2WQD

Crystal structure of enzyme I of the phosphoenolpyruvate:sugar phosphotransferase system in the dephosphorylated state

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003824	molecular_function	catalytic activity
A	0005737	cellular_component	cytoplasm
A	0008965	molecular_function	phosphoenolpyruvate-protein phosphotransferase activity
A	0009401	biological_process	phosphoenolpyruvate-dependent sugar phosphotransferase system
A	0016301	molecular_function	kinase activity
A	0016310	biological_process	phosphorylation
A	0016772	molecular_function	transferase activity, transferring phosphorus-containing groups
A	0046872	molecular_function	metal ion binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	3
Details	BINDING SITE FOR RESIDUE CA A 1572

Chain	Residue
A	THR397
A	ASN399
A	GLN477

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Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	ASP449-ARG467

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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:0000250|UniProtKB:P08839, ECO:0000305|PubMed:19801641

Chain	Residue	Details
A	ALA191

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site_id	SWS_FT_FI2
Number of Residues	1
Details	ACT_SITE: Proton donor => ECO:0000250|UniProtKB:P08839

Chain	Residue	Details
A	CYS504

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site_id	SWS_FT_FI3
Number of Residues	2
Details	BINDING: BINDING => ECO:0000250|UniProtKB:P23533

Chain	Residue	Details
A	ARG298
A	ARG467

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site_id	SWS_FT_FI4
Number of Residues	4
Details	BINDING: BINDING => ECO:0000250|UniProtKB:P08839

Chain	Residue	Details
A	ARG334
A	GLU433
A	ASN456
A	ASP457

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Catalytic Information from CSA

site_id	CSA1
Number of Residues	2
Details	Annotated By Reference To The Literature 1zym

Chain	Residue	Details
A	THR170
A	ALA191

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