4ZR1

Hydroxylase domain of scs7p

External Resource: Annotation

Domain Annotation: SCOP2 Classification
Domain Annotation: ECOD Classification
Protein Family Annotation
Gene Ontology: Gene Product Annotation
InterPro: Protein Family Classification
Membrane Protein Annotation: OPM
Membrane Protein Annotation: PDBTM
Membrane Protein Annotation: MemProtMD

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2B Superfamily	Fatty acid hydroxylase-like	8090348	3002435	SCOP2B (2022-06-29)
B	SCOP2 Family	Fatty acid hydroxylase-like	8045369	4004440	SCOP2 (2022-06-29)
B	SCOP2 Superfamily	Fatty acid hydroxylase-like	8090348	3002435	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)
A	FA_hydroxylase	e4zr1A1	A: alpha complex topology	X: Integral membrane Acyl-CoA desaturase (From Topology)	H: Integral membrane Acyl-CoA desaturase (From Topology)	T: Integral membrane Acyl-CoA desaturase	F: FA_hydroxylase	ECOD (1.6)
B	FA_hydroxylase	e4zr1B1	A: alpha complex topology	X: Integral membrane Acyl-CoA desaturase (From Topology)	H: Integral membrane Acyl-CoA desaturase (From Topology)	T: Integral membrane Acyl-CoA desaturase	F: FA_hydroxylase	ECOD (1.6)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B	PF04116	Fatty acid hydroxylase (FA_hydroxylase)	Fatty acid hydroxylase	-	Family

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B	Ceramide very long chain fatty acid hydroxylase SCS7	oxidoreductase activity sphingosine hydroxylase activity catalytic activity dihydroceramide fatty acyl 2-hydroxylase activity oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, another compound as one donor, and incorporation of one atom of oxygen monooxygenase activity oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen fatty acid 2-hydroxylase activity binding organic cyclic compound binding tetrapyrrole binding heme binding cation binding transition metal ion binding oxidoreductase activity sphingosine hydroxylase activity catalytic activity dihydroceramide fatty acyl 2-hydroxylase activity oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, another compound as one donor, and incorporation of one atom of oxygen monooxygenase activity oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen fatty acid 2-hydroxylase activity binding organic cyclic compound binding tetrapyrrole binding heme binding cation binding transition metal ion binding iron ion binding ion binding metal ion binding small molecule binding zinc ion binding	fatty acid metabolic process oxoacid metabolic process carboxylic acid metabolic process primary metabolic process metabolic process cellular process small molecule metabolic process monocarboxylic acid metabolic process organic acid metabolic process lipid metabolic process monocarboxylic acid biosynthetic process small molecule biosynthetic process lipid biosynthetic process organic acid biosynthetic process fatty acid metabolic process oxoacid metabolic process carboxylic acid metabolic process primary metabolic process metabolic process cellular process small molecule metabolic process monocarboxylic acid metabolic process organic acid metabolic process lipid metabolic process monocarboxylic acid biosynthetic process small molecule biosynthetic process lipid biosynthetic process organic acid biosynthetic process fatty acid biosynthetic process carboxylic acid biosynthetic process biosynthetic process ceramide metabolic process membrane lipid metabolic process sphingolipid biosynthetic process amide biosynthetic process sphingolipid metabolic process ceramide biosynthetic process amide metabolic process membrane lipid biosynthetic process very long-chain fatty acid metabolic process inositol phosphoceramide metabolic process phospholipid metabolic process organophosphate metabolic process phosphate-containing compound metabolic process phosphorus metabolic process	cellular anatomical structure membrane membrane-bounded organelle intracellular organelle intracellular anatomical structure organelle endoplasmic reticulum cytoplasm intracellular membrane-bounded organelle endomembrane system organelle subcompartment endoplasmic reticulum subcompartment nuclear outer membrane-endoplasmic reticulum membrane network organelle membrane cellular anatomical structure membrane membrane-bounded organelle intracellular organelle intracellular anatomical structure organelle endoplasmic reticulum cytoplasm intracellular membrane-bounded organelle endomembrane system organelle subcompartment endoplasmic reticulum subcompartment nuclear outer membrane-endoplasmic reticulum membrane network organelle membrane endoplasmic reticulum membrane

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B	IPR036400	Cytochrome b5-like heme/steroid binding domain superfamily	Homologous Superfamily
A, B	IPR018506	Cytochrome b5, heme-binding site	Binding Site
A, B	IPR006694	Fatty acid hydroxylase	Domain
A, B	IPR014430	Sterol desaturase Scs7	Family
A, B	IPR001199	Cytochrome b5-like heme/steroid binding domain	Domain

Membrane Protein Annotation: OPM OPM Database Homepage

Chains	External Link	Type	Class	Superfamily	Family
A, B	OPM	Transmembrane	Alpha-helical polytopic	Fatty acid desaturase/hydroxylase	Fatty acid hydroxylase

Membrane Protein Annotation: PDBTM PDBTM Database Homepage

Chains	External Link	Comment
A, B	PDBTM	Annotated as membrane protein by PDBTM

Membrane Protein Annotation: MemProtMD MemProtMD Database Homepage

Chains	External Link	Comment
A, B	MemProtMD	Annotated as membrane protein by MemProtMD

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.