5XZ7

Crystal Structure of Phosphofructokinase from Staphylococcus aureus in complex with adenylylimidodiphosphate, the ATP analogue

Functional Information from GO Data

Chain	GOid	namespace	contents
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	0016310	biological_process	phosphorylation
A	0030388	biological_process	fructose 1,6-bisphosphate metabolic process
A	0042802	molecular_function	identical protein binding
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

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	ARG245-ARG263

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	ACT_SITE: Proton acceptor => ECO:0000255|HAMAP-Rule:MF_00339

Chain	Residue	Details
A	ASP129

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site_id	SWS_FT_FI2
Number of Residues	7
Details	BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00339

Chain	Residue	Details
A	GLY11
A	ARG21
A	ARG72
A	GLY102
A	ASP103
A	ARG164
A	ARG245

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site_id	SWS_FT_FI3
Number of Residues	8
Details	BINDING: in other chain => ECO:0000255|HAMAP-Rule:MF_00339

Chain	Residue	Details
A	THR127
A	ARG156
A	MET171
A	GLY187
A	ARG213
A	LYS215
A	GLU224
A	HIS251

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