1VWL

STREPTAVIDIN-CYCLO-[5-S-VALERAMIDE-HPQGPPC]K-NH2, PH 3.5, I222 COMPLEX

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 [auth B]	d1vwlb_	All beta proteins	Streptavidin-like	Avidin/streptavidin	Avidin/streptavidin	Streptavidin	(Streptomyces avidinii ) [TaxId: 1895 ],	SCOPe (2.08)
B [auth D]	d1vwld_	All beta proteins	Streptavidin-like	Avidin/streptavidin	Avidin/streptavidin	Streptavidin	(Streptomyces avidinii ) [TaxId: 1895 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A [auth B]	SCOP2B Superfamily	Avidin/streptavidin	8040372	3001465	SCOP2B (2022-06-29)
B [auth D]	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 [auth B]	Avidin	e1vwlB1	A: beta barrels	X: Lipocalins/Streptavidin	H: Avidin/Streptavidin (From Topology)	T: Avidin/Streptavidin	F: Avidin	ECOD (1.6)
B [auth D]	Avidin	e1vwlD1	A: beta barrels	X: Lipocalins/Streptavidin	H: Avidin/Streptavidin (From Topology)	T: Avidin/Streptavidin	F: Avidin	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A [auth B]	2.40.128.30	Mainly Beta	Beta Barrel	Lipocalin	Avidin-like	CATH (4.3.0)
B [auth D]	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 [auth B], B [auth D]	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 [auth B], B [auth D]	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 [auth M], D [auth P]	PEPTIDE LIGAND CONTAINING HPQ	-	-	-

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A [auth B], B [auth D]	IPR017889	Avidin-like, conserved site	Conserved Site
A [auth B], B [auth D]	IPR036896	Avidin-like superfamily	Homologous Superfamily
A [auth B], B [auth D]	IPR051764	Avidin/Streptavidin-related	Family
A [auth B], B [auth D]	IPR005468	Avidin/streptavidin	Family
A [auth B], B [auth D]	IPR005469	Avidin	Family

Protein Modification Annotation

Modified Residue(s)
Chain	Residue(s)	Description
C [auth M], D [auth P]	NH2	RESID: AA0081 , AA0083 , AA0084 , AA0086 , AA0087 , AA0088 , AA0090 , AA0091 , AA0092 , AA0093 , AA0095 , AA0096 , AA0097 , AA0098 , AA0099 , AA0100 PSI-MOD : L-alanine amide MOD:00090 , L-asparagine amide MOD:00092 , L-aspartic acid 1-amide MOD:00093 , L-glutamine amide MOD:00095 , L-glutamic acid 1-amide MOD:00096 , glycine amide MOD:00097 , L-isoleucine amide MOD:00099 , L-leucine amide MOD:00100 , L-lysine amide MOD:00101 , L-methionine amide MOD:00102 , L-proline amide MOD:00104 , L-serine amide MOD:00105 , L-threonine amide MOD:00106 , L-tryptophan amide MOD:00107 , L-tyrosine amide MOD:00108 , L-valine amide MOD:00109

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.