3W68

Crystal structure of mouse alpha-tocopherol transfer protein in complex with alpha-tocopherol and phosphatidylinositol-(4,5)-bisphosphate

External Resource: Annotation

Domain Annotation: SCOP/SCOPe 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	d3w68b1	All alpha proteins	RuvA C-terminal domain-like	CRAL/TRIO N-terminal domain	automated matches	automated matches	mouse (Mus musculus ) [TaxId: 10090 ],	SCOPe (2.08)
B	d3w68b2	Alpha and beta proteins (a/b)	SpoIIaa-like	CRAL/TRIO domain	CRAL/TRIO domain	automated matches	mouse (Mus musculus ) [TaxId: 10090 ],	SCOPe (2.08)
C	d3w68c1	All alpha proteins	RuvA C-terminal domain-like	CRAL/TRIO N-terminal domain	automated matches	automated matches	mouse (Mus musculus ) [TaxId: 10090 ],	SCOPe (2.08)
C	d3w68c2	Alpha and beta proteins (a/b)	SpoIIaa-like	CRAL/TRIO domain	CRAL/TRIO domain	automated matches	mouse (Mus musculus ) [TaxId: 10090 ],	SCOPe (2.08)
D	d3w68d1	All alpha proteins	RuvA C-terminal domain-like	CRAL/TRIO N-terminal domain	automated matches	automated matches	mouse (Mus musculus ) [TaxId: 10090 ],	SCOPe (2.08)
D	d3w68d2	Alpha and beta proteins (a/b)	SpoIIaa-like	CRAL/TRIO domain	CRAL/TRIO domain	automated matches	mouse (Mus musculus ) [TaxId: 10090 ],	SCOPe (2.08)
A	d3w68a1	All alpha proteins	RuvA C-terminal domain-like	CRAL/TRIO N-terminal domain	automated matches	automated matches	mouse (Mus musculus ) [TaxId: 10090 ],	SCOPe (2.08)
A	d3w68a2	Alpha and beta proteins (a/b)	SpoIIaa-like	CRAL/TRIO domain	CRAL/TRIO domain	automated matches	mouse (Mus musculus ) [TaxId: 10090 ],	SCOPe (2.08)

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
B	CRAL_TRIO_N	e3w68B3	A: alpha arrays	X: RuvA-C	H: RuvA-C, UBA, CRAL/TRIO-N, HBS1 (From Topology)	T: RuvA-C, UBA, CRAL/TRIO-N, HBS1	F: CRAL_TRIO_N	ECOD (1.6)
B	CRAL_TRIO	e3w68B4	A: a/b three-layered sandwiches	X: SpoIIaa-like (From Topology)	H: SpoIIaa-like (From Topology)	T: SpoIIaa-like	F: CRAL_TRIO	ECOD (1.6)
C	CRAL_TRIO_N	e3w68C1	A: alpha arrays	X: RuvA-C	H: RuvA-C, UBA, CRAL/TRIO-N, HBS1 (From Topology)	T: RuvA-C, UBA, CRAL/TRIO-N, HBS1	F: CRAL_TRIO_N	ECOD (1.6)
C	CRAL_TRIO	e3w68C4	A: a/b three-layered sandwiches	X: SpoIIaa-like (From Topology)	H: SpoIIaa-like (From Topology)	T: SpoIIaa-like	F: CRAL_TRIO	ECOD (1.6)
D	CRAL_TRIO_N	e3w68D3	A: alpha arrays	X: RuvA-C	H: RuvA-C, UBA, CRAL/TRIO-N, HBS1 (From Topology)	T: RuvA-C, UBA, CRAL/TRIO-N, HBS1	F: CRAL_TRIO_N	ECOD (1.6)
D	CRAL_TRIO	e3w68D4	A: a/b three-layered sandwiches	X: SpoIIaa-like (From Topology)	H: SpoIIaa-like (From Topology)	T: SpoIIaa-like	F: CRAL_TRIO	ECOD (1.6)
A	CRAL_TRIO_N	e3w68A3	A: alpha arrays	X: RuvA-C	H: RuvA-C, UBA, CRAL/TRIO-N, HBS1 (From Topology)	T: RuvA-C, UBA, CRAL/TRIO-N, HBS1	F: CRAL_TRIO_N	ECOD (1.6)
A	CRAL_TRIO	e3w68A4	A: a/b three-layered sandwiches	X: SpoIIaa-like (From Topology)	H: SpoIIaa-like (From Topology)	T: SpoIIaa-like	F: CRAL_TRIO	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
B	1.10.8.20	Mainly Alpha	Orthogonal Bundle	Helicase, Ruva Protein	domain 3	CATH (4.3.0)
B	1.20.5.1200	Mainly Alpha	Up-down Bundle	Single alpha-helices involved in coiled-coils or other helix-helix interfaces	Alpha-tocopherol transfer	CATH (4.3.0)
B	3.40.525.10	Alpha Beta	3-Layer(aba) Sandwich	Phosphatidylinositol Transfer Protein Sec14p	CRAL-TRIO lipid binding domain	CATH (4.3.0)
C	1.10.8.20	Mainly Alpha	Orthogonal Bundle	Helicase, Ruva Protein	domain 3	CATH (4.3.0)
C	1.20.5.1200	Mainly Alpha	Up-down Bundle	Single alpha-helices involved in coiled-coils or other helix-helix interfaces	Alpha-tocopherol transfer	CATH (4.3.0)
C	3.40.525.10	Alpha Beta	3-Layer(aba) Sandwich	Phosphatidylinositol Transfer Protein Sec14p	CRAL-TRIO lipid binding domain	CATH (4.3.0)
D	1.10.8.20	Mainly Alpha	Orthogonal Bundle	Helicase, Ruva Protein	domain 3	CATH (4.3.0)
D	1.20.5.1200	Mainly Alpha	Up-down Bundle	Single alpha-helices involved in coiled-coils or other helix-helix interfaces	Alpha-tocopherol transfer	CATH (4.3.0)
D	3.40.525.10	Alpha Beta	3-Layer(aba) Sandwich	Phosphatidylinositol Transfer Protein Sec14p	CRAL-TRIO lipid binding domain	CATH (4.3.0)
A	1.10.8.20	Mainly Alpha	Orthogonal Bundle	Helicase, Ruva Protein	domain 3	CATH (4.3.0)
A	1.20.5.1200	Mainly Alpha	Up-down Bundle	Single alpha-helices involved in coiled-coils or other helix-helix interfaces	Alpha-tocopherol transfer	CATH (4.3.0)
A	3.40.525.10	Alpha Beta	3-Layer(aba) Sandwich	Phosphatidylinositol Transfer Protein Sec14p	CRAL-TRIO lipid binding domain	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B, C, D	PF00650	CRAL/TRIO domain (CRAL_TRIO)	CRAL/TRIO domain	-	Domain
A, B, C, D	PF03765	CRAL/TRIO, N-terminal domain (CRAL_TRIO_N)	CRAL/TRIO, N-terminal domain	This all-alpha domain is found to the N-terminus of Pfam:PF00650.	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B, C, D	Alpha-tocopherol transfer protein	binding ion binding phosphatidylinositol-4,5-bisphosphate binding anion binding phosphatidylinositol bisphosphate binding phospholipid binding lipid binding phosphatidylinositol phosphate binding phosphatidylinositol binding small molecule binding phosphatidylinositol-3,4-bisphosphate binding vitamin binding organic cyclic compound binding heterocyclic compound binding binding ion binding phosphatidylinositol-4,5-bisphosphate binding anion binding phosphatidylinositol bisphosphate binding phospholipid binding lipid binding phosphatidylinositol phosphate binding phosphatidylinositol binding small molecule binding phosphatidylinositol-3,4-bisphosphate binding vitamin binding organic cyclic compound binding heterocyclic compound binding vitamin E binding lipid transporter activity lipid transfer activity transporter activity	response to stimulus response to pH response to abiotic stimulus localization transport vitamin transport establishment of localization vitamin E metabolic process fat-soluble vitamin metabolic process organic hydroxy compound metabolic process metabolic process cellular process small molecule metabolic process vitamin metabolic process response to stimulus response to pH response to abiotic stimulus localization transport vitamin transport establishment of localization vitamin E metabolic process fat-soluble vitamin metabolic process organic hydroxy compound metabolic process metabolic process cellular process small molecule metabolic process vitamin metabolic process developmental process placenta development animal organ development anatomical structure development membrane organization intermembrane lipid transfer lipid localization lipid transport cellular component organization macromolecule localization cellular component organization or biogenesis multicellular organismal process regulation of biological process biological regulation positive regulation of biological process positive regulation of amyloid-beta clearance positive regulation of multicellular organismal process regulation of multicellular organismal process amyloid-beta clearance regulation of amyloid-beta clearance chordate embryonic development embryo development in utero embryonic development multicellular organism development embryonic placenta development embryo development ending in birth or egg hatching embryonic organ development regulation of cellular process regulation of developmental process cellular developmental process regulation of establishment of blood-brain barrier negative regulation of biological process cell development regulation of cell differentiation regulation of cell development cell differentiation negative regulation of cellular process negative regulation of cell differentiation system development establishment of blood-brain barrier negative regulation of developmental process nervous system development negative regulation of cell development central nervous system development negative regulation of establishment of blood-brain barrier response to chemical response to toxic substance regulation of epithelial cell apoptotic process negative regulation of programmed cell death regulation of apoptotic process regulation of programmed cell death cell death epithelial cell apoptotic process negative regulation of apoptotic process negative regulation of epithelial cell apoptotic process apoptotic process programmed cell death homeostatic process intracellular pH reduction regulation of intracellular pH cellular homeostasis chemical homeostasis intracellular monoatomic cation homeostasis regulation of pH monoatomic ion homeostasis intracellular chemical homeostasis regulation of biological quality monoatomic cation homeostasis regulation of cellular pH intracellular monoatomic ion homeostasis	membrane-bounded organelle intracellular anatomical structure endosome intracellular vesicle intracellular membrane-bounded organelle endomembrane system intracellular organelle cellular anatomical structure cytoplasmic vesicle organelle late endosome cytoplasm vesicle

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B, C, D	IPR001251	CRAL-TRIO lipid binding domain	Domain
A, B, C, D	IPR036865	CRAL-TRIO lipid binding domain superfamily	Homologous Superfamily
A, B, C, D	IPR011074	CRAL/TRIO, N-terminal domain	Domain
A, B, C, D	IPR036273	CRAL/TRIO, N-terminal domain superfamily	Homologous Superfamily

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.