Annotations: 5N8W

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2B Superfamily	Avidin/streptavidin	8040372	3001465	SCOP2B (2022-06-29)
B	SCOP2B Superfamily	Avidin/streptavidin	8040372	3001465	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	PF01382	e5n8wA1	A: beta barrels	X: Lipocalins/Streptavidin	H: Avidin/Streptavidin (From Topology)	T: Avidin/Streptavidin	F: PF01382	ECOD (1.6)
B	PF01382	e5n8wB1	A: beta barrels	X: Lipocalins/Streptavidin	H: Avidin/Streptavidin (From Topology)	T: Avidin/Streptavidin	F: PF01382	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	2.40.128.30	Mainly Beta	Beta Barrel	Lipocalin	Avidin-like	CATH (4.3.0)
B	2.40.128.30	Mainly Beta	Beta Barrel	Lipocalin	Avidin-like	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B	PF01382	Avidin family (Avidin)	Avidin family	-	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B	Streptavidin	biotin binding amide binding organic acid binding binding vitamin binding ion binding organic cyclic compound binding anion binding carboxylic acid binding heterocyclic compound binding monocarboxylic acid binding small molecule binding sulfur compound binding	-	extracellular region cellular anatomical entity
C, D	GLY-GLY-DTR-DHI-DAS-DGL-DAL-DTH-DTR-DLY	-	-	-

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B	IPR017889	Avidin-like, conserved site	Conserved Site
A, B	IPR036896	Avidin-like superfamily	Homologous Superfamily
A, B	IPR005468	Avidin/streptavidin	Family
A, B	IPR005469	Avidin	Family

Protein Modification Annotation

Modified Residue(s)
Chain	Residue(s)	Description
C, D	DAL	RESID: AA0111 , AA0191 PSI-MOD : meso-lanthionine MOD:00120 , D-alanine (Ala) MOD:00198 , D-alanine (Ser) MOD:00858 , D-alanine MOD:00862
C, D	DAS	RESID: AA0111 , AA0191 , AA0190 PSI-MOD : meso-lanthionine MOD:00120 , D-alanine (Ala) MOD:00198 , D-alanine (Ser) MOD:00858 , D-alanine MOD:00862 , D-aspartic acid (Asp) MOD:01921 , D-aspartic acid (Asn) MOD:01930
C, D	DGL	RESID: AA0111 , AA0191 , AA0190
C, D	DHI	RESID: AA0111 , AA0191 , AA0190
C, D	DLY	RESID: AA0111 , AA0191 , AA0190
C, D	DPR	RESID: AA0111 , AA0191 , AA0190
C, D	DTH	RESID: AA0111 , AA0191 , AA0190 , AA0199 PSI-MOD : meso-lanthionine MOD:00120 , D-alanine (Ala) MOD:00198 , D-alanine (Ser) MOD:00858 , D-alanine MOD:00862 , D-aspartic acid (Asp) MOD:01921 , D-aspartic acid (Asn) MOD:01930 , D-allo-threonine MOD:00863
C, D	DTR	RESID: AA0111 , AA0191 , AA0190 , AA0199 , AA0198 PSI-MOD : meso-lanthionine MOD:00120 , D-alanine (Ala) MOD:00198 , D-alanine (Ser) MOD:00858 , D-alanine MOD:00862 , D-aspartic acid (Asp) MOD:01921 , D-aspartic acid (Asn) MOD:01930 , D-allo-threonine MOD:00863 , D-tryptophan MOD:00205

RCSB PDB Core Operations are funded by the National Science Foundation (DBI-1832184), 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.