4NBE | pdb_00004nbe

Fluorene-bound oxygenase with Phe275 replaced by Trp and ferredoxin complex of carbazole 1,9a-dioxygenase (form2)

External Resource: Annotation

Domain Annotation: SCOP2 Classification
Domain Annotation: ECOD Classification
Domain Annotation: CATH
Gene Ontology: Gene Product Annotation
InterPro: Protein Family Classification

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
E	SCOP2B Superfamily	ISP domain	8080536	3000233	SCOP2B (2022-06-29)
D	SCOP2B Superfamily	ISP domain	8080536	3000233	SCOP2B (2022-06-29)
C	SCOP2B Superfamily	ISP domain	8039674	3000233	SCOP2B (2022-06-29)
C	SCOP2B Superfamily	Bet v1-like	8039675	3000738	SCOP2B (2022-06-29)
B	SCOP2B Superfamily	Bet v1-like	8039675	3000738	SCOP2B (2022-06-29)
B	SCOP2B Superfamily	ISP domain	8039674	3000233	SCOP2B (2022-06-29)
A	SCOP2B Superfamily	ISP domain	8039674	3000233	SCOP2B (2022-06-29)
A	SCOP2B Superfamily	Bet v1-like	8039675	3000738	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)
E	Rieske_RO_ferredoxin	e4nbeE2	A: beta sandwiches	X: ISP domain (From Topology)	H: ISP domain (From Topology)	T: ISP domain	F: Rieske_RO_ferredoxin	ECOD (1.6)
E	Rieske	e4nbeE1	A: few secondary structure elements	X: Trm112p-like (From Topology)	H: Trm112p-like (From Topology)	T: Trm112p-like	F: Rieske	ECOD (1.6)
D	Rieske_RO_ferredoxin	e4nbeD2	A: beta sandwiches	X: ISP domain (From Topology)	H: ISP domain (From Topology)	T: ISP domain	F: Rieske_RO_ferredoxin	ECOD (1.6)
D	Rieske	e4nbeD1	A: few secondary structure elements	X: Trm112p-like (From Topology)	H: Trm112p-like (From Topology)	T: Trm112p-like	F: Rieske	ECOD (1.6)
C	Rieske_8	e4nbeC3	A: beta sandwiches	X: ISP domain (From Topology)	H: ISP domain (From Topology)	T: ISP domain	F: Rieske_8	ECOD (1.6)
C	Aromatic_hydrox	e4nbeC1	A: a+b two layers	X: TBP-like	H: Bet v1-like (From Topology)	T: Bet v1-like	F: Aromatic_hydrox	ECOD (1.6)
C	Rieske_1	e4nbeC2	A: few secondary structure elements	X: Trm112p-like (From Topology)	H: Trm112p-like (From Topology)	T: Trm112p-like	F: Rieske_1	ECOD (1.6)
B	Rieske_8	e4nbeB3	A: beta sandwiches	X: ISP domain (From Topology)	H: ISP domain (From Topology)	T: ISP domain	F: Rieske_8	ECOD (1.6)
B	Aromatic_hydrox	e4nbeB1	A: a+b two layers	X: TBP-like	H: Bet v1-like (From Topology)	T: Bet v1-like	F: Aromatic_hydrox	ECOD (1.6)
B	Rieske_1	e4nbeB2	A: few secondary structure elements	X: Trm112p-like (From Topology)	H: Trm112p-like (From Topology)	T: Trm112p-like	F: Rieske_1	ECOD (1.6)
A	Rieske_8	e4nbeA3	A: beta sandwiches	X: ISP domain (From Topology)	H: ISP domain (From Topology)	T: ISP domain	F: Rieske_8	ECOD (1.6)
A	Aromatic_hydrox	e4nbeA1	A: a+b two layers	X: TBP-like	H: Bet v1-like (From Topology)	T: Bet v1-like	F: Aromatic_hydrox	ECOD (1.6)
A	Rieske_1	e4nbeA2	A: few secondary structure elements	X: Trm112p-like (From Topology)	H: Trm112p-like (From Topology)	T: Trm112p-like	F: Rieske_1	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
E	2.102.10.10	Mainly Beta	3-layer Sandwich	Rieske Iron-sulfur Protein	Rieske [2Fe-2S] iron-sulphur domain	CATH (4.3.0)
D	2.102.10.10	Mainly Beta	3-layer Sandwich	Rieske Iron-sulfur Protein	Rieske [2Fe-2S] iron-sulphur domain	CATH (4.3.0)
C	3.90.380.10	Alpha Beta	Alpha-Beta Complex	Naphthalene 1,2-dioxygenase Alpha Subunit	Chain A, domain 1	CATH (4.3.0)
C	2.20.25.680	Mainly Beta	Single Sheet	N-terminal domain of TfIIb		CATH (4.3.0)
C	2.20.25.10	Mainly Beta	Single Sheet	N-terminal domain of TfIIb		CATH (4.3.0)
B	3.90.380.10	Alpha Beta	Alpha-Beta Complex	Naphthalene 1,2-dioxygenase Alpha Subunit	Chain A, domain 1	CATH (4.3.0)
B	2.20.25.680	Mainly Beta	Single Sheet	N-terminal domain of TfIIb		CATH (4.3.0)
B	2.20.25.10	Mainly Beta	Single Sheet	N-terminal domain of TfIIb		CATH (4.3.0)
A	3.90.380.10	Alpha Beta	Alpha-Beta Complex	Naphthalene 1,2-dioxygenase Alpha Subunit	Chain A, domain 1	CATH (4.3.0)
A	2.20.25.680	Mainly Beta	Single Sheet	N-terminal domain of TfIIb		CATH (4.3.0)
A	2.20.25.10	Mainly Beta	Single Sheet	N-terminal domain of TfIIb		CATH (4.3.0)

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
D, E	Ferredoxin CarAc	oxidoreductase activity oxidoreductase activity, acting on hydrogen as donor, iron-sulfur protein as acceptor oxidoreductase activity, acting on hydrogen as donor ferredoxin hydrogenase activity catalytic activity dioxygenase activity iron-sulfur cluster binding 2 iron, 2 sulfur cluster binding binding metal cluster binding small molecule binding cation binding ion binding metal ion binding	cellular response to stimulus catabolic process response to stimulus cellular response to xenobiotic stimulus carbazole catabolic process xenobiotic catabolic process xenobiotic metabolic process response to xenobiotic stimulus cellular response to chemical stimulus response to chemical metabolic process cellular process	-
A, B, C	Terminal oxygenase component of carbazole	oxidoreductase activity catalytic activity iron-sulfur cluster binding 2 iron, 2 sulfur cluster binding binding metal cluster binding small molecule binding cation binding ion binding metal ion binding	-	-

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
D, E	IPR017941	Rieske [2Fe-2S] iron-sulphur domain	Domain
D, E	IPR036922	Rieske [2Fe-2S] iron-sulphur domain superfamily	Homologous Superfamily
A, B, C	IPR017941	Rieske [2Fe-2S] iron-sulphur domain	Domain
A, B, C	IPR050584	Cholesterol 7-desaturase	Family
A, B, C	IPR036922	Rieske [2Fe-2S] iron-sulphur domain superfamily	Homologous Superfamily
A, B, C	IPR021028	Homotrimeric ring hydroxylase, catalytic domain	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.