8UOY

Major interface of Streptococcal surface enolase dimer from AP53 group A streptococcus bound to a lipid vesicle

Functional Information from GO Data

Chain	GOid	namespace	contents
B	0000015	cellular_component	phosphopyruvate hydratase complex
B	0000287	molecular_function	magnesium ion binding
B	0004634	molecular_function	phosphopyruvate hydratase activity
B	0005576	cellular_component	extracellular region
B	0005737	cellular_component	cytoplasm
B	0006096	biological_process	glycolytic process
B	0009274	cellular_component	peptidoglycan-based cell wall
B	0009986	cellular_component	cell surface
B	0016829	molecular_function	lyase activity
B	0046872	molecular_function	metal ion binding
C	0000015	cellular_component	phosphopyruvate hydratase complex
C	0000287	molecular_function	magnesium ion binding
C	0004634	molecular_function	phosphopyruvate hydratase activity
C	0005576	cellular_component	extracellular region
C	0005737	cellular_component	cytoplasm
C	0006096	biological_process	glycolytic process
C	0009274	cellular_component	peptidoglycan-based cell wall
C	0009986	cellular_component	cell surface
C	0016829	molecular_function	lyase activity
C	0046872	molecular_function	metal ion binding

Functional Information from PROSITE/UniProt

site_id	PS00164
Number of Residues	14
Details	ENOLASE Enolase signature. ILIKvNQIGTLTET

Chain	Residue	Details
B	ILE341-THR354

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	ACT_SITE: Proton donor => ECO:0000255\|HAMAP-Rule:MF_00318

site_id	SWS_FT_FI2
Number of Residues	2
Details	ACT_SITE: Proton acceptor => ECO:0000255\|HAMAP-Rule:MF_00318

site_id	SWS_FT_FI3
Number of Residues	14
Details	BINDING: BINDING => ECO:0000255\|HAMAP-Rule:MF_00318

site_id	SWS_FT_FI4
Number of Residues	2
Details	BINDING: covalent; in inhibited form => ECO:0000255\|HAMAP-Rule:MF_00318