Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

4I7E

Crystal Structure of the Bacillus stearothermophilus Phosphofructokinase Mutant D12A in Complex with PEP

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	12
Details	BINDING SITE FOR RESIDUE PEP A 401

Chain	Residue
A	ARG21
B	LYS214
B	HIS215
B	HOH626
A	ARG25
A	GLY58
A	ASP59
A	HOH529
B	ARG154
B	GLY185
B	ARG211
B	LYS213

site_id	AC2
Number of Residues	11
Details	BINDING SITE FOR RESIDUE PEP B 401

Chain	Residue
A	ARG154
A	ARG211
A	LYS213
A	LYS214
A	HIS215
B	ARG21
B	ARG25
B	GLY58
B	ASP59
B	HOH503
B	HOH538

site_id	AC3
Number of Residues	15
Details	BINDING SITE FOR RESIDUE PEP C 401

Chain	Residue
C	ARG21
C	ARG25
C	GLY55
C	GLY58
C	ASP59
C	HOH508
C	HOH549
C	HOH612
D	ARG154
D	GLY185
D	ARG211
D	LYS213
D	LYS214
D	HIS215
D	HOH529

site_id	AC4
Number of Residues	14
Details	BINDING SITE FOR RESIDUE PEP D 401

Chain	Residue
C	ARG154
C	ARG211
C	LYS213
C	LYS214
C	HIS215
C	HOH503
D	ARG21
D	ARG25
D	GLY55
D	GLY58
D	ASP59
D	HOH511
D	HOH571
D	HOH648

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

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