5GP0

Crystal structure of geraniol-NUDX1 complex

External Resource: Annotation

Domain Annotation: ECOD Classification
Domain Annotation: CATH
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 E]	PF00293	e5gp0E1	A: a+b two layers	X: beta-Grasp	H: Nudix (From Topology)	T: Nudix	F: PF00293	ECOD (1.6)
B [auth F]	PF00293	e5gp0F1	A: a+b two layers	X: beta-Grasp	H: Nudix (From Topology)	T: Nudix	F: PF00293	ECOD (1.6)
C [auth I]	PF00293	e5gp0I1	A: a+b two layers	X: beta-Grasp	H: Nudix (From Topology)	T: Nudix	F: PF00293	ECOD (1.6)
D [auth A]	PF00293	e5gp0A1	A: a+b two layers	X: beta-Grasp	H: Nudix (From Topology)	T: Nudix	F: PF00293	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A [auth E]	3.90.79.10	Alpha Beta	Alpha-Beta Complex	Nucleoside Triphosphate Pyrophosphohydrolase	Nucleoside Triphosphate Pyrophosphohydrolase	CATH (4.3.0)
B [auth F]	3.90.79.10	Alpha Beta	Alpha-Beta Complex	Nucleoside Triphosphate Pyrophosphohydrolase	Nucleoside Triphosphate Pyrophosphohydrolase	CATH (4.3.0)
C [auth I]	3.90.79.10	Alpha Beta	Alpha-Beta Complex	Nucleoside Triphosphate Pyrophosphohydrolase	Nucleoside Triphosphate Pyrophosphohydrolase	CATH (4.3.0)
D [auth A]	3.90.79.10	Alpha Beta	Alpha-Beta Complex	Nucleoside Triphosphate Pyrophosphohydrolase	Nucleoside Triphosphate Pyrophosphohydrolase	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A [auth E], B [auth F], C [auth I], D [auth A]	PF00293	NUDIX domain (NUDIX)	NUDIX domain	-	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A [auth E], B [auth F], C [auth I], D [auth A]	Nudix hydrolase 1	pyrophosphatase activity 8-oxo-7,8-dihydrodeoxyguanosine triphosphate pyrophosphatase activity nucleoside triphosphate diphosphatase activity hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides hydrolase activity hydrolase activity, acting on acid anhydrides catalytic activity dihydroneopterin triphosphate pyrophosphohydrolase activity NAD+ diphosphatase activity dinucleotide phosphatase activity NADH pyrophosphatase activity 8-oxo-7,8-dihydroguanosine triphosphate pyrophosphatase activity cation binding ion binding pyrophosphatase activity 8-oxo-7,8-dihydrodeoxyguanosine triphosphate pyrophosphatase activity nucleoside triphosphate diphosphatase activity hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides hydrolase activity hydrolase activity, acting on acid anhydrides catalytic activity dihydroneopterin triphosphate pyrophosphohydrolase activity NAD+ diphosphatase activity dinucleotide phosphatase activity NADH pyrophosphatase activity 8-oxo-7,8-dihydroguanosine triphosphate pyrophosphatase activity cation binding ion binding binding metal ion binding small molecule binding	cellular response to stimulus cellular response to stress response to stimulus DNA damage response response to stress cellular process	intracellular anatomical structure cytoplasm cellular anatomical entity cytosol

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A [auth E], B [auth F], C [auth I], D [auth A]	IPR000086	NUDIX hydrolase domain	Domain
A [auth E], B [auth F], C [auth I], D [auth A]	IPR015797	NUDIX hydrolase-like domain superfamily	Homologous Superfamily
A [auth E], B [auth F], C [auth I], D [auth A]	IPR020084	NUDIX hydrolase, conserved site	Conserved Site
A [auth E], B [auth F], C [auth I], D [auth A]	IPR020476	NUDIX hydrolase	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 R01GM133198.