7P1O

Structure of KDNase from Aspergillus Terrerus in complex with 2-keto-3-deoxynononic acid

External Resource: Annotation

Domain Annotation: ECOD Classification
Protein Family Annotation
Gene Ontology: Gene Product Annotation
InterPro: Protein Family Classification
Protein Modification Annotation

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
A [auth X]	BNR_2	e7p1oX1	A: beta duplicates or obligate multimers	X: beta-propeller-like	H: beta-propeller	T: 6-bladed	F: BNR_2	ECOD (1.6)
B [auth A]	BNR_2	e7p1oA1	A: beta duplicates or obligate multimers	X: beta-propeller-like	H: beta-propeller	T: 6-bladed	F: BNR_2	ECOD (1.6)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A [auth X], B [auth A]	PF13088	BNR repeat-like domain (BNR_2)	BNR repeat-like domain	-	Repeat

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A [auth X], B [auth A]	Sialidase domain-containing protein	cation binding ion binding binding metal ion binding small molecule binding hydrolase activity, acting on glycosyl bonds alpha-sialidase activity hydrolase activity, hydrolyzing O-glycosyl compounds hydrolase activity exo-alpha-sialidase activity catalytic activity	-	-

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A [auth X], B [auth A]	IPR011040	Sialidase	Domain
A [auth X], B [auth A]	IPR026856	Sialidase family	Family
A [auth X], B [auth A]	IPR036278	Sialidase superfamily	Homologous Superfamily

Protein Modification Annotation

Modified Residue(s)
Chain	Residue(s)	Description
A [auth X], B [auth A]	SNN	Parent Component: ASN RESID: AA0302 , AA0593 PSI-MOD : L-aspartimide MOD:00307 , 2-(2-aminosuccinimidyl)pentanedioic acid (Asn) MOD:01940 , 2-(2-aminosuccinimidyl)pentanedioic acid (Asp) MOD:01941

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.