Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

4RH3

AMPPCP-bound structure of human platelet phosphofructokinase in an R-state, crystal form II

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	0005515	molecular_function	protein binding
A	0005524	molecular_function	ATP binding
A	0005634	cellular_component	nucleus
A	0005737	cellular_component	cytoplasm
A	0005829	cellular_component	cytosol
A	0005945	cellular_component	6-phosphofructokinase complex
A	0006002	biological_process	fructose 6-phosphate metabolic process
A	0006096	biological_process	glycolytic process
A	0016020	cellular_component	membrane
A	0016301	molecular_function	kinase activity
A	0016740	molecular_function	transferase activity
A	0030388	biological_process	fructose 1,6-bisphosphate metabolic process
A	0044877	molecular_function	protein-containing complex binding
A	0045296	molecular_function	cadherin binding
A	0046872	molecular_function	metal ion binding
A	0061621	biological_process	canonical glycolysis
A	0070062	cellular_component	extracellular exosome
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	0005515	molecular_function	protein binding
B	0005524	molecular_function	ATP binding
B	0005634	cellular_component	nucleus
B	0005737	cellular_component	cytoplasm
B	0005829	cellular_component	cytosol
B	0005945	cellular_component	6-phosphofructokinase complex
B	0006002	biological_process	fructose 6-phosphate metabolic process
B	0006096	biological_process	glycolytic process
B	0016020	cellular_component	membrane
B	0016301	molecular_function	kinase activity
B	0016740	molecular_function	transferase activity
B	0030388	biological_process	fructose 1,6-bisphosphate metabolic process
B	0044877	molecular_function	protein-containing complex binding
B	0045296	molecular_function	cadherin binding
B	0046872	molecular_function	metal ion binding
B	0061621	biological_process	canonical glycolysis
B	0070062	cellular_component	extracellular exosome
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	0005515	molecular_function	protein binding
C	0005524	molecular_function	ATP binding
C	0005634	cellular_component	nucleus
C	0005737	cellular_component	cytoplasm
C	0005829	cellular_component	cytosol
C	0005945	cellular_component	6-phosphofructokinase complex
C	0006002	biological_process	fructose 6-phosphate metabolic process
C	0006096	biological_process	glycolytic process
C	0016020	cellular_component	membrane
C	0016301	molecular_function	kinase activity
C	0016740	molecular_function	transferase activity
C	0030388	biological_process	fructose 1,6-bisphosphate metabolic process
C	0044877	molecular_function	protein-containing complex binding
C	0045296	molecular_function	cadherin binding
C	0046872	molecular_function	metal ion binding
C	0061621	biological_process	canonical glycolysis
C	0070062	cellular_component	extracellular exosome
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	0005515	molecular_function	protein binding
D	0005524	molecular_function	ATP binding
D	0005634	cellular_component	nucleus
D	0005737	cellular_component	cytoplasm
D	0005829	cellular_component	cytosol
D	0005945	cellular_component	6-phosphofructokinase complex
D	0006002	biological_process	fructose 6-phosphate metabolic process
D	0006096	biological_process	glycolytic process
D	0016020	cellular_component	membrane
D	0016301	molecular_function	kinase activity
D	0016740	molecular_function	transferase activity
D	0030388	biological_process	fructose 1,6-bisphosphate metabolic process
D	0044877	molecular_function	protein-containing complex binding
D	0045296	molecular_function	cadherin binding
D	0046872	molecular_function	metal ion binding
D	0061621	biological_process	canonical glycolysis
D	0070062	cellular_component	extracellular exosome
D	0070095	molecular_function	fructose-6-phosphate binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	14
Details	BINDING SITE FOR RESIDUE ACP A 800

Chain	Residue
A	GLY33
A	GLY129
A	SER130
A	GLY133
A	LEU136
A	ASP177
A	GLY34
A	TYR64
A	ARG97
A	CYS98
A	PHE101
A	ARG102
A	GLY127
A	ASP128

site_id	AC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE PO4 A 801

Chain	Residue
A	GLY233
A	LYS264
A	ARG430
A	ARG434
A	GLY467
A	GLY468

site_id	AC3
Number of Residues	4
Details	BINDING SITE FOR RESIDUE PO4 A 802

Chain	Residue
A	ARG481
A	HIS671
B	ARG576
B	ARG665

site_id	AC4
Number of Residues	5
Details	BINDING SITE FOR RESIDUE PO4 B 801

Chain	Residue
A	ARG576
A	ARG665
B	ALA420
B	ARG481
B	HIS671

site_id	AC5
Number of Residues	14
Details	BINDING SITE FOR RESIDUE ACP B 802

Chain	Residue
B	SER32
B	GLY33
B	GLY34
B	ARG97
B	CYS98
B	PHE101
B	ARG102
B	GLY127
B	ASP128
B	GLY129
B	SER130
B	GLY133
B	ASP175
B	ASP177

site_id	AC6
Number of Residues	6
Details	BINDING SITE FOR RESIDUE PO4 B 803

Chain	Residue
B	GLY233
B	LYS264
B	ARG430
B	ARG434
B	GLY467
B	GLY468

site_id	AC7
Number of Residues	12
Details	BINDING SITE FOR RESIDUE ACP C 800

Chain	Residue
C	SER32
C	GLY33
C	ARG97
C	CYS98
C	PHE101
C	ARG102
C	GLY127
C	ASP128
C	GLY129
C	SER130
C	GLY133
C	LEU136

site_id	AC8
Number of Residues	6
Details	BINDING SITE FOR RESIDUE PO4 C 801

Chain	Residue
C	GLY233
C	LYS264
C	ARG430
C	ARG434
C	GLY467
C	GLY468

site_id	AC9
Number of Residues	5
Details	BINDING SITE FOR RESIDUE PO4 C 802

Chain	Residue
C	ALA420
C	ARG481
C	HIS671
D	ARG576
D	ARG665

site_id	BC1
Number of Residues	14
Details	BINDING SITE FOR RESIDUE ACP D 800

Chain	Residue
D	GLY33
D	GLY34
D	TYR64
D	ARG97
D	CYS98
D	PHE101
D	ARG102
D	GLY127
D	ASP128
D	GLY129
D	SER130
D	GLY133
D	SER173
D	ASP177

site_id	BC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE PO4 D 801

Chain	Residue
D	GLY233
D	LYS264
D	ARG430
D	ARG434
D	GLY467
D	GLY468

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	ARG301-ARG319
A	ARG665-ARG683

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	44
Details	Region: {"description":"Interdomain linker"}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	4
Details	Active site: {"description":"Proton acceptor","evidences":[{"source":"HAMAP-Rule","id":"MF_03184","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	40
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_03184","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	80
Details	Binding site: {"description":"in other chain","evidences":[{"source":"HAMAP-Rule","id":"MF_03184","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	4
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P47860","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	4
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"33607258","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16964243","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"18669648","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"18691976","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"20068231","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"21406692","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI7
Number of Residues	12
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI8
Number of Residues	4
Details	Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"PubMed","id":"15592455","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI9
Number of Residues	4
Details	Glycosylation: {"description":"O-linked (GlcNAc) serine","evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

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