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1OEP

Structure of Trypanosoma brucei enolase reveals the inhibitory divalent metal site

Functional Information from GO Data
ChainGOidnamespacecontents
A0000015cellular_componentphosphopyruvate hydratase complex
A0000287molecular_functionmagnesium ion binding
A0004634molecular_functionphosphopyruvate hydratase activity
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006096biological_processglycolytic process
A0016829molecular_functionlyase activity
A0046872molecular_functionmetal ion binding
A0097014cellular_componentciliary plasm
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN A 500
ChainResidue
AASP243
AGLU291
AASP292
AASP318
AHOH2234

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 501
ChainResidue
AHIS156
AGLN164
AGLU165
AGLU208

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 A 600
ChainResidue
AGLY38
ALYS343
AARG372
ASER373
AHOH2234
AHOH2235

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE EDO A 700
ChainResidue
AARG32
ATYR129
AGLN409
AGLU416
AHOH2236

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE EDO A 701
ChainResidue
AGLU10
ASER177
ALEU411
AGLU414
AGLU415

site_idAC6
Number of Residues6
DetailsBINDING SITE FOR RESIDUE EDO A 702
ChainResidue
AARG130
ALYS139
AGLU140
ALEU141
AHOH2238
AHOH2239

Functional Information from PROSITE/UniProt
site_idPS00164
Number of Residues14
DetailsENOLASE Enolase signature. LLLKiNQIGTISEA
ChainResidueDetails
ALEU340-ALA353

Catalytic Information from CSA
site_idCSA1
Number of Residues4
DetailsAnnotated By Reference To The Literature 1els
ChainResidueDetails
AGLU208
AGLU165
AHIS371
ALYS394

site_idCSA2
Number of Residues4
DetailsAnnotated By Reference To The Literature 1els
ChainResidueDetails
AGLU208
ALYS343
AGLU165
AHIS371

site_idCSA3
Number of Residues2
DetailsAnnotated By Reference To The Literature 1els
ChainResidueDetails
ALYS343
AHIS188

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PDB entries from 2025-12-17

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