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7E2Q

Crystal structure of Mycoplasma pneumoniae Enolase

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
A0005829cellular_componentcytosol
A0006096biological_processglycolytic process
A0009986cellular_componentcell surface
A0016829molecular_functionlyase activity
A0046872molecular_functionmetal ion binding
B0000015cellular_componentphosphopyruvate hydratase complex
B0000287molecular_functionmagnesium ion binding
B0004634molecular_functionphosphopyruvate hydratase activity
B0005515molecular_functionprotein binding
B0005576cellular_componentextracellular region
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0006096biological_processglycolytic process
B0009986cellular_componentcell surface
B0016829molecular_functionlyase activity
B0046872molecular_functionmetal ion binding
C0000015cellular_componentphosphopyruvate hydratase complex
C0000287molecular_functionmagnesium ion binding
C0004634molecular_functionphosphopyruvate hydratase activity
C0005515molecular_functionprotein binding
C0005576cellular_componentextracellular region
C0005737cellular_componentcytoplasm
C0005829cellular_componentcytosol
C0006096biological_processglycolytic process
C0009986cellular_componentcell surface
C0016829molecular_functionlyase activity
C0046872molecular_functionmetal ion binding
D0000015cellular_componentphosphopyruvate hydratase complex
D0000287molecular_functionmagnesium ion binding
D0004634molecular_functionphosphopyruvate hydratase activity
D0005515molecular_functionprotein binding
D0005576cellular_componentextracellular region
D0005737cellular_componentcytoplasm
D0005829cellular_componentcytosol
D0006096biological_processglycolytic process
D0009986cellular_componentcell surface
D0016829molecular_functionlyase activity
D0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues5
Detailsbinding site for residue SO4 A 501
ChainResidue
AGLY48
AALA49
ALYS362
AARG391
ASER392

site_idAC2
Number of Residues5
Detailsbinding site for residue SO4 B 501
ChainResidue
BHOH729
BGLY48
BLYS362
BARG391
BSER392

site_idAC3
Number of Residues6
Detailsbinding site for residue SO4 C 501
ChainResidue
CGLY48
CALA49
CLYS362
CARG391
CSER392
CHOH602

site_idAC4
Number of Residues5
Detailsbinding site for residue SO4 D 501
ChainResidue
DGLY48
DALA49
DLYS362
DARG391
DSER392

Functional Information from PROSITE/UniProt
site_idPS00164
Number of Residues14
DetailsENOLASE Enolase signature. ILIKlNQIGTLTET
ChainResidueDetails
AILE359-THR372

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsACT_SITE: Proton donor => ECO:0000255|HAMAP-Rule:MF_00318
ChainResidueDetails
AGLU219
BGLU219
CGLU219
DGLU219

site_idSWS_FT_FI2
Number of Residues4
DetailsACT_SITE: Proton acceptor => ECO:0000255|HAMAP-Rule:MF_00318
ChainResidueDetails
ALYS362
BLYS362
CLYS362
DLYS362

site_idSWS_FT_FI3
Number of Residues28
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00318
ChainResidueDetails
AHIS169
BASP256
BGLU310
BASP337
BSER389
BLYS413
CHIS169
CGLU178
CASP256
CGLU310
CASP337
AGLU178
CSER389
CLYS413
DHIS169
DGLU178
DASP256
DGLU310
DASP337
DSER389
DLYS413
AASP256
AGLU310
AASP337
ASER389
ALYS413
BHIS169
BGLU178

site_idSWS_FT_FI4
Number of Residues4
DetailsBINDING: covalent; in inhibited form => ECO:0000255|HAMAP-Rule:MF_00318
ChainResidueDetails
ALYS362
BLYS362
CLYS362
DLYS362

220113

PDB entries from 2024-05-22

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