6IBZ

Human PFKFB3 in complex with a N-Aryl 6-Aminoquinoxaline inhibitor 7

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003824	molecular_function	catalytic activity
A	0003873	molecular_function	6-phosphofructo-2-kinase activity
A	0005524	molecular_function	ATP binding
A	0006000	biological_process	fructose metabolic process
A	0006003	biological_process	fructose 2,6-bisphosphate metabolic process

Functional Information from PROSITE/UniProt

site_id	PS00175
Number of Residues	10
Details	PG_MUTASE Phosphoglycerate mutase family phosphohistidine signature. LcRHGEnEhN

Chain	Residue	Details
A	LEU250-ASN259

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	ACT_SITE: ACT_SITE => ECO:0000255

Chain	Residue	Details
A	LEU137
A	VAL167

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site_id	SWS_FT_FI2
Number of Residues	1
Details	ACT_SITE: Tele-phosphohistidine intermediate => ECO:0000269|PubMed:22275052

Chain	Residue	Details
A	GLY266

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site_id	SWS_FT_FI3
Number of Residues	1
Details	ACT_SITE: Proton donor/acceptor => ECO:0000269|PubMed:22275052

Chain	Residue	Details
A	GLU335

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site_id	SWS_FT_FI4
Number of Residues	3
Details	BINDING: BINDING => ECO:0000269|PubMed:16316985, ECO:0000269|PubMed:17499765, ECO:0000269|PubMed:22275052

Chain	Residue	Details
A	LEU54
A	ASP176
A	SER437

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site_id	SWS_FT_FI5
Number of Residues	7
Details	BINDING: BINDING => ECO:0000269|PubMed:16316985

Chain	Residue	Details
A	PHE87
A	SER111
A	PHE139
A	PHE145
A	GLU181
A	PRO202
A	ASP206

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site_id	SWS_FT_FI6
Number of Residues	8
Details	BINDING: BINDING => ECO:0000269|PubMed:25849762

Chain	Residue	Details
A	GLY265
A	SER272
A	ALA278
A	LEU346
A	GLU360
A	ASP364
A	GLU375
A	LYS401

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site_id	SWS_FT_FI7
Number of Residues	2
Details	BINDING: BINDING => ECO:0000250|UniProtKB:P07953

Chain	Residue	Details
A	PRO357
A	GLU405

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site_id	SWS_FT_FI8
Number of Residues	3
Details	SITE: Transition state stabilizer => ECO:0000269|PubMed:22275052

Chain	Residue	Details
A	GLY265
A	SER272
A	ASP400

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