6ZIC

CRYSTAL STRUCTURE OF RAT PEROXISOMAL MULTIFUNCTIONAL ENZYME TYPE-1 (RPMFE1) COMPLEXED WITH 3S-HYDROXYBUTANOYL-COA AND NADH

External Resource: Annotation

Domain Annotation: ECOD Classification
Protein Family Annotation
Gene Ontology: Gene Product Annotation
InterPro: Protein Family Classification

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
A [auth AAA]	3HCDH	e6zicAAA4	A: alpha arrays	X: 6-phosphogluconate dehydrogenase C-terminal domain-like (From Topology)	H: 6-phosphogluconate dehydrogenase C-terminal domain-like (From Topology)	T: 6-phosphogluconate dehydrogenase C-terminal domain-like	F: 3HCDH	ECOD (1.6)
A [auth AAA]	3HCDH_N	e6zicAAA2	A: a/b three-layered sandwiches	X: Rossmann-like	H: Rossmann-related	T: NAD(P)-binding Rossmann-fold domains	F: 3HCDH_N	ECOD (1.6)
A [auth AAA]	ECH_1	e6zicAAA3	A: a/b three-layered sandwiches	X: ClpP/crotonase (From Topology)	H: ClpP/crotonase (From Topology)	T: ClpP/crotonase	F: ECH_1	ECOD (1.6)
B [auth BBB]	3HCDH	e6zicBBB3	A: alpha arrays	X: 6-phosphogluconate dehydrogenase C-terminal domain-like (From Topology)	H: 6-phosphogluconate dehydrogenase C-terminal domain-like (From Topology)	T: 6-phosphogluconate dehydrogenase C-terminal domain-like	F: 3HCDH	ECOD (1.6)
B [auth BBB]	3HCDH_N	e6zicBBB4	A: a/b three-layered sandwiches	X: Rossmann-like	H: Rossmann-related	T: NAD(P)-binding Rossmann-fold domains	F: 3HCDH_N	ECOD (1.6)
B [auth BBB]	ECH_1	e6zicBBB1	A: a/b three-layered sandwiches	X: ClpP/crotonase (From Topology)	H: ClpP/crotonase (From Topology)	T: ClpP/crotonase	F: ECH_1	ECOD (1.6)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A [auth AAA], B [auth BBB]	PF02737	3-hydroxyacyl-CoA dehydrogenase, NAD binding domain (3HCDH_N)	3-hydroxyacyl-CoA dehydrogenase, NAD binding domain	This family also includes lambda crystallin.	Domain
A [auth AAA], B [auth BBB]	PF00725	3-hydroxyacyl-CoA dehydrogenase, C-terminal domain (3HCDH)	3-hydroxyacyl-CoA dehydrogenase, C-terminal domain	This family also includes lambda crystallin. Some proteins include two copies of this domain.	Domain
A [auth AAA], B [auth BBB]	PF00378	Enoyl-CoA hydratase/isomerase (ECH_1)	Enoyl-CoA hydratase/isomerase	This family contains a diverse set of enzymes including: enoyl-CoA hydratase, napthoate synthase, carnitate racemase, 3-hydroxybutyryl-CoA dehydratase and dodecanoyl-CoA delta-isomerase.	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A [auth AAA], B [auth BBB]	Peroxisomal bifunctional enzyme	isomerase activity intramolecular oxidoreductase activity, transposing C=C bonds intramolecular oxidoreductase activity catalytic activity NAD+ binding NAD binding binding nucleotide binding nucleoside phosphate binding ion binding purine nucleotide binding organic cyclic compound binding anion binding adenyl nucleotide binding isomerase activity intramolecular oxidoreductase activity, transposing C=C bonds intramolecular oxidoreductase activity catalytic activity NAD+ binding NAD binding binding nucleotide binding nucleoside phosphate binding ion binding purine nucleotide binding organic cyclic compound binding anion binding adenyl nucleotide binding heterocyclic compound binding small molecule binding oxidoreductase activity oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor oxidoreductase activity, acting on CH-OH group of donors 3-hydroxyacyl-CoA dehydrogenase activity delta(3)-delta(2)-enoyl-CoA isomerase activity enoyl-CoA hydratase activity hydro-lyase activity lyase activity carbon-oxygen lyase activity long-chain-3-hydroxyacyl-CoA dehydrogenase activity protein binding enzyme binding	fatty acid metabolic process lipid catabolic process catabolic process oxoacid metabolic process carboxylic acid metabolic process primary metabolic process lipid modification organic acid catabolic process organic acid metabolic process fatty acid catabolic process cellular catabolic process monocarboxylic acid catabolic process fatty acid oxidation carboxylic acid catabolic process fatty acid beta-oxidation fatty acid metabolic process lipid catabolic process catabolic process oxoacid metabolic process carboxylic acid metabolic process primary metabolic process lipid modification organic acid catabolic process organic acid metabolic process fatty acid catabolic process cellular catabolic process monocarboxylic acid catabolic process fatty acid oxidation carboxylic acid catabolic process fatty acid beta-oxidation metabolic process cellular process small molecule metabolic process monocarboxylic acid metabolic process lipid oxidation small molecule catabolic process lipid metabolic process	membrane-bounded organelle intracellular organelle cellular anatomical structure intracellular anatomical structure organelle peroxisome microbody cytoplasm intracellular membrane-bounded organelle cytosol

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A [auth AAA], B [auth BBB]	IPR001753	Enoyl-CoA hydratase/isomerase	Family
A [auth AAA], B [auth BBB]	IPR029045	ClpP/crotonase-like domain superfamily	Homologous Superfamily
A [auth AAA], B [auth BBB]	IPR018376	Enoyl-CoA hydratase/isomerase, conserved site	Conserved Site
A [auth AAA], B [auth BBB]	IPR008927	6-phosphogluconate dehydrogenase-like, C-terminal domain superfamily	Homologous Superfamily
A [auth AAA], B [auth BBB]	IPR006108	3-hydroxyacyl-CoA dehydrogenase, C-terminal	Domain
A [auth AAA], B [auth BBB]	IPR036291	NAD(P)-binding domain superfamily	Homologous Superfamily
A [auth AAA], B [auth BBB]	IPR006180	3-hydroxyacyl-CoA dehydrogenase, conserved site	Conserved Site
A [auth AAA], B [auth BBB]	IPR006176	3-hydroxyacyl-CoA dehydrogenase, NAD binding	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.