1TIP

THE BISPHOSPHATASE DOMAIN OF THE BIFUNCTIONAL RAT LIVER 6-PHOSPHOFRUCTO-2-KINASE/FRUCTOSE-2,6-BISPHOSPHATASE

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003824	molecular_function	catalytic activity
A	0005524	molecular_function	ATP binding
A	0006003	biological_process	fructose 2,6-bisphosphate metabolic process
B	0003824	molecular_function	catalytic activity
B	0005524	molecular_function	ATP binding
B	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. LcRHGEsElN

Chain	Residue	Details
A	LEU6-ASN15

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	ACT_SITE: Tele-phosphohistidine intermediate => ECO:0000269|PubMed:9253407

Chain	Residue	Details
A	GLY10
B	GLY10

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site_id	SWS_FT_FI2
Number of Residues	2
Details	ACT_SITE: Proton donor/acceptor => ECO:0000269|PubMed:9253407

Chain	Residue	Details
A	ILE79
B	ILE79

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site_id	SWS_FT_FI3
Number of Residues	8
Details	BINDING: BINDING => ECO:0000250|UniProtKB:Q16875

Chain	Residue	Details
A	THR59
A	GLY181
B	NEP9
B	LEU16
B	THR59
B	GLY181
A	NEP9
A	LEU16

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site_id	SWS_FT_FI4
Number of Residues	14
Details	BINDING: BINDING => ECO:0000269|PubMed:9253407

Chain	Residue	Details
A	CYS149
B	GLY22
B	GLU90
B	ASP104
B	TYR108
B	GLU119
B	ALA145
B	CYS149
A	GLY22
A	GLU90
A	ASP104
A	TYR108
A	GLU119
A	ALA145

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site_id	SWS_FT_FI5
Number of Residues	2
Details	BINDING: BINDING => ECO:0000269|Ref.15

Chain	Residue	Details
A	ALA101
B	ALA101

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site_id	SWS_FT_FI6
Number of Residues	2
Details	SITE: Transition state stabilizer => ECO:0000250|UniProtKB:P00950

Chain	Residue	Details
A	GLN144
B	GLN144

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