1ZI7

Structure of truncated yeast oxysterol binding protein Osh4

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
Membrane Protein Annotation: OPM

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

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
A	d1zi7a1	Alpha and beta proteins (a+b)	Oxysterol-binding protein-like	Oxysterol-binding protein-like	Oxysterol-binding protein	Oxysterol-binding protein homolog 4, KES1	baker's yeast (Saccharomyces cerevisiae ) [TaxId: 4932 ],	SCOPe (2.08)
B	d1zi7b_	Alpha and beta proteins (a+b)	Oxysterol-binding protein-like	Oxysterol-binding protein-like	Oxysterol-binding protein	Oxysterol-binding protein homolog 4, KES1	baker's yeast (Saccharomyces cerevisiae ) [TaxId: 4932 ],	SCOPe (2.08)
C	d1zi7c_	Alpha and beta proteins (a+b)	Oxysterol-binding protein-like	Oxysterol-binding protein-like	Oxysterol-binding protein	Oxysterol-binding protein homolog 4, KES1	baker's yeast (Saccharomyces cerevisiae ) [TaxId: 4932 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2B Superfamily	Oxysterol-binding protein-like	8035707	3000239	SCOP2B (2022-06-29)
B	SCOP2B Superfamily	Oxysterol-binding protein-like	8035707	3000239	SCOP2B (2022-06-29)
C	SCOP2B Superfamily	Oxysterol-binding protein-like	8035707	3000239	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	Oxysterol_BP	e1zi7A1	A: beta barrels	X: Oxysterol-binding protein (From Topology)	H: Oxysterol-binding protein (From Topology)	T: Oxysterol-binding protein	F: Oxysterol_BP	ECOD (1.6)
B	Oxysterol_BP	e1zi7B1	A: beta barrels	X: Oxysterol-binding protein (From Topology)	H: Oxysterol-binding protein (From Topology)	T: Oxysterol-binding protein	F: Oxysterol_BP	ECOD (1.6)
C	Oxysterol_BP	e1zi7C1	A: beta barrels	X: Oxysterol-binding protein (From Topology)	H: Oxysterol-binding protein (From Topology)	T: Oxysterol-binding protein	F: Oxysterol_BP	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	6.10.140.1150	Special	Helix non-globular	Helix Hairpins		CATH (4.3.0)
B	6.10.140.1150	Special	Helix non-globular	Helix Hairpins		CATH (4.3.0)
C	6.10.140.1150	Special	Helix non-globular	Helix Hairpins		CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B, C	PF01237	Oxysterol-binding protein (Oxysterol_BP)	Oxysterol-binding protein	-	Family

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B, C	KES1 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 sterol binding oxysterol binding organic cyclic compound binding steroid 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 sterol binding oxysterol binding organic cyclic compound binding steroid binding phosphatidic acid binding phosphatidylinositol-4-phosphate binding sterol transfer activity lipid transporter activity lipid transfer activity transporter activity	membrane lipid metabolic process cellular metabolic process cellular lipid metabolic process sphingolipid metabolic process primary metabolic process metabolic process cellular process lipid metabolic process localization post-Golgi vesicle-mediated transport transport establishment of localization Golgi vesicle transport vesicle-mediated transport membrane lipid metabolic process cellular metabolic process cellular lipid metabolic process sphingolipid metabolic process primary metabolic process metabolic process cellular process lipid metabolic process localization post-Golgi vesicle-mediated transport transport establishment of localization Golgi vesicle transport vesicle-mediated transport maintenance of cell polarity establishment or maintenance of cell polarity import into cell endocytosis catabolic process macroautophagy autophagy piecemeal microautophagy of the nucleus microautophagy cellular catabolic process nucleophagy process utilizing autophagic mechanism secretion by cell exocytosis secretion export from cell macromolecule localization lipid localization lipid transport sterol transport organic hydroxy compound transport cellular localization nitrogen compound transport ER to Golgi ceramide transport intracellular lipid transport intracellular transport ceramide transport amide transport establishment of localization in cell	membrane cellular anatomical entity membrane-bounded organelle Golgi membrane intracellular anatomical structure Golgi apparatus intracellular membrane-bounded organelle endomembrane system intracellular organelle bounding membrane of organelle organelle cytoplasm organelle membrane cytosol

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B, C	IPR018494	Oxysterol-binding protein, conserved site	Conserved Site
A, B, C	IPR037239	Oxysterol-binding protein superfamily	Homologous Superfamily
A, B, C	IPR000648	Oxysterol-binding protein	Family

Membrane Protein Annotation: OPM OPM Database Homepage

Chains	External Link	Type	Class	Superfamily	Family
A, B, C	OPM				OSBP-related proteins

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.