3HNO

Crystal Structure of Pyrophosphate-dependent phosphofructokinase from Nitrosospira multiformis. Northeast Structural Genomics Consortium target id NmR42

External Resource: Annotation

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

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
A	PFK_N_1	e3hnoA2	A: a/b three-layered sandwiches	X: Flavodoxin-like	H: Class I glutamine amidotransferase-like	T: Phosphofructokinase N-terminal domain	F: PFK_N_1	ECOD (1.6)
A	PFK_C	e3hnoA1	A: a/b three-layered sandwiches	X: Phosphofructokinase C-terminal domain (From Topology)	H: Phosphofructokinase C-terminal domain (From Topology)	T: Phosphofructokinase C-terminal domain	F: PFK_C	ECOD (1.6)
B	PFK_N_1	e3hnoB1	A: a/b three-layered sandwiches	X: Flavodoxin-like	H: Class I glutamine amidotransferase-like	T: Phosphofructokinase N-terminal domain	F: PFK_N_1	ECOD (1.6)
B	PFK_C	e3hnoB2	A: a/b three-layered sandwiches	X: Phosphofructokinase C-terminal domain (From Topology)	H: Phosphofructokinase C-terminal domain (From Topology)	T: Phosphofructokinase C-terminal domain	F: PFK_C	ECOD (1.6)
C	PFK_N_1	e3hnoC2	A: a/b three-layered sandwiches	X: Flavodoxin-like	H: Class I glutamine amidotransferase-like	T: Phosphofructokinase N-terminal domain	F: PFK_N_1	ECOD (1.6)
C	PFK_C	e3hnoC1	A: a/b three-layered sandwiches	X: Phosphofructokinase C-terminal domain (From Topology)	H: Phosphofructokinase C-terminal domain (From Topology)	T: Phosphofructokinase C-terminal domain	F: PFK_C	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	3.40.50.450	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold		CATH (4.3.0)
A	3.40.50.460	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	Phosphofructokinase domain	CATH (4.3.0)
B	3.40.50.450	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold		CATH (4.3.0)
B	3.40.50.460	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	Phosphofructokinase domain	CATH (4.3.0)
C	3.40.50.450	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold		CATH (4.3.0)
C	3.40.50.460	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	Phosphofructokinase domain	CATH (4.3.0)
D	3.40.50.450	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold		CATH (4.3.0)
D	3.40.50.460	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	Phosphofructokinase domain	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B, C, D	PF00365	Phosphofructokinase (PFK)	Phosphofructokinase	-	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B, C, D	Pyrophosphate-dependent phosphofructokinase	carbohydrate kinase activity kinase activity phosphofructokinase activity 6-phosphofructokinase activity transferase activity catalytic activity phosphotransferase activity, alcohol group as acceptor transferase activity, transferring phosphorus-containing groups diphosphate-fructose-6-phosphate 1-phosphotransferase activity cation binding ion binding binding metal ion binding small molecule binding	organic substance metabolic process organophosphate metabolic process cellular metabolic process phosphate-containing compound metabolic process fructose 6-phosphate metabolic process carbohydrate derivative metabolic process metabolic process cellular process phosphorus metabolic process	intracellular anatomical structure cytoplasm cellular anatomical entity

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B, C, D	IPR000023	Phosphofructokinase domain	Domain
A, B, C, D	IPR022953	ATP-dependent 6-phosphofructokinase	Family
A, B, C, D	IPR035966	Phosphofructokinase superfamily	Homologous Superfamily
A, B, C, D	IPR011404	Pyrophosphate--fructose 6-phosphate 1-phosphotransferase	Family

RCSB PDB Core Operations are funded by the National Science Foundation (DBI-1832184), 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 R01GM133198.