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Cryo-EM structure of PEIP-Bs_enolase complex

Functional Information from GO Data
ChainGOidnamespacecontents
A0000015cellular_componentphosphopyruvate hydratase complex
A0000287molecular_functionmagnesium ion binding
A0004634molecular_functionphosphopyruvate hydratase activity
A0005515molecular_functionprotein binding
A0005576cellular_componentextracellular region
A0005737cellular_componentcytoplasm
A0006096biological_processglycolytic process
A0009986cellular_componentcell surface
A0016829molecular_functionlyase activity
A0030435biological_processsporulation resulting in formation of a cellular spore
A0046872molecular_functionmetal ion binding
B0000015cellular_componentphosphopyruvate hydratase complex
B0000287molecular_functionmagnesium ion binding
B0004634molecular_functionphosphopyruvate hydratase activity
B0005515molecular_functionprotein binding
B0005576cellular_componentextracellular region
B0005737cellular_componentcytoplasm
B0006096biological_processglycolytic process
B0009986cellular_componentcell surface
B0016829molecular_functionlyase activity
B0030435biological_processsporulation resulting in formation of a cellular spore
B0046872molecular_functionmetal ion binding
Functional Information from PROSITE/UniProt
site_idPS00164
Number of Residues14
DetailsENOLASE Enolase signature. ILIKvNQIGTLTET
ChainResidueDetails
AILE336-THR349

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
ALYS339
BLYS339

site_idSWS_FT_FI3
Number of Residues16
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00318
ChainResidueDetails
AGLN163
BASP242
BGLU287
BASP314
BLYS339
BARG368
BSER369
BLYS390
AASP242
AGLU287
AASP314
ALYS339
AARG368
ASER369
ALYS390
BGLN163

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: Phosphothreonine => ECO:0000269|PubMed:17218307
ChainResidueDetails
ATHR141
BTHR141

site_idSWS_FT_FI5
Number of Residues4
DetailsMOD_RES: Phosphoserine => ECO:0000269|PubMed:17218307
ChainResidueDetails
ASER259
ASER325
BSER259
BSER325

site_idSWS_FT_FI6
Number of Residues2
DetailsMOD_RES: Phosphotyrosine => ECO:0000269|PubMed:17218307
ChainResidueDetails
ATYR281
BTYR281

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PDB entries from 2024-07-24

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