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8UOP

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

Functional Information from GO Data
ChainGOidnamespacecontents
A0000015cellular_componentphosphopyruvate hydratase complex
A0000287molecular_functionmagnesium ion binding
A0004634molecular_functionphosphopyruvate hydratase activity
A0005576cellular_componentextracellular region
A0005737cellular_componentcytoplasm
A0006096biological_processglycolytic process
A0009274cellular_componentpeptidoglycan-based cell wall
A0009986cellular_componentcell surface
A0016829molecular_functionlyase activity
A0046872molecular_functionmetal ion binding
B0000015cellular_componentphosphopyruvate hydratase complex
B0000287molecular_functionmagnesium ion binding
B0004634molecular_functionphosphopyruvate hydratase activity
B0005576cellular_componentextracellular region
B0005737cellular_componentcytoplasm
B0006096biological_processglycolytic process
B0009274cellular_componentpeptidoglycan-based cell wall
B0009986cellular_componentcell surface
B0016829molecular_functionlyase activity
B0046872molecular_functionmetal ion binding
Functional Information from PROSITE/UniProt
site_idPS00164
Number of Residues14
DetailsENOLASE Enolase signature. ILIKvNQIGTLTET
ChainResidueDetails
AILE341-THR354

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton donor => ECO:0000255|HAMAP-Rule:MF_00318
ChainResidueDetails
AGLU205
BGLU205

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: Proton acceptor => ECO:0000255|HAMAP-Rule:MF_00318
ChainResidueDetails
ALYS344
BLYS344

site_idSWS_FT_FI3
Number of Residues14
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00318
ChainResidueDetails
AHIS155
BASP243
BGLU292
BASP319
BSER371
BLYS395
AGLU164
AASP243
AGLU292
AASP319
ASER371
ALYS395
BHIS155
BGLU164

site_idSWS_FT_FI4
Number of Residues2
DetailsBINDING: covalent; in inhibited form => ECO:0000255|HAMAP-Rule:MF_00318
ChainResidueDetails
ALYS344
BLYS344

223166

PDB entries from 2024-07-31

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