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2PU1

Crystal Structure of the T. brucei enolase complexed with Fluoro-phosphonoacetohydroxamate (FPAH)

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
AASP318
AFSG600
AHOH759

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 501
ChainResidue
ASER40
AFSG600
AHOH727
AHOH817

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 550
ChainResidue
AHIS0
AGLU27
AHIS283
AHOH1042

site_idAC4
Number of Residues20
DetailsBINDING SITE FOR RESIDUE FSG A 600
ChainResidue
AGLY38
AALA39
ASER40
AGLN164
AGLU165
AGLU208
AASP243
AGLU291
AASP318
ALEU341
ALYS343
AARG372
ASER373
ALYS394
AZN500
AZN501
AHOH722
AHOH727
AHOH760
AHOH817

site_idAC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE EDO A 700
ChainResidue
AARG32
ATYR129
AGLN409
AGLU416
AHOH738
AHOH782

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

226707

PDB entries from 2024-10-30

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