Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

5BOE

Crystal structure of Staphylococcus aureus enolase in complex with PEP

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 Residues13
Detailsbinding site for residue PEP A 501
ChainResidue
AGLY40
ALYS394
AMG502
AHOH687
AHOH747
AALA41
ASER42
AASP244
AASP318
ALYS343
AHIS371
AARG372
ASER373

site_idAC2
Number of Residues6
Detailsbinding site for residue MG A 502
ChainResidue
AASP244
AGLU291
AASP318
APEP501
AHOH686
AHOH687

site_idAC3
Number of Residues8
Detailsbinding site for residue GOL A 503
ChainResidue
ATYR133
AGLN409
AGLU416
AHOH684
AHOH710
AHOH733
BARG34
BHOH651

site_idAC4
Number of Residues13
Detailsbinding site for residue PEP B 501
ChainResidue
BGLY40
BALA41
BSER42
BASP244
BASP318
BLYS343
BHIS371
BARG372
BSER373
BLYS394
BMG502
BHOH724
BHOH748

site_idAC5
Number of Residues6
Detailsbinding site for residue MG B 502
ChainResidue
BASP244
BGLU291
BASP318
BPEP501
BHOH644
BHOH724

site_idAC6
Number of Residues8
Detailsbinding site for residue GOL B 503
ChainResidue
AARG34
AHOH636
BTYR133
BGLN409
BGLU416
BHOH671
BHOH700
BHOH709

site_idAC7
Number of Residues9
Detailsbinding site for residue GOL B 504
ChainResidue
AASP88
ASER91
AHOH835
BLYS134
BGLU416
BLEU417
BPHE418
BGLU419
BHOH722

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 Residues14
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00318
ChainResidueDetails
AHIS157
BASP244
BGLU291
BASP318
BSER370
BLYS394
AGLU166
AASP244
AGLU291
AASP318
ASER370
ALYS394
BHIS157
BGLU166

site_idSWS_FT_FI4
Number of Residues2
DetailsBINDING: covalent; in inhibited form => ECO:0000255|HAMAP-Rule:MF_00318
ChainResidueDetails
ALYS343
BLYS343

218853

PDB entries from 2024-04-24

PDB statisticsPDBj update infoContact PDBjnumon