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5BOF

Crystal Structure of Staphylococcus aureus Enolase

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 MG A 501
ChainResidue
AASP244
AGLU291
AASP318

site_idAC2
Number of Residues3
Detailsbinding site for residue SO4 A 502
ChainResidue
ALYS343
AARG372
ASER373

site_idAC3
Number of Residues4
Detailsbinding site for residue SO4 A 503
ChainResidue
BARG58
ALYS178
AGLU179
AARG182

site_idAC4
Number of Residues4
Detailsbinding site for residue SO4 A 504
ChainResidue
AARG16
AASN18
BHIS189
BLYS192

site_idAC5
Number of Residues4
Detailsbinding site for residue SO4 B 501
ChainResidue
AHIS189
ALYS192
BARG16
BASN18

site_idAC6
Number of Residues3
Detailsbinding site for residue SO4 B 502
ChainResidue
AARG58
BGLU179
BARG182

site_idAC7
Number of Residues3
Detailsbinding site for residue MG B 503
ChainResidue
BASP244
BGLU291
BASP318

site_idAC8
Number of Residues3
Detailsbinding site for residue SO4 B 504
ChainResidue
BLYS343
BARG372
BSER373

Functional Information from PROSITE/UniProt
site_idPS00164
Number of Residues14
DetailsENOLASE Enolase signature. ILIKvNQIGTLTET
ChainResidueDetails
AILE340-THR353

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
ALYS343
BLYS343

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING: BINDING => ECO:0007744|PDB:5BOE
ChainResidueDetails
AALA41
BALA41

site_idSWS_FT_FI4
Number of Residues2
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00318
ChainResidueDetails
AGLN165
BGLN165

site_idSWS_FT_FI5
Number of Residues6
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00318, ECO:0000269|PubMed:26627653, ECO:0007744|PDB:5BOE, ECO:0007744|PDB:5BOF
ChainResidueDetails
AASP244
AGLU291
AASP318
BASP244
BGLU291
BASP318

site_idSWS_FT_FI6
Number of Residues8
DetailsBINDING: BINDING => ECO:0000269|PubMed:26627653, ECO:0007744|PDB:5BOE
ChainResidueDetails
ALYS343
AARG372
ASER373
ALYS394
BLYS343
BARG372
BSER373
BLYS394

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PDB entries from 2024-10-30

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