1C81

MICHAELIS COMPLEX OF 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

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	LEU255-ASN264

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	ACT_SITE: Tele-phosphohistidine intermediate => ECO:0000269|PubMed:9253407

Chain	Residue	Details
A	GLY259

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site_id	SWS_FT_FI2
Number of Residues	1
Details	ACT_SITE: Proton donor/acceptor => ECO:0000269|PubMed:9253407

Chain	Residue	Details
A	ILE328

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site_id	SWS_FT_FI3
Number of Residues	4
Details	BINDING: BINDING => ECO:0000250|UniProtKB:Q16875

Chain	Residue	Details
A	HIS258
A	LEU265
A	THR308
A	GLY430

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site_id	SWS_FT_FI4
Number of Residues	7
Details	BINDING: BINDING => ECO:0000269|PubMed:9253407

Chain	Residue	Details
A	GLY271
A	GLU339
A	ASP353
A	TYR357
A	GLU368
A	ALA394
A	CYS398

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site_id	SWS_FT_FI5
Number of Residues	1
Details	BINDING: BINDING => ECO:0000269|Ref.15

Chain	Residue	Details
A	ALA350

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site_id	SWS_FT_FI6
Number of Residues	1
Details	SITE: Transition state stabilizer => ECO:0000250|UniProtKB:P00950

Chain	Residue	Details
A	GLN393

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Catalytic Information from CSA

site_id	CSA1
Number of Residues	4
Details	Annotated By Reference To The Literature 1qhf

Chain	Residue	Details
A	HIS392
A	HIS258
A	GLU327
A	ARG307

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site_id	CSA2
Number of Residues	6
Details	Annotated By Reference To The Literature 1qhf

Chain	Residue	Details
A	ASN264
A	HIS392
A	ARG257
A	HIS258
A	ARG307
A	GLU327

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