Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
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
DetailsActive site: {"description":"Proton donor","evidences":[{"source":"HAMAP-Rule","id":"MF_00318","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues2
DetailsActive site: {"description":"Proton acceptor","evidences":[{"source":"HAMAP-Rule","id":"MF_00318","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues2
DetailsBinding site: {"evidences":[{"source":"PDB","id":"5BOE","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues2
DetailsBinding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00318","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues6
DetailsBinding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00318","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"26627653","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5BOE","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5BOF","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues8
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"26627653","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5BOE","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

247536

PDB entries from 2026-01-14

PDB statisticsPDBj update infoContact PDBjnumon