2KX9

Solution Structure of the Enzyme I dimer Using Residual Dipolar Couplings and Small Angle X-Ray Scattering

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005515	molecular_function	protein binding
A	0005737	cellular_component	cytoplasm
A	0005829	cellular_component	cytosol
A	0008965	molecular_function	phosphoenolpyruvate-protein phosphotransferase activity
A	0009401	biological_process	phosphoenolpyruvate-dependent sugar phosphotransferase system
A	0016301	molecular_function	kinase activity
A	0042802	molecular_function	identical protein binding
A	0046872	molecular_function	metal ion binding
B	0005515	molecular_function	protein binding
B	0005737	cellular_component	cytoplasm
B	0005829	cellular_component	cytosol
B	0008965	molecular_function	phosphoenolpyruvate-protein phosphotransferase activity
B	0009401	biological_process	phosphoenolpyruvate-dependent sugar phosphotransferase system
B	0016301	molecular_function	kinase activity
B	0042802	molecular_function	identical protein binding
B	0046872	molecular_function	metal ion binding

Functional Information from PROSITE/UniProt

site_id	PS00370
Number of Residues	12
Details	PEP_ENZYMES_PHOS_SITE PEP-utilizing enzymes phosphorylation site signature. GGrTsHTSIMAR

Chain	Residue	Details
A	GLY184-ARG195

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site_id	PS00742
Number of Residues	19
Details	PEP_ENZYMES_2 PEP-utilizing enzymes signature 2. DfFSIGTNDLtQYTLAvdR

Chain	Residue	Details
A	ASP447-ARG465

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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:12705838, ECO:0000269|PubMed:17053069

Chain	Residue	Details
A	HIS189
B	HIS189

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site_id	SWS_FT_FI2
Number of Residues	2
Details	ACT_SITE: Proton donor => ECO:0000269|PubMed:12705838, ECO:0000305|PubMed:17053069

Chain	Residue	Details
A	CYS502
B	CYS502

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site_id	SWS_FT_FI3
Number of Residues	4
Details	BINDING: BINDING => ECO:0000250|UniProtKB:P23533

Chain	Residue	Details
A	ARG296
A	ARG465
B	ARG296
B	ARG465

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site_id	SWS_FT_FI4
Number of Residues	8
Details	BINDING: BINDING => ECO:0000269|PubMed:17053069

Chain	Residue	Details
A	ARG332
A	GLU431
A	ASN454
A	ASP455
B	ARG332
B	GLU431
B	ASN454
B	ASP455

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Catalytic Information from CSA

site_id	MCSA1
Number of Residues	4
Details	M-CSA 920

Chain	Residue	Details
A	HIS189	covalent catalysis
A	GLU431	metal ligand
A	ASP455	metal ligand
A	CYS502	proton shuttle (general acid/base)

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site_id	MCSA2
Number of Residues	4
Details	M-CSA 920

Chain	Residue	Details
B	HIS189	covalent catalysis
B	GLU431	metal ligand
B	ASP455	metal ligand
B	CYS502	proton shuttle (general acid/base)

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