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2PTY

Crystal Structure of the T. brucei enolase complexed with PEP

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
APEP600
AHOH745

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 501
ChainResidue
ASER40
APEP600
AHOH738
AHOH775

site_idAC3
Number of Residues18
DetailsBINDING SITE FOR RESIDUE PEP A 600
ChainResidue
AGLY38
AALA39
ASER40
AHIS156
AGLN164
AGLU165
AGLU208
AASP243
AGLU291
AASP318
ALEU341
ALYS343
AARG372
ASER373
ALYS394
AZN500
AZN501
AHOH775

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE EDO A 700
ChainResidue
AARG32
ATYR129
AGLN409
AGLU416
AHOH717
AHOH751

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

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PDB entries from 2024-06-12

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