1BWO

THE CRYSTAL STRUCTURE OF WHEAT NON-SPECIFIC TRANSFER PROTEIN COMPLEXED WITH TWO MOLECULES OF PHOSPHOLIPID AT 2.1 A RESOLUTION

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)
A	d1bwoa_	All alpha proteins	Bifunctional inhibitor/lipid-transfer protein/seed storage 2S albumin	Bifunctional inhibitor/lipid-transfer protein/seed storage 2S albumin	Plant lipid-transfer and hydrophobic proteins	Plant non-specific lipid-transfer protein (ns-LTP, ns-LTP1)	(Triticum aestivum ) [TaxId: 4565 ],	SCOPe (2.08)
B	d1bwob_	All alpha proteins	Bifunctional inhibitor/lipid-transfer protein/seed storage 2S albumin	Bifunctional inhibitor/lipid-transfer protein/seed storage 2S albumin	Plant lipid-transfer and hydrophobic proteins	Plant non-specific lipid-transfer protein (ns-LTP, ns-LTP1)	(Triticum aestivum ) [TaxId: 4565 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2 Family	Plant lipid-transfer and hydrophobic proteins	8025233	4000994	SCOP2 (2022-06-29)
A	SCOP2 Superfamily	Bifunctional inhibitor/lipid-transfer protein/seed storage 2S albumin	8037612	3000401	SCOP2 (2022-06-29)
B	SCOP2B Superfamily	Bifunctional inhibitor/lipid-transfer protein/seed storage 2S albumin	8037612	3000401	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	Tryp_alpha_amyl	e1bwoA1	A: alpha superhelices	X: Bifunctional inhibitor/lipid-transfer protein/seed storage 2S albumin-like	H: Bifunctional inhibitor/lipid-transfer protein/seed storage 2S albumin/Protein HNS-dependent expression A HdeA	T: Bifunctional inhibitor/lipid-transfer protein/seed storage 2S albumin	F: Tryp_alpha_amyl	ECOD (1.6)
B	Tryp_alpha_amyl	e1bwoB1	A: alpha superhelices	X: Bifunctional inhibitor/lipid-transfer protein/seed storage 2S albumin-like	H: Bifunctional inhibitor/lipid-transfer protein/seed storage 2S albumin/Protein HNS-dependent expression A HdeA	T: Bifunctional inhibitor/lipid-transfer protein/seed storage 2S albumin	F: Tryp_alpha_amyl	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	1.10.110.10	Mainly Alpha	Orthogonal Bundle	Hydrophobic Seed Protein	Plant lipid-transfer and hydrophobic proteins	CATH (4.3.0)
B	1.10.110.10	Mainly Alpha	Orthogonal Bundle	Hydrophobic Seed Protein	Plant lipid-transfer and hydrophobic proteins	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B	PF00234	Protease inhibitor/seed storage/LTP family (Tryp_alpha_amyl)	Protease inhibitor/seed storage/LTP family	This family is composed of trypsin-alpha amylase inhibitors, seed storage proteins and lipid transfer proteins from plants.	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B	NONSPECIFIC LIPID-TRANSFER PROTEIN	binding lipid binding	localization transport macromolecule localization lipid localization lipid transport establishment of localization	-

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B	IPR000528	Plant non-specific lipid-transfer protein/Par allergen	Family
A, B	IPR036312	Bifunctional inhibitor/plant lipid transfer protein/seed storage helical domain superfamily	Homologous Superfamily
A, B	IPR016140	Bifunctional inhibitor/plant lipid transfer protein/seed storage helical 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.