1OUW

Crystal structure of Calystegia sepium agglutinin

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

Domain Annotation: SCOP/SCOPe Classification SCOP-e Database Homepage

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
B	d1ouwb_	All beta proteins	beta-Prism I	Mannose-binding lectins	Mannose-binding lectins	Calystegia sepium agglutinin	(Calystegia sepium ) [TaxId: 47519 ],	SCOPe (2.08)
D	d1ouwd_	All beta proteins	beta-Prism I	Mannose-binding lectins	Mannose-binding lectins	Calystegia sepium agglutinin	(Calystegia sepium ) [TaxId: 47519 ],	SCOPe (2.08)
A	d1ouwa_	All beta proteins	beta-Prism I	Mannose-binding lectins	Mannose-binding lectins	Calystegia sepium agglutinin	(Calystegia sepium ) [TaxId: 47519 ],	SCOPe (2.08)
C	d1ouwc_	All beta proteins	beta-Prism I	Mannose-binding lectins	Mannose-binding lectins	Calystegia sepium agglutinin	(Calystegia sepium ) [TaxId: 47519 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
B	SCOP2B Superfamily	Mannose-binding lectins	8037808	3001715	SCOP2B (2022-06-29)
D	SCOP2B Superfamily	Mannose-binding lectins	8037808	3001715	SCOP2B (2022-06-29)
A	SCOP2B Superfamily	Mannose-binding lectins	8037808	3001715	SCOP2B (2022-06-29)
C	SCOP2 Family	Mannose-binding lectins	8025429	4002758	SCOP2 (2022-06-29)
C	SCOP2 Superfamily	Mannose-binding lectins	8037808	3001715	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)
B	Jacalin	e1ouwB1	A: beta duplicates or obligate multimers	X: beta-Prism I (From Topology)	H: beta-Prism I (From Topology)	T: beta-Prism I	F: Jacalin	ECOD (1.6)
D	Jacalin	e1ouwD1	A: beta duplicates or obligate multimers	X: beta-Prism I (From Topology)	H: beta-Prism I (From Topology)	T: beta-Prism I	F: Jacalin	ECOD (1.6)
A	Jacalin	e1ouwA1	A: beta duplicates or obligate multimers	X: beta-Prism I (From Topology)	H: beta-Prism I (From Topology)	T: beta-Prism I	F: Jacalin	ECOD (1.6)
C	Jacalin	e1ouwC1	A: beta duplicates or obligate multimers	X: beta-Prism I (From Topology)	H: beta-Prism I (From Topology)	T: beta-Prism I	F: Jacalin	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
B	2.100.10.30	Mainly Beta	Aligned Prism	Vitelline Membrane Outer Layer Protein I, subunit A	Jacalin-like lectin domain	CATH (4.3.0)
D	2.100.10.30	Mainly Beta	Aligned Prism	Vitelline Membrane Outer Layer Protein I, subunit A	Jacalin-like lectin domain	CATH (4.3.0)
A	2.100.10.30	Mainly Beta	Aligned Prism	Vitelline Membrane Outer Layer Protein I, subunit A	Jacalin-like lectin domain	CATH (4.3.0)
C	2.100.10.30	Mainly Beta	Aligned Prism	Vitelline Membrane Outer Layer Protein I, subunit A	Jacalin-like lectin domain	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B, C, D	PF01419	Jacalin-like lectin domain (Jacalin)	Jacalin-like lectin domain	-	Repeat

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B, C, D	lectin	binding carbohydrate binding D-mannose binding monosaccharide binding small molecule binding cell adhesion molecule binding protein binding identical protein binding protein homodimerization activity protein dimerization activity D-glucose binding	heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules cell adhesion cell-cell adhesion cellular process cell-cell adhesion via plasma-membrane adhesion molecules positive regulation of organelle organization regulation of cellular component organization regulation of cellular process positive regulation of cellular component organization positive regulation of biological process regulation of mitotic nuclear division positive regulation of mitotic nuclear division mitotic cell cycle cellular component organization heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules cell adhesion cell-cell adhesion cellular process cell-cell adhesion via plasma-membrane adhesion molecules positive regulation of organelle organization regulation of cellular component organization regulation of cellular process positive regulation of cellular component organization positive regulation of biological process regulation of mitotic nuclear division positive regulation of mitotic nuclear division mitotic cell cycle cellular component organization regulation of mitotic cell cycle positive regulation of cell cycle process cellular component organization or biogenesis cell cycle regulation of cell cycle positive regulation of cellular process cell cycle process regulation of biological process mitotic nuclear division regulation of cell cycle process organelle fission biological regulation positive regulation of nuclear division regulation of organelle organization positive regulation of cell cycle organelle organization nuclear division mitotic cell cycle process regulation of nuclear division	cellular anatomical structure intracellular anatomical structure cytoplasm

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B, C, D	IPR036404	Jacalin-like lectin domain superfamily	Homologous Superfamily
A, B, C, D	IPR033734	Jacalin-like lectin domain, plant	Domain
A, B, C, D	IPR001229	Jacalin-like lectin domain	Domain

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.