Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

6PFK

PHOSPHOFRUCTOKINASE, INHIBITED T-STATE

Replaces: 5PFK

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000166	molecular_function	nucleotide binding
A	0003824	molecular_function	catalytic activity
A	0003872	molecular_function	6-phosphofructokinase activity
A	0005524	molecular_function	ATP binding
A	0005737	cellular_component	cytoplasm
A	0005945	cellular_component	6-phosphofructokinase complex
A	0006002	biological_process	fructose 6-phosphate metabolic process
A	0006096	biological_process	glycolytic process
A	0008443	molecular_function	phosphofructokinase activity
A	0016208	molecular_function	AMP binding
A	0016301	molecular_function	kinase activity
A	0016740	molecular_function	transferase activity
A	0030388	biological_process	fructose 1,6-bisphosphate metabolic process
A	0042802	molecular_function	identical protein binding
A	0046835	biological_process	carbohydrate phosphorylation
A	0046872	molecular_function	metal ion binding
A	0048029	molecular_function	monosaccharide binding
A	0061621	biological_process	canonical glycolysis
A	0070095	molecular_function	fructose-6-phosphate binding
B	0000166	molecular_function	nucleotide binding
B	0003824	molecular_function	catalytic activity
B	0003872	molecular_function	6-phosphofructokinase activity
B	0005524	molecular_function	ATP binding
B	0005737	cellular_component	cytoplasm
B	0005945	cellular_component	6-phosphofructokinase complex
B	0006002	biological_process	fructose 6-phosphate metabolic process
B	0006096	biological_process	glycolytic process
B	0008443	molecular_function	phosphofructokinase activity
B	0016208	molecular_function	AMP binding
B	0016301	molecular_function	kinase activity
B	0016740	molecular_function	transferase activity
B	0030388	biological_process	fructose 1,6-bisphosphate metabolic process
B	0042802	molecular_function	identical protein binding
B	0046835	biological_process	carbohydrate phosphorylation
B	0046872	molecular_function	metal ion binding
B	0048029	molecular_function	monosaccharide binding
B	0061621	biological_process	canonical glycolysis
B	0070095	molecular_function	fructose-6-phosphate binding
C	0000166	molecular_function	nucleotide binding
C	0003824	molecular_function	catalytic activity
C	0003872	molecular_function	6-phosphofructokinase activity
C	0005524	molecular_function	ATP binding
C	0005737	cellular_component	cytoplasm
C	0005945	cellular_component	6-phosphofructokinase complex
C	0006002	biological_process	fructose 6-phosphate metabolic process
C	0006096	biological_process	glycolytic process
C	0008443	molecular_function	phosphofructokinase activity
C	0016208	molecular_function	AMP binding
C	0016301	molecular_function	kinase activity
C	0016740	molecular_function	transferase activity
C	0030388	biological_process	fructose 1,6-bisphosphate metabolic process
C	0042802	molecular_function	identical protein binding
C	0046835	biological_process	carbohydrate phosphorylation
C	0046872	molecular_function	metal ion binding
C	0048029	molecular_function	monosaccharide binding
C	0061621	biological_process	canonical glycolysis
C	0070095	molecular_function	fructose-6-phosphate binding
D	0000166	molecular_function	nucleotide binding
D	0003824	molecular_function	catalytic activity
D	0003872	molecular_function	6-phosphofructokinase activity
D	0005524	molecular_function	ATP binding
D	0005737	cellular_component	cytoplasm
D	0005945	cellular_component	6-phosphofructokinase complex
D	0006002	biological_process	fructose 6-phosphate metabolic process
D	0006096	biological_process	glycolytic process
D	0008443	molecular_function	phosphofructokinase activity
D	0016208	molecular_function	AMP binding
D	0016301	molecular_function	kinase activity
D	0016740	molecular_function	transferase activity
D	0030388	biological_process	fructose 1,6-bisphosphate metabolic process
D	0042802	molecular_function	identical protein binding
D	0046835	biological_process	carbohydrate phosphorylation
D	0046872	molecular_function	metal ion binding
D	0048029	molecular_function	monosaccharide binding
D	0061621	biological_process	canonical glycolysis
D	0070095	molecular_function	fructose-6-phosphate binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	10
Details	BINDING SITE FOR RESIDUE PGA A 325

Chain	Residue
A	ARG154
B	HOH338
A	ARG211
A	LYS213
A	LYS214
A	HOH372
B	ARG21
B	ARG25
B	GLY58
B	ASP59

site_id	AC2
Number of Residues	10
Details	BINDING SITE FOR RESIDUE PGA B 325

Chain	Residue
A	ARG21
A	ARG25
A	GLY58
A	ASP59
A	HOH333
B	ARG154
B	ARG211
B	LYS213
B	LYS214
B	HOH328

site_id	AC3
Number of Residues	10
Details	BINDING SITE FOR RESIDUE PGA C 325

Chain	Residue
C	ARG154
C	ARG211
C	LYS213
C	LYS214
C	HOH372
D	ARG21
D	ARG25
D	GLY58
D	ASP59
D	HOH347

site_id	AC4
Number of Residues	11
Details	BINDING SITE FOR RESIDUE PGA D 325

Chain	Residue
C	ARG21
C	ARG25
C	GLY55
C	GLY58
C	ASP59
D	ARG154
D	ARG211
D	LYS213
D	LYS214
D	HOH331
D	HOH335

Functional Information from PROSITE/UniProt

site_id	PS00433
Number of Residues	19
Details	PHOSPHOFRUCTOKINASE Phosphofructokinase signature. RvtvlGHvQRGGsptafDR

Chain	Residue	Details
A	ARG243-ARG261

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	Active site: {"description":"Proton acceptor","evidences":[{"source":"HAMAP-Rule","id":"MF_00339","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	16
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00339","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	32
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00339","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"6115424","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	32
Details	Binding site: {"description":"in other chain","evidences":[{"source":"HAMAP-Rule","id":"MF_00339","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"12390023","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"6115424","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	24
Details	Binding site: {"description":"in other chain","evidences":[{"source":"HAMAP-Rule","id":"MF_00339","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"6115424","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	4
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00339","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"12390023","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"6115424","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

Catalytic Information from CSA

site_id	CSA1
Number of Residues	5
Details	Annotated By Reference To The Literature 1pfk

Chain	Residue	Details
A	GLY11
A	ASP127
A	THR125
A	ARG72
A	ARG171

site_id	CSA2
Number of Residues	5
Details	Annotated By Reference To The Literature 1pfk

Chain	Residue	Details
B	GLY11
B	ASP127
B	THR125
B	ARG72
B	ARG171

site_id	CSA3
Number of Residues	5
Details	Annotated By Reference To The Literature 1pfk

Chain	Residue	Details
C	GLY11
C	ASP127
C	THR125
C	ARG72
C	ARG171

site_id	CSA4
Number of Residues	5
Details	Annotated By Reference To The Literature 1pfk

Chain	Residue	Details
D	GLY11
D	ASP127
D	THR125
D	ARG72
D	ARG171

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)
		EDMap 2fo-fc (MTZ)