4Q56

Structure of Helix aspersa agglutinin with natural glycosylation and N-acetyl-alpha-D-galactosamine (GalNAc)

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	d4q56a_	All beta proteins	HPA-like	Agglutinin HPA-like	Agglutinin HPA-like	automated matches	(Cornu aspersum ) [TaxId: 6535 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2 Family	Agglutinin HPA-like	8085262	4001624	SCOP2 (2022-06-29)
A	SCOP2 Superfamily	Agglutinin HPA-like	8085263	3001999	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	H_lectin	e4q56A1	A: beta sandwiches	X: Agglutinin HPA-like	H: Agglutinin HPA-like (From Topology)	T: Agglutinin HPA-like	F: H_lectin	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	2.60.40.2080	Mainly Beta	Sandwich	Immunoglobulin-like		CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A	PF09458	H-type lectin domain (H_lectin)	H-type lectin domain	The H-type lectin domain is a unit of six beta chains, combined into a homo-hexamer. It is involved in self/non-self recognition of cells, through binding with carbohydrates [1]. It is sometimes found in association with the F5_F8_type_C domain Pfam: ...	The H-type lectin domain is a unit of six beta chains, combined into a homo-hexamer. It is involved in self/non-self recognition of cells, through binding with carbohydrates [1]. It is sometimes found in association with the F5_F8_type_C domain Pfam:PF00754.	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A	Helix aspersa agglutinin (HAA)	binding polysaccharide binding carbohydrate binding N-acetylgalactosamine binding carbohydrate derivative binding oligosaccharide binding cation binding ion binding metal ion binding small molecule binding	cell adhesion cell-cell adhesion cellular process	cell surface cellular anatomical structure membrane-bounded organelle intracellular anatomical structure intracellular vesicle phagocytic vesicle intracellular membrane-bounded organelle intracellular organelle cytoplasmic vesicle organelle cytoplasm vesicle endocytic vesicle protein-containing complex cell surface cellular anatomical structure membrane-bounded organelle intracellular anatomical structure intracellular vesicle phagocytic vesicle intracellular membrane-bounded organelle intracellular organelle cytoplasmic vesicle organelle cytoplasm vesicle endocytic vesicle protein-containing complex protein complex involved in cell adhesion

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A	IPR037221	H-type lectin domain superfamily	Homologous Superfamily
A	IPR019019	H-type lectin domain	Domain
A	IPR052487	Galactose-binding lectin	Family

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.