1O97

Structure of electron transferring flavoprotein from Methylophilus methylotrophus, recognition loop removed by limited proteolysis

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

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

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
B [auth D]	d1o97d1	Alpha and beta proteins (a/b)	Adenine nucleotide alpha hydrolase-like	Adenine nucleotide alpha hydrolases-like	ETFP subunits	Large, alpha subunit of electron transfer flavoprotein ETFP, N-terminal domain	(Methylophilus methylotrophus ) [TaxId: 17 ],	SCOPe (2.08)
B [auth D]	d1o97d2	Alpha and beta proteins (a/b)	DHS-like NAD/FAD-binding domain	DHS-like NAD/FAD-binding domain	C-terminal domain of the electron transfer flavoprotein alpha subunit	C-terminal domain of the electron transfer flavoprotein alpha subunit	(Methylophilus methylotrophus ) [TaxId: 17 ],	SCOPe (2.08)
A [auth C]	d1o97c_	Alpha and beta proteins (a/b)	Adenine nucleotide alpha hydrolase-like	Adenine nucleotide alpha hydrolases-like	ETFP subunits	Small, beta subunit of electron transfer flavoprotein ETFP	(Methylophilus methylotrophus ) [TaxId: 17 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
B [auth D]	SCOP2B Superfamily	Adenine nucleotide alpha hydrolases-like	8040144	3001593	SCOP2B (2022-06-29)
B [auth D]	SCOP2B Superfamily	DHS-like NAD/FAD-binding domain	8040145	3001728	SCOP2B (2022-06-29)
A [auth C]	SCOP2B Superfamily	Adenine nucleotide alpha hydrolases-like	8040143	3001593	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)
B [auth D]	ETF_alpha	e1o97D1	A: a/b three-layered sandwiches	X: Rossmann-like	H: Rossmann-related	T: DHS-like NAD/FAD-binding domain	F: ETF_alpha	ECOD (1.6)
B [auth D]	ETF	e1o97D2	A: a/b three-layered sandwiches	X: HUP domain-like	H: HUP domains (From Topology)	T: HUP domains	F: ETF	ECOD (1.6)
A [auth C]	ETF	e1o97C1	A: a/b three-layered sandwiches	X: HUP domain-like	H: HUP domains (From Topology)	T: HUP domains	F: ETF	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
B [auth D]	3.40.50.620	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	HUPs	CATH (4.3.0)
B [auth D]	3.40.50.1220	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	TPP-binding domain	CATH (4.3.0)
A [auth C]	3.40.50.620	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	HUPs	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
B [auth D]	PF00766	Electron transfer flavoprotein FAD-binding domain (ETF_alpha)	Electron transfer flavoprotein FAD-binding domain	This domain found at the C-terminus of electron transfer flavoprotein alpha chain and binds to FAD [1]. The fold consists of a five-stranded parallel beta sheet as the core of the domain, flanked by alternating helices. A small part of this domain i ...	This domain found at the C-terminus of electron transfer flavoprotein alpha chain and binds to FAD [1]. The fold consists of a five-stranded parallel beta sheet as the core of the domain, flanked by alternating helices. A small part of this domain is donated by the beta chain [1].	Domain
B [auth D]	PF01012	Electron transfer flavoprotein domain (ETF)	Electron transfer flavoprotein domain	This family includes the homologous domain shared between the alpha and beta subunits of the electron transfer flavoprotein [1].	Domain
A [auth C]	PF01012	Electron transfer flavoprotein domain (ETF)	Electron transfer flavoprotein domain	This family includes the homologous domain shared between the alpha and beta subunits of the electron transfer flavoprotein [1].	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
B [auth D]	ELECTRON TRANSFERRING FLAVOPROTEIN ALPHA-SUBUNIT	electron transfer activity flavin adenine dinucleotide binding binding nucleoside phosphate binding ion binding organic cyclic compound binding anion binding nucleotide binding heterocyclic compound binding small molecule binding	-	-
A [auth C]	ELECTRON TRANSFERRING FLAVOPROTEIN BETA-SUBUNIT	binding nucleoside phosphate binding organic cyclic compound binding nucleotide binding heterocyclic compound binding small molecule binding electron transfer activity	-	-

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
B [auth D]	IPR014730	Electron transfer flavoprotein, alpha/beta-subunit, N-terminal	Domain
B [auth D]	IPR001308	Electron transfer flavoprotein alpha subunit/FixB	Family
B [auth D]	IPR014731	Electron transfer flavoprotein, alpha subunit, C-terminal	Domain
B [auth D]	IPR029035	DHS-like NAD/FAD-binding domain superfamily	Homologous Superfamily
B [auth D]	IPR018206	Electron transfer flavoprotein subunit alpha, conserved site	Conserved Site
B [auth D]	IPR014729	Rossmann-like alpha/beta/alpha sandwich fold	Homologous Superfamily
B [auth D]	IPR033947	Electron transfer flavoprotein, alpha subunit, N-terminal	Domain
A [auth C]	IPR014730	Electron transfer flavoprotein, alpha/beta-subunit, N-terminal	Domain
A [auth C]	IPR033948	Electron transfer flavoprotein, beta subunit, N-terminal	Domain
A [auth C]	IPR000049	Electron transfer flavoprotein, beta-subunit, conserved site	Conserved Site
A [auth C]	IPR012255	Electron transfer flavoprotein, beta subunit	Family
A [auth C]	IPR014729	Rossmann-like alpha/beta/alpha sandwich fold	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.