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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
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 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
DetailsACT_SITE: Proton donor => ECO:0000255|HAMAP-Rule:MF_00318
ChainResidueDetails
AGLU204
BGLU204

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: Proton acceptor => ECO:0000255|HAMAP-Rule:MF_00318
ChainResidueDetails
ALYS339
BLYS339

site_idSWS_FT_FI3
Number of Residues12
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00318
ChainResidueDetails
AHIS154
BASP314
BSER366
BLYS390
AGLU163
AGLU287
AASP314
ASER366
ALYS390
BHIS154
BGLU163
BGLU287

site_idSWS_FT_FI4
Number of Residues2
DetailsBINDING:
ChainResidueDetails
AASP241
BASP241

site_idSWS_FT_FI5
Number of Residues2
DetailsBINDING: covalent; in inhibited form => ECO:0000255|HAMAP-Rule:MF_00318
ChainResidueDetails
ALYS339
BLYS339

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PDB entries from 2024-04-24

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