2VR0

Crystal structure of cytochrome c nitrite reductase NrfHA complex bound to the HQNO inhibitor

External Resource: Annotation

Domain Annotation: SCOP/SCOPe Classification
Domain Annotation: ECOD Classification
Domain Annotation: CATH
Protein Family Annotation
Gene Ontology: Gene Product Annotation
InterPro: Protein Family Classification
Membrane Protein Annotation: PDBTM

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

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
A	d2vr0a_	All alpha proteins	Multiheme cytochromes	Multiheme cytochromes	Di-heme elbow motif	automated matches	(Nitratidesulfovibrio vulgaris str. Hildenborough ) [TaxId: 882 ],	SCOPe (2.08)
B	d2vr0b_	All alpha proteins	Multiheme cytochromes	Multiheme cytochromes	Di-heme elbow motif	automated matches	(Nitratidesulfovibrio vulgaris str. Hildenborough ) [TaxId: 882 ],	SCOPe (2.08)
D	d2vr0d_	All alpha proteins	Multiheme cytochromes	Multiheme cytochromes	Di-heme elbow motif	automated matches	(Nitratidesulfovibrio vulgaris str. Hildenborough ) [TaxId: 882 ],	SCOPe (2.08)
E	d2vr0e_	All alpha proteins	Multiheme cytochromes	Multiheme cytochromes	Di-heme elbow motif	automated matches	(Nitratidesulfovibrio vulgaris str. Hildenborough ) [TaxId: 882 ],	SCOPe (2.08)

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
A	Cytochrom_C552	e2vr0A1	A: few secondary structure elements	X: Multiheme cytochromes	H: Di-heme elbow motif (From Topology)	T: Di-heme elbow motif	F: Cytochrom_C552	ECOD (1.6)
B	Cytochrom_C552	e2vr0B1	A: few secondary structure elements	X: Multiheme cytochromes	H: Di-heme elbow motif (From Topology)	T: Di-heme elbow motif	F: Cytochrom_C552	ECOD (1.6)
D	Cytochrom_C552	e2vr0D1	A: few secondary structure elements	X: Multiheme cytochromes	H: Di-heme elbow motif (From Topology)	T: Di-heme elbow motif	F: Cytochrom_C552	ECOD (1.6)
E	Cytochrom_C552	e2vr0E1	A: few secondary structure elements	X: Multiheme cytochromes	H: Di-heme elbow motif (From Topology)	T: Di-heme elbow motif	F: Cytochrom_C552	ECOD (1.6)
C	Cytochrom_NNT	e2vr0C1	A: few secondary structure elements	X: Multiheme cytochromes	H: Cytochrome c3-like (From Topology)	T: Cytochrome c3-like	F: Cytochrom_NNT	ECOD (1.6)
F	Cytochrom_NNT	e2vr0F1	A: few secondary structure elements	X: Multiheme cytochromes	H: Cytochrome c3-like (From Topology)	T: Cytochrome c3-like	F: Cytochrom_NNT	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	1.10.1130.10	Mainly Alpha	Orthogonal Bundle	Flavocytochrome C3	Chain A, domain 2	CATH (4.3.0)
A	1.20.140.10	Mainly Alpha	Up-down Bundle	Butyryl-CoA Dehydrogenase, subunit A	domain 3	CATH (4.3.0)
B	1.10.1130.10	Mainly Alpha	Orthogonal Bundle	Flavocytochrome C3	Chain A, domain 2	CATH (4.3.0)
B	1.20.140.10	Mainly Alpha	Up-down Bundle	Butyryl-CoA Dehydrogenase, subunit A	domain 3	CATH (4.3.0)
D	1.10.1130.10	Mainly Alpha	Orthogonal Bundle	Flavocytochrome C3	Chain A, domain 2	CATH (4.3.0)
D	1.20.140.10	Mainly Alpha	Up-down Bundle	Butyryl-CoA Dehydrogenase, subunit A	domain 3	CATH (4.3.0)
E	1.10.1130.10	Mainly Alpha	Orthogonal Bundle	Flavocytochrome C3	Chain A, domain 2	CATH (4.3.0)
E	1.20.140.10	Mainly Alpha	Up-down Bundle	Butyryl-CoA Dehydrogenase, subunit A	domain 3	CATH (4.3.0)
C	1.10.3820.10	Mainly Alpha	Orthogonal Bundle	Multiheme cytochrome fold	Di-heme elbow motif domain	CATH (4.3.0)
F	1.10.3820.10	Mainly Alpha	Orthogonal Bundle	Multiheme cytochrome fold	Di-heme elbow motif domain	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B, D, E	PF02335	Cytochrome c552 (Cytochrom_C552)	Cytochrome c552	-	Family

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B, D, E	CYTOCHROME C NITRITE REDUCTASE, CATALYTIC SUBUNIT NFRA	oxidoreductase activity, acting on other nitrogenous compounds as donors, cytochrome as acceptor oxidoreductase activity nitrite reductase (cytochrome, ammonia-forming) activity oxidoreductase activity, acting on other nitrogenous compounds as donors nitrite reductase activity catalytic activity binding organic cyclic compound binding tetrapyrrole binding heme binding cation binding ion binding metal ion binding small molecule binding	anaerobic electron transport chain cellular respiration energy derivation by oxidation of organic compounds respiratory electron transport chain electron transport chain metabolic process cellular process generation of precursor metabolites and energy anaerobic respiration	cell periphery cellular anatomical structure plasma membrane membrane outer membrane-bounded periplasmic space cell envelope periplasmic space
C, F	NAPC/NIRT CYTOCHROME C FAMILY PROTEIN	binding organic cyclic compound binding tetrapyrrole binding heme binding electron transfer activity cation binding ion binding metal ion binding small molecule binding	nitrogen cycle metabolic process denitrification pathway metabolic process cellular process cellular respiration energy derivation by oxidation of organic compounds generation of precursor metabolites and energy anaerobic respiration	cell periphery cellular anatomical structure plasma membrane membrane

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B, D, E	IPR036280	Multiheme cytochrome superfamily	Homologous Superfamily
A, B, D, E	IPR003321	Cytochrome c552	Family
C, F	IPR005126	NapC/NirT cytochrome c, N-terminal	Domain
C, F	IPR036280	Multiheme cytochrome superfamily	Homologous Superfamily
C, F	IPR024717	Denitrification system component NapC/NirT/NrfH	Family
C, F	IPR051174	Cytochrome c-type Electron Transfer	Family
C, F	IPR038266	NapC/NirT cytochrome c superfamily	Homologous Superfamily

Membrane Protein Annotation: PDBTM PDBTM Database Homepage

Chains	External Link	Comment
A, B, C, D, E A, B, C, D, E, F	PDBTM	Annotated as membrane protein by PDBTM

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.