3CLT

Crystal structure of the R236E mutant of Methylophilus methylotrophus ETF

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]	d3cltd1	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]	d3cltd2	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]	d3cltc_	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	e3cltD1	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	e3cltD2	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	e3cltC1	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 transfer flavoprotein subunit alpha	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 transfer flavoprotein subunit beta	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.