1MTO

Crystal structure of a Phosphofructokinase mutant from Bacillus stearothermophilus bound with fructose-6-phosphate

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	d1mtoa_	Alpha and beta proteins (a/b)	Phosphofructokinase	Phosphofructokinase	Phosphofructokinase	ATP-dependent phosphofructokinase	(Geobacillus stearothermophilus ) [TaxId: 1422 ],	SCOPe (2.08)
D	d1mtod_	Alpha and beta proteins (a/b)	Phosphofructokinase	Phosphofructokinase	Phosphofructokinase	ATP-dependent phosphofructokinase	(Geobacillus stearothermophilus ) [TaxId: 1422 ],	SCOPe (2.08)
E	d1mtoe_	Alpha and beta proteins (a/b)	Phosphofructokinase	Phosphofructokinase	Phosphofructokinase	ATP-dependent phosphofructokinase	(Geobacillus stearothermophilus ) [TaxId: 1422 ],	SCOPe (2.08)
F	d1mtof_	Alpha and beta proteins (a/b)	Phosphofructokinase	Phosphofructokinase	Phosphofructokinase	ATP-dependent phosphofructokinase	(Geobacillus stearothermophilus ) [TaxId: 1422 ],	SCOPe (2.08)
G	d1mtog_	Alpha and beta proteins (a/b)	Phosphofructokinase	Phosphofructokinase	Phosphofructokinase	ATP-dependent phosphofructokinase	(Geobacillus stearothermophilus ) [TaxId: 1422 ],	SCOPe (2.08)
H	d1mtoh_	Alpha and beta proteins (a/b)	Phosphofructokinase	Phosphofructokinase	Phosphofructokinase	ATP-dependent phosphofructokinase	(Geobacillus stearothermophilus ) [TaxId: 1422 ],	SCOPe (2.08)
B	d1mtob_	Alpha and beta proteins (a/b)	Phosphofructokinase	Phosphofructokinase	Phosphofructokinase	ATP-dependent phosphofructokinase	(Geobacillus stearothermophilus ) [TaxId: 1422 ],	SCOPe (2.08)
C	d1mtoc_	Alpha and beta proteins (a/b)	Phosphofructokinase	Phosphofructokinase	Phosphofructokinase	ATP-dependent phosphofructokinase	(Geobacillus stearothermophilus ) [TaxId: 1422 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2B Superfamily	Phosphofructokinase	8033227	3001648	SCOP2B (2022-06-29)
D	SCOP2B Superfamily	Phosphofructokinase	8033227	3001648	SCOP2B (2022-06-29)
E	SCOP2B Superfamily	Phosphofructokinase	8033227	3001648	SCOP2B (2022-06-29)
F	SCOP2B Superfamily	Phosphofructokinase	8033227	3001648	SCOP2B (2022-06-29)
G	SCOP2B Superfamily	Phosphofructokinase	8033227	3001648	SCOP2B (2022-06-29)
H	SCOP2B Superfamily	Phosphofructokinase	8033227	3001648	SCOP2B (2022-06-29)
B	SCOP2B Superfamily	Phosphofructokinase	8033227	3001648	SCOP2B (2022-06-29)
C	SCOP2B Superfamily	Phosphofructokinase	8033227	3001648	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	PFK_N	e1mtoA2	A: a/b three-layered sandwiches	X: Flavodoxin-like	H: Class I glutamine amidotransferase-like	T: Phosphofructokinase N-terminal domain	F: PFK_N	ECOD (1.6)
A	PFK_C	e1mtoA1	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)
D	PFK_N	e1mtoD1	A: a/b three-layered sandwiches	X: Flavodoxin-like	H: Class I glutamine amidotransferase-like	T: Phosphofructokinase N-terminal domain	F: PFK_N	ECOD (1.6)
D	PFK_C	e1mtoD2	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)
E	PFK_N	e1mtoE1	A: a/b three-layered sandwiches	X: Flavodoxin-like	H: Class I glutamine amidotransferase-like	T: Phosphofructokinase N-terminal domain	F: PFK_N	ECOD (1.6)
E	PFK_C	e1mtoE2	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)
F	PFK_N	e1mtoF1	A: a/b three-layered sandwiches	X: Flavodoxin-like	H: Class I glutamine amidotransferase-like	T: Phosphofructokinase N-terminal domain	F: PFK_N	ECOD (1.6)
F	PFK_C	e1mtoF2	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)
G	PFK_N	e1mtoG2	A: a/b three-layered sandwiches	X: Flavodoxin-like	H: Class I glutamine amidotransferase-like	T: Phosphofructokinase N-terminal domain	F: PFK_N	ECOD (1.6)
G	PFK_C	e1mtoG1	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)
H	PFK_N	e1mtoH1	A: a/b three-layered sandwiches	X: Flavodoxin-like	H: Class I glutamine amidotransferase-like	T: Phosphofructokinase N-terminal domain	F: PFK_N	ECOD (1.6)
H	PFK_C	e1mtoH2	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	e1mtoB2	A: a/b three-layered sandwiches	X: Flavodoxin-like	H: Class I glutamine amidotransferase-like	T: Phosphofructokinase N-terminal domain	F: PFK_N	ECOD (1.6)
B	PFK_C	e1mtoB1	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	e1mtoC2	A: a/b three-layered sandwiches	X: Flavodoxin-like	H: Class I glutamine amidotransferase-like	T: Phosphofructokinase N-terminal domain	F: PFK_N	ECOD (1.6)
C	PFK_C	e1mtoC1	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)
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)
E	3.40.50.450	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold		CATH (4.3.0)
E	3.40.50.460	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	Phosphofructokinase domain	CATH (4.3.0)
F	3.40.50.450	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold		CATH (4.3.0)
F	3.40.50.460	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	Phosphofructokinase domain	CATH (4.3.0)
G	3.40.50.450	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold		CATH (4.3.0)
G	3.40.50.460	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	Phosphofructokinase domain	CATH (4.3.0)
H	3.40.50.450	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold		CATH (4.3.0)
H	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)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B, C, D, E A, B, C, D, E, F, G, H	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, E A, B, C, D, E, F, G, H	6-phosphofructokinase	binding adenyl ribonucleotide binding nucleotide binding purine ribonucleotide binding purine ribonucleoside triphosphate binding nucleoside phosphate binding ion binding purine nucleotide binding organic cyclic compound binding anion binding adenyl nucleotide binding ATP binding heterocyclic compound binding carbohydrate derivative binding binding adenyl ribonucleotide binding nucleotide binding purine ribonucleotide binding purine ribonucleoside triphosphate binding nucleoside phosphate binding ion binding purine nucleotide binding organic cyclic compound binding anion binding adenyl nucleotide binding ATP binding heterocyclic compound binding carbohydrate derivative binding ribonucleotide binding small molecule binding 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 cation binding metal ion 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, E A, B, C, D, E, F, G, H	IPR012828	ATP-dependent 6-phosphofructokinase, prokaryotic	Family
A, B, C, D, E A, B, C, D, E, F, G, H	IPR000023	Phosphofructokinase domain	Domain
A, B, C, D, E A, B, C, D, E, F, G, H	IPR012003	ATP-dependent 6-phosphofructokinase, prokaryotic-type	Family
A, B, C, D, E A, B, C, D, E, F, G, H	IPR022953	ATP-dependent 6-phosphofructokinase	Family
A, B, C, D, E A, B, C, D, E, F, G, H	IPR035966	Phosphofructokinase superfamily	Homologous Superfamily
A, B, C, D, E A, B, C, D, E, F, G, H	IPR015912	Phosphofructokinase, conserved site	Conserved Site

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.