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1IYX

Crystal structure of enolase from Enterococcus hirae

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
B0000015cellular_componentphosphopyruvate hydratase complex
B0000287molecular_functionmagnesium ion binding
B0004634molecular_functionphosphopyruvate hydratase activity
B0005576cellular_componentextracellular region
B0005737cellular_componentcytoplasm
B0006096biological_processglycolytic process
B0009986cellular_componentcell surface
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE MG A 1432
ChainResidue
AGLN162
AASP241
AGLU287
ALYS390

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MG B 1432
ChainResidue
BASP241
BGLU287
BASP288
BASP314
BHOH2084

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 B 1001
ChainResidue
BGLY39
BALA40
BLYS339
BARG368
BSER369

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 A 1002
ChainResidue
ALYS339
AARG368
ASER369
AHOH2032
AHOH2087

site_idAC5
Number of Residues3
DetailsBINDING SITE FOR RESIDUE GOL A 2001
ChainResidue
AASP411
AHOH2057
BTYR7

site_idAC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE GOL A 2002
ChainResidue
AASP5
ATYR7
ATYR25
AHOH2070

site_idAC7
Number of Residues2
DetailsBINDING SITE FOR RESIDUE GOL A 2003
ChainResidue
AALA77
AILE79

site_idAC8
Number of Residues3
DetailsBINDING SITE FOR RESIDUE GOL B 2004
ChainResidue
BALA77
BILE79
BTYR81

site_idAC9
Number of Residues3
DetailsBINDING SITE FOR RESIDUE GOL A 2005
ChainResidue
AMET87
AGLU348
AGLU351

site_idBC1
Number of Residues8
DetailsBINDING SITE FOR RESIDUE GOL B 2006
ChainResidue
ALEU125
AHIS131
ATYR132
AHOH2084
BLEU125
BHIS131
BGLY135
BHOH2083

Functional Information from PROSITE/UniProt
site_idPS00164
Number of Residues14
DetailsENOLASE Enolase signature. ILIKvNQIGTLTET
ChainResidueDetails
AILE336-THR349

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 Residues10
DetailsBinding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00318","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues6
DetailsBinding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00318","evidenceCode":"ECO:0000255"},{"source":"PDB","id":"1IYX","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues4
DetailsAnnotated By Reference To The Literature 1els
ChainResidueDetails
AGLU204
ALYS390
AHIS367
AGLU163

site_idCSA2
Number of Residues4
DetailsAnnotated By Reference To The Literature 1els
ChainResidueDetails
BGLU204
BLYS390
BHIS367
BGLU163

site_idCSA3
Number of Residues4
DetailsAnnotated By Reference To The Literature 1els
ChainResidueDetails
AGLU204
ALYS339
AHIS367
AGLU163

site_idCSA4
Number of Residues4
DetailsAnnotated By Reference To The Literature 1els
ChainResidueDetails
BGLU204
BLYS339
BHIS367
BGLU163

251174

PDB entries from 2026-03-25

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