2.08)
A	d4hkwa2	Artifacts	Tags	Tags	Tags	N-terminal Tags	(Trichoderma reesei ) [TaxId: 51453 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2B Superfamily	Concanavalin A-like lectins/glucanases	8039639	3000120	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	Glyco_hydro_11	e4hkwA1	A: beta sandwiches	X: jelly-roll	H: Concanavalin A-like	T: Concanavalin A-like lectins/glucanases	F: Glyco_hydro_11	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	2.60.120.180	Mainly Beta	Sandwich	Jelly Rolls	Glycoside hydrolase family 11/12, catalytic domain	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A	PF00457	Glycosyl hydrolases family 11 (Glyco_hydro_11)	Glycosyl hydrolases family 11	-	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A	Endo-1,4-beta-xylanase 2	xylanase activity hydrolase activity, acting on glycosyl bonds endo-1,4-beta-xylanase activity hydrolase activity, hydrolyzing O-glycosyl compounds hydrolase activity catalytic activity	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 polysaccharide catabolic process metabolic 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 polysaccharide catabolic process metabolic process cellular process macromolecule metabolic process cell wall polysaccharide metabolic process cell wall macromolecule metabolic process cell wall polysaccharide catabolic process	cellular anatomical structure extracellular region

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A	IPR001137	Glycoside hydrolase family 11	Family
A	IPR013320	Concanavalin A-like lectin/glucanase domain superfamily	Homologous Superfamily
A	IPR018208	Glycoside hydrolase family 11, active site 1	Active Site
A	IPR013319	Glycoside hydrolase family 11/12	Homologous Superfamily
A	IPR033123	Glycosyl hydrolases family 11 (GH11) domain	Domain
A	IPR033119	Glycoside hydrolase family 11, active site 2	Active Site

Protein Modification Annotation

Modified Residue(s)
Chain	Residue(s)	Description
A	PCA	Parent Component: GLN RESID: AA0031 PSI-MOD : 2-pyrrolidone-5-carboxylic acid (Gln) MOD:00040 , 2-pyrrolidone-5-carboxylic acid (Glu) MOD:00420

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.