2Z48

Crystal Structure of Hemolytic Lectin CEL-III Complexed with 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	d2z48a1	All beta proteins	beta-Trefoil	Ricin B-like lectins	Ricin B-like	Hemolytic lectin CEL-III, domains 1 and 2	(Pseudocnus echinatus ) [TaxId: 2592315 ],	SCOPe (2.08)
A	d2z48a3	Alpha and beta proteins (a+b)	Hemolytic lectin CEL-III, C-terminal domain	Hemolytic lectin CEL-III, C-terminal domain	Hemolytic lectin CEL-III, C-terminal domain	Hemolytic lectin CEL-III, C-terminal domain	(Pseudocnus echinatus ) [TaxId: 2592315 ],	SCOPe (2.08)
B	d2z48b1	All beta proteins	beta-Trefoil	Ricin B-like lectins	Ricin B-like	Hemolytic lectin CEL-III, domains 1 and 2	(Pseudocnus echinatus ) [TaxId: 2592315 ],	SCOPe (2.08)
B	d2z48b3	Alpha and beta proteins (a+b)	Hemolytic lectin CEL-III, C-terminal domain	Hemolytic lectin CEL-III, C-terminal domain	Hemolytic lectin CEL-III, C-terminal domain	Hemolytic lectin CEL-III, C-terminal domain	(Pseudocnus echinatus ) [TaxId: 2592315 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2B Superfamily	Aerolisin/ETX/LSL pore-forming domain-like	8041259	3000278	SCOP2B (2022-06-29)
A	SCOP2B Superfamily	Ricin B-like lectins	8041271	3000678	SCOP2B (2022-06-29)
A	SCOP2B Superfamily	Ricin B-like lectins	8041268	3000678	SCOP2B (2022-06-29)
B	SCOP2B Superfamily	Aerolisin/ETX/LSL pore-forming domain-like	8041259	3000278	SCOP2B (2022-06-29)
B	SCOP2B Superfamily	Ricin B-like lectins	8041271	3000678	SCOP2B (2022-06-29)
B	SCOP2B Superfamily	Ricin B-like lectins	8041268	3000678	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	Ricin_B_lectin	e2z48A1	A: beta duplicates or obligate multimers	X: beta-Trefoil (From Topology)	H: beta-Trefoil (From Topology)	T: beta-Trefoil	F: Ricin_B_lectin	ECOD (1.6)
A	EUF08571	e2z48A3	A: beta complex topology	X: Aerolysin family of pore-forming toxins (From Topology)	H: Aerolysin family of pore-forming toxins (From Topology)	T: Aerolysin family of pore-forming toxins	F: EUF08571	ECOD (1.6)
B	Ricin_B_lectin	e2z48B1	A: beta duplicates or obligate multimers	X: beta-Trefoil (From Topology)	H: beta-Trefoil (From Topology)	T: beta-Trefoil	F: Ricin_B_lectin	ECOD (1.6)
B	EUF08571	e2z48B3	A: beta complex topology	X: Aerolysin family of pore-forming toxins (From Topology)	H: Aerolysin family of pore-forming toxins (From Topology)	T: Aerolysin family of pore-forming toxins	F: EUF08571	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	2.80.10.50	Mainly Beta	Trefoil	Trefoil (Acidic Fibroblast Growth Factor, subunit A)		CATH (4.3.0)
A	3.30.1750.10	Alpha Beta	2-Layer Sandwich	hemolytic lectin cel-iii, domain 3	Hemolytic lectin CEL-III, C-terminal domain	CATH (4.3.0)
B	2.80.10.50	Mainly Beta	Trefoil	Trefoil (Acidic Fibroblast Growth Factor, subunit A)		CATH (4.3.0)
B	3.30.1750.10	Alpha Beta	2-Layer Sandwich	hemolytic lectin cel-iii, domain 3	Hemolytic lectin CEL-III, C-terminal domain	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B	PF00652	Ricin-type beta-trefoil lectin domain (Ricin_B_lectin)	Ricin-type beta-trefoil lectin domain	-	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B	Hemolytic lectin CEL-III	cation binding magnesium ion binding ion binding binding metal ion binding small molecule binding calcium ion binding N-acetylgalactosamine binding carbohydrate derivative binding fucose binding monosaccharide binding carbohydrate binding oligosaccharide binding lactose binding cation binding magnesium ion binding ion binding binding metal ion binding small molecule binding calcium ion binding N-acetylgalactosamine binding carbohydrate derivative binding fucose binding monosaccharide binding carbohydrate binding oligosaccharide binding lactose binding disaccharide binding galactose binding UDP-glycosyltransferase activity polypeptide N-acetylgalactosaminyltransferase activity catalytic activity, acting on a protein glycosyltransferase activity transferase activity acetylgalactosaminyltransferase activity hexosyltransferase activity catalytic activity melibiose binding	biological process involved in interspecies interaction between organisms response to stimulus response to other organism defense response response to external stimulus defense response to Gram-negative bacterium response to biotic stimulus defense response to bacterium defense response to other organism response to stress response to bacterium response to external biotic stimulus humoral immune response immune response biological process involved in interspecies interaction between organisms response to stimulus response to other organism defense response response to external stimulus defense response to Gram-negative bacterium response to biotic stimulus defense response to bacterium defense response to other organism response to stress response to bacterium response to external biotic stimulus humoral immune response immune response antibacterial humoral response defense response to symbiont antimicrobial humoral response immune system process hemolysis in another organism cytolysis in another organism cellular process disruption of cell in another organism disruption of anatomical structure in another organism cytolysis killing of cells of another organism cell killing cellular component organization cellular component biogenesis cellular component assembly protein-containing complex organization protein complex oligomerization protein-containing complex assembly protein homooligomerization cellular component organization or biogenesis carbohydrate derivative biosynthetic process glycoprotein biosynthetic process carbohydrate derivative metabolic process primary metabolic process glycoprotein metabolic process protein glycosylation macromolecule biosynthetic process biosynthetic process glycosylation macromolecule modification macromolecule glycosylation protein O-linked glycosylation metabolic process protein metabolic process macromolecule metabolic process protein modification process positive regulation of erythrocyte aggregation regulation of biological process erythrocyte aggregation regulation of cellular process regulation of erythrocyte aggregation regulation of homotypic cell-cell adhesion positive regulation of cell adhesion regulation of cell adhesion biological regulation homotypic cell-cell adhesion positive regulation of biological process positive regulation of cell-cell adhesion cell adhesion cell-cell adhesion positive regulation of homotypic cell-cell adhesion regulation of cell-cell adhesion positive regulation of cellular process disruption of cellular anatomical structure in another organism disruption of plasma membrane integrity in another organism defense response to Gram-positive bacterium	membrane-bounded organelle intracellular organelle cellular anatomical structure intracellular anatomical structure Golgi apparatus organelle cytoplasm intracellular membrane-bounded organelle endomembrane system extracellular region extracellular space

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B	IPR035992	Ricin B-like lectins	Homologous Superfamily
A, B	IPR028988	Hemolytic lectin CEL-III, C-terminal domain superfamily	Homologous Superfamily
A, B	IPR000772	Ricin B, lectin domain	Domain

Protein Modification Annotation

Modified Residue(s)
Chain	Residue(s)	Description
A, B	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.