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3TQP

Structure of an enolase (eno) from Coxiella burnetii

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
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
B0009986cellular_componentcell surface
B0016829molecular_functionlyase activity
B0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE PO4 B 429
ChainResidue
BLYS337
BARG366
BSER367

site_idAC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE PO4 A 429
ChainResidue
AHOH558
AGLY41
AALA42
ALYS337
AARG366
ASER367
AHOH556

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG B 430
ChainResidue
BASP244
BGLU285
BASP312
BHOH464
BHOH480
BHOH495

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG A 430
ChainResidue
AASP244
AGLU285
AASP312
AHOH549
AHOH556
AHOH558

Functional Information from PROSITE/UniProt
site_idPS00164
Number of Residues14
DetailsENOLASE Enolase signature. ILVKlNQIGTLTET
ChainResidueDetails
AILE334-THR347

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton donor => ECO:0000255|HAMAP-Rule:MF_00318
ChainResidueDetails
AGLU207
BGLU207

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: Proton acceptor => ECO:0000255|HAMAP-Rule:MF_00318
ChainResidueDetails
ALYS337
BLYS337

site_idSWS_FT_FI3
Number of Residues10
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00318
ChainResidueDetails
AGLN165
BLYS388
ALYS337
AARG366
ASER367
ALYS388
BGLN165
BLYS337
BARG366
BSER367

site_idSWS_FT_FI4
Number of Residues6
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00318, ECO:0000269|PubMed:26033498, ECO:0007744|PDB:3TQP
ChainResidueDetails
AASP312
BASP244
BGLU285
BASP312
AASP244
AGLU285

221051

PDB entries from 2024-06-12

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