4FDK

F78L Tt H-NOX

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)
A	d4fdka_	Alpha and beta proteins (a+b)	Ligand-binding domain in the NO signalling and Golgi transport	Ligand-binding domain in the NO signalling and Golgi transport	H-NOX domain	Methyl-accepting chemotaxis protein	(Caldanaerobacter subterraneus subsp. tengcongensis MB4 ) [TaxId: 273068 ],	SCOPe (2.08)
B	d4fdkb_	Alpha and beta proteins (a+b)	Ligand-binding domain in the NO signalling and Golgi transport	Ligand-binding domain in the NO signalling and Golgi transport	H-NOX domain	Methyl-accepting chemotaxis protein	(Caldanaerobacter subterraneus subsp. tengcongensis MB4 ) [TaxId: 273068 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2B Superfamily	Ligand-binding domain in the NO signalling and Golgi transport	8040724	3001668	SCOP2B (2022-06-29)
B	SCOP2B Superfamily	Ligand-binding domain in the NO signalling and Golgi transport	8040724	3001668	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)
A	HNOB	e4fdkA1	A: a+b complex topology	X: H-NOX domain (From Topology)	H: H-NOX domain (From Topology)	T: H-NOX domain	F: HNOB	ECOD (1.6)
B	HNOB	e4fdkB1	A: a+b complex topology	X: H-NOX domain (From Topology)	H: H-NOX domain (From Topology)	T: H-NOX domain	F: HNOB	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	3.90.1520.10	Alpha Beta	Alpha-Beta Complex	H-NOX domain	H-NOX domain	CATH (4.3.0)
B	3.90.1520.10	Alpha Beta	Alpha-Beta Complex	H-NOX domain	H-NOX domain	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B	PF07700	Haem-NO-binding (HNOB)	Haem-NO-binding	The HNOB (Haem NO Binding) domain, is a predominantly alpha-helical domain and binds heme via a covalent linkage to histidine. It is a haem protein sensor (SONO) that displays femtomolar affinity for nitrous oxide, NO [3]. It is predicted to function ...	The HNOB (Haem NO Binding) domain, is a predominantly alpha-helical domain and binds heme via a covalent linkage to histidine. It is a haem protein sensor (SONO) that displays femtomolar affinity for nitrous oxide, NO [3]. It is predicted to function as a haem-dependent sensor for gaseous ligands and to transduce diverse downstream signals in both bacteria and animals.	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B	Methyl-accepting chemotaxis protein	binding organic cyclic compound binding tetrapyrrole binding heme binding cation binding ion binding metal ion binding small molecule binding	cellular response to stimulus regulation of biological process regulation of cellular process response to stimulus signaling biological regulation cellular process signal transduction cell communication	membrane cellular anatomical entity

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B	IPR038158	H-NOX domain superfamily	Homologous Superfamily
A, B	IPR024096	NO signalling/Golgi transport ligand-binding domain superfamily	Homologous Superfamily
A, B	IPR011644	Heme NO-binding	Domain
A, B	IPR004089	Methyl-accepting chemotaxis protein (MCP) signalling 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.